LOCUS       NP_899044               4981 aa            linear   ROD 14-JUN-2024
DEFINITION  protocadherin Fat 4 precursor [Mus musculus].
ACCESSION   NP_899044 XP_006535547 XP_619892 XP_896333
VERSION     NP_899044.3
DBSOURCE    REFSEQ: accession NM_183221.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 4981)
  AUTHORS   Wang,D., Wu,S., He,J., Sun,L., Zhu,H., Zhang,Y., Liu,S., Duan,X.,
            Wang,Y. and Xu,T.
  TITLE     FAT4 overexpression promotes antitumor immunity by regulating the
            beta-catenin/STT3/PD-L1 axis in cervical cancer
  JOURNAL   J Exp Clin Cancer Res 42 (1), 222 (2023)
   PUBMED   37658376
  REMARK    GeneRIF: FAT4 overexpression promotes antitumor immunity by
            regulating the beta-catenin/STT3/PD-L1 axis in cervical cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4981)
  AUTHORS   Zhang,C.H., Gao,Y., Hung,H.H., Zhuo,Z., Grodzinsky,A.J. and
            Lassar,A.B.
  TITLE     Creb5 coordinates synovial joint formation with the genesis of
            articular cartilage
  JOURNAL   Nat Commun 13 (1), 7295 (2022)
   PUBMED   36435829
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4981)
  AUTHORS   Wu,Y., Zhou,Y., Huang,J., Ma,K., Yuan,T., Jiang,Y., Ye,M. and Li,J.
  TITLE     The Role of Sorting Nexin 17 in Cardiac Development
  JOURNAL   Front Cardiovasc Med 8, 748891 (2021)
   PUBMED   34988124
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 4981)
  AUTHORS   Weiss,A.C., Rivera-Reyes,R., Englert,C. and Kispert,A.
  TITLE     Expansion of the renal capsular stroma, ureteric bud branching
            defects and cryptorchidism in mice with Wilms tumor 1 gene deletion
            in the stromal compartment of the developing kidney
  JOURNAL   J Pathol 252 (3), 290-303 (2020)
   PUBMED   32715478
REFERENCE   5  (residues 1 to 4981)
  AUTHORS   Lodge,E.J., Xekouki,P., Silva,T.S., Kochi,C., Longui,C.A.,
            Faucz,F.R., Santambrogio,A., Mills,J.L., Pankratz,N., Lane,J.,
            Sosnowska,D., Hodgson,T., Patist,A.L., Francis-West,P.,
            Helmbacher,F., Stratakis,C. and Andoniadou,C.L.
  TITLE     Requirement of FAT and DCHS protocadherins during
            hypothalamic-pituitary development
  JOURNAL   JCI Insight 5 (23), 134310 (2020)
   PUBMED   33108146
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 4981)
  AUTHORS   Mao,Y., Mulvaney,J., Zakaria,S., Yu,T., Morgan,K.M., Allen,S.,
            Basson,M.A., Francis-West,P. and Irvine,K.D.
  TITLE     Characterization of a Dchs1 mutant mouse reveals requirements for
            Dchs1-Fat4 signaling during mammalian development
  JOURNAL   Development 138 (5), 947-957 (2011)
   PUBMED   21303848
  REMARK    GeneRIF: Dchs1 and Fat4 function as a ligand-receptor pair during
            murine development, and novel requirements for Dchs1-Fat4
REFERENCE   7  (residues 1 to 4981)
  AUTHORS   Ishiuchi,T., Misaki,K., Yonemura,S., Takeichi,M. and Tanoue,T.
  TITLE     Mammalian Fat and Dachsous cadherins regulate apical membrane
            organization in the embryonic cerebral cortex
  JOURNAL   J Cell Biol 185 (6), 959-967 (2009)
   PUBMED   19506035
  REMARK    GeneRIF: Results highlight the importance of the
            Fat4-Dachsous1-Pals1 complex in organizing the apical membrane
            architecture of neural progenitor cells.
REFERENCE   8  (residues 1 to 4981)
  AUTHORS   Qi,C., Zhu,Y.T., Hu,L. and Zhu,Y.J.
  TITLE     Identification of Fat4 as a candidate tumor suppressor gene in
            breast cancers
  JOURNAL   Int J Cancer 124 (4), 793-798 (2009)
   PUBMED   19048595
  REMARK    GeneRIF: Fat4 may be a breast tumor suppressor gene
REFERENCE   9  (residues 1 to 4981)
  AUTHORS   Saburi,S., Hester,I., Fischer,E., Pontoglio,M., Eremina,V.,
            Gessler,M., Quaggin,S.E., Harrison,R., Mount,R. and McNeill,H.
  TITLE     Loss of Fat4 disrupts PCP signaling and oriented cell division and
            leads to cystic kidney disease
  JOURNAL   Nat Genet 40 (8), 1010-1015 (2008)
   PUBMED   18604206
  REMARK    GeneRIF: Study shows that Fat4 is an essential gene that has a key
            role in vertebrate core planar cell polarity; loss of Fat4 disrupts
            oriented cell divisions and tubule elongation during kidney
            development, leading to cystic kidney disease.
REFERENCE   10 (residues 1 to 4981)
  AUTHORS   Rock,R., Schrauth,S. and Gessler,M.
  TITLE     Expression of mouse dchs1, fjx1, and fat-j suggests conservation of
            the planar cell polarity pathway identified in Drosophila
  JOURNAL   Dev Dyn 234 (3), 747-755 (2005)
   PUBMED   16059920
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC161228.7 and AC122841.4.
            
            On or before Dec 20, 2022 this sequence version replaced
            XP_006535547.1, NP_899044.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14777535.1238131.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN00849374, SAMN00849380 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4981
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 18.72 cM"
     Protein         1..4981
                     /product="protocadherin Fat 4 precursor"
                     /note="protocadherin Fat 4; fat-like cadherin protein
                     FAT-J; FAT tumor suppressor homolog 4"
                     /calculated_mol_wt=535786
     sig_peptide     1..42
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
                     /calculated_mol_wt=4550
     mat_peptide     43..4981
                     /product="Protocadherin Fat 4. /id=PRO_0000324638"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
                     /calculated_mol_wt=535786
     Region          48..131
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(53..54,97,99,127,129..130)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          139..246
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(146..147,209,211,242,244..245)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          254..349
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(261..262,312,314,345,347..348)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          364..471
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(369..370,427,429,467,469..470)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          479..577
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            483
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            order(486..487,541,543,574,576..577)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          588..685
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(594..595,648,650,681,683..684)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            615
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            676
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          693..789
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(700..701,752,754,785,787..788)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          798..889
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(804..805,855,857,885,887..888)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            825
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            880
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          904..992
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(904..905,956,958,988,990..991)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1000..1096
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1007..1008,1059,1061,1092,1094..1095)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1085
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            1101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            1104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1105..1206
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1111..1112,1162,1164,1202,1204..1205)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1215..1311
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1221..1222,1274,1276,1307,1309..1310)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1225
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            1296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1321..1416
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1326..1327,1379,1381,1412,1414..1415)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1428..1525
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1431..1432,1485,1487,1521,1523..1524)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1540..1622
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          1634..1736
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1640..1641,1697,1699,1732,1734..1735)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1747..1837
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1751..1752,1803,1805,1833,1835..1836)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1828
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1845..1940
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1852..1853,1905,1907,1936,1938..1939)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1899
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          1948..2047
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1955..1956,2007,2009,2043,2045..2046)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1967
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          2057..2150
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2061..2062,2113,2115,2146,2148..2149)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          2159..2254
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2165..2166,2218,2220,2251,2253..2254)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2263..2360
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2270..2271,2323,2325,2356,2358..2359)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2369..2464
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2375..2376,2426,2428,2460,2462..2463)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            2432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          2472..2559
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          2573..2667
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2580..2581,2630,2632,2663,2665..2666)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2675..2771
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2682..2683,2734,2736,2767,2769..2770)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2778..2870
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2785..2786,2836,2838,2866,2868..2869)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2878..2981
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2885..2886,2936,2938,2977,2979..2980)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2923
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            2939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          2990..3085
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2996..2997,3050,3052,3083,3085)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3038
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3095..3192
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3102..3103,3155,3157,3188,3190..3191)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3200..3295
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3207..3208,3259,3261,3292,3294..3295)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3305..3402
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3311..3312,3364,3366,3399,3401..3402)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3394
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3410..3508
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3417..3418,3471,3473,3504,3506..3507)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3516..3612
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3521..3522,3575,3577,3608,3610..3611)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3708
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            3760
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          3804..3862
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(3804,3807,3821)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          3864..3900
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(3864,3867,3881)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          3902..3938
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(3902,3905,3919)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          3941..3976
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3979..4142
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            4019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4168..4200
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          4252..4375
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            4269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            4314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4430..4464
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            4506..4526
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4535..4585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4677..4713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4708..4797
                     /region_name="Necessary and sufficient for interaction
                     with MPDZ. /evidence=ECO:0000269|PubMed:19506035"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4753..4773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4796..4911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Site            4878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747; propagated from
                     UniProtKB/Swiss-Prot (Q2PZL6.2)"
     Region          4957..4981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2PZL6.2)"
     CDS             1..4981
                     /gene="Fat4"
                     /gene_synonym="6030410K14Rik; 9430004M15"
                     /coded_by="NM_183221.4:880..15825"
                     /db_xref="CCDS:CCDS17325.1"
                     /db_xref="GeneID:329628"
                     /db_xref="MGI:MGI:3045256"
ORIGIN      
        1 mnlaanrapg rrrlplpsps lcqllrvwgl lsllpgsarv qaaeqrqvfq vmeeqppgtl
       61 vgtiptrpgf tyrlseshal fainsstgal yttatidres lpsdvvnlvv lsssptypte
      121 vrvlvrdlnd napvfpdpsi vvtfkedsgs grqvildtat dsdigsngvd hhsyrivsgn
      181 eagrfrldit lnpsgegafl hlvskggldr evtpqyqllv evedkgepkr rgylqvnvtv
      241 qdindnppvf gsshyqagvp edavvgssvl qvaaadadeg tnadiryrlq degtpfqmdp
      301 etglitvrep ldfearrqys ltvqatdrgv psltgraeaf iqlldvndnd pvvkfryfpa
      361 tsryasvden aqvgtvvall tvtdadspaa ngnisvqilg gneqrhfevq rskvpnlsli
      421 kvasaldrer ipsynltvsv sdnsgappta evqarssvas lvifvndind hppvfeqqvy
      481 rvnlseevpp gsyvsgvsat dgdsglnanl rysivsgngl gwfhisehsg lvttsaaggl
      541 drelasqivl nisardqgvh pkvsyaqlvv tvldvndekp vfsqpegyev svvenaptgt
      601 ellvlgatdr dlgdngtvrf slqeaendqr lfrldpvsgr lstassldre eqafyclsil
      661 atdlgsppqs staqvnvsll dindnspvfy pvqyfahiqe nepggsyvtt vsatdpdmgp
      721 ngtvkysisa gdrsrfqiha ksgvistkma ldreektayq lqvvatdggn lqspnqaivt
      781 vtvldtqdnp pvfsqaaysf vvfenvalgy hvgsvsattm dlnanisyli ttgdqrgmfa
      841 mnpvtgqltt asvidreeqs fyqlkivasg gavtgdtvvn itvkdlndna phflqavesi
      901 navenwqagh sifqakavdp degvngrvly slkqnpknlf tineqngnis llgaldvhag
      961 syqveivasd mgvpqlsssi lltvyvhdvn dnppvfdqis yevtlsesep vnsrffkvqa
     1021 sdkdsgange iaytitdgnn gdafgifpdg qlyikseldr elqdryvllv vasdravepl
     1081 satvnvtvll edvndnrplf nstnytfyfe eeqragsfvg kvsavdkdfg pngevryafe
     1141 vtqpnfelha vtgeitsthk fdreslmrrr gtavfsftvt amdrglpqpl kdqatvhvym
     1201 kdindnapkf lkdfyqatvs etatnltqvl rvsasdvdeg snglihysil kgneerqfai
     1261 dsfsgqvtlv gkldyeatsa yslliqavds gaiplnstct lsidildend ntpsfpkstl
     1321 fvdvlenmri gelvssvtat dsdsgvnadl hytitgsnnh gtfsispntg siflakkldf
     1381 etqslyklni takdqgrppr sstmsvviqv rdfndnppsf ppgdifksiv eniplgtsvi
     1441 svtahdpdad ingqlsyaii qqmprgnhfs idevkgtiyt saeidrefan lfeltvkand
     1501 qavpietrry alknvtilvt dlndnvpmfi sqnalaadps amigsvltti maadpdegan
     1561 geveyeilng dtdtftvdry sgdlrvasal vpsqliynli vsatdlgper rkstteltvi
     1621 lqgldgpvft qtkyitilke gepigtnvis ieaasprgse apveyyivsv rceektvgrl
     1681 ftigrqtgvi qtaaildreq gaclylvdvy aiekssafpr tqraeveitl qdindnppvf
     1741 ptdtldltve enigdgskim qltamdadeg analvtyali sgaddsfrid pesgdliatk
     1801 rldrehrsky sllvraddgl qssdmrinit isdvndhtpr fsrpvysfdi pedttpgslv
     1861 aailatddds gvngeisyvv eeddgdgvff lnlvtgvfnl traldyetqq yyiltvraed
     1921 gggqsttira yfnildvndn ppvfsmssys tslmenlplg stvlvfnvtd addgvnsqls
     1981 ysiasgdslg qfavdkhgvl ktlkaldres qsfynlviqv hdlpqpptsr ftstaqvsii
     2041 lldvndnppm flspkltyip entpidtvvf kaqatdpdsg pnsyieytll npsgnkfsig
     2101 tidgevhltg eldreevsny sltvvatdkg qpplssstev vvmvldindn npvfaqamyr
     2161 vqikeniltg tdiiqvsaad ndegtngqvr ygivggnthq efridsvtga itvaksldre
     2221 ttpaytltvq atdrgssprt dsctvaitll dmndfvpvfe lspysvnvpe nlgtlprail
     2281 qvvardddqg pnsqlsyvll ggnednafvl tasgelrvtq sldreardhf vlvvtaadag
     2341 spaltgtgti niivddindn vptfannmyl tsiaedartg tdvllvnasd adaaanavis
     2401 ysiiggnsqf tinpstgqii tsalldretk dnytlvvvas dagspeslss stsvlvtitd
     2461 vndnpprfqh hpyvthipsp tppgsfvfav tvtdadigsn selhyslsgr nsekfhidpl
     2521 rgaimaagpl sgasevtfsv hvkdggsfpk tdsttvtvrf ankadfpkvr akeqtfmfpe
     2581 nqpvgtlvtt itgsslrget lsyyiasgnl gdtfqidplt gqvsisqpld fekiqkyvvw
     2641 ieardggfpp fssyekldit vldindnapt feedpfvsei lenlsprkil tvsatdkdsg
     2701 pngqldyeiv ngnqessfti nhatgeirsi rpldrekish yeltvkssdk gspsqstsvk
     2761 viisildend naprfsqifs ayvsensplg ytvtrvttsd ediginaisr ysivdtslpf
     2821 tinpntgdiv isrplnredt dryrirvsah dsgwtvstdv tifvtdindn tprfsrpsyy
     2881 ldcpelpelg srvtqvsatd pdegsngqvf yfiksqseyf rinattgeif nkqvlkyqnv
     2941 sgfsnvninr hsfivtasdr gnpsllsett vtintvdsnd nppqflqnky ftpvtknvkv
     3001 gtklikvtav ddkdfglnse veyfvsdgnh lgkfkldndt gwisiasslv sdlnqnflir
     3061 vtakdkgnpp lssqavvhit vteenyhtpe fsqnhisati peshsigsvv rtvsardrdt
     3121 amnglisyni isgneegifa insstgvvtl akaldyemss khemtisatd ggwvartgyc
     3181 sltvsvidvn dnspvfvpde ffptvmenap sgttvihlna tdadsganav iaytvqssds
     3241 dlfvidpnmg vittqgfldf etkqsyhltv kafnvpdeek csfatvdiql kgtneyvprf
     3301 vsklyyfevs eaasrgtavg evfasdrdmg adgevhylif gnsrkkgfqi nkmtgqiyvs
     3361 glldrekeer vslkvlaknf gnirgadide vtvnitvlda ndppvfslst yrvqisegvp
     3421 igthvtfvsa fdsdsipsws rfsyfigsgn engafsinpq tgqitvtsgl dreslpvynl
     3481 tvlavdsgtp satgsaslvv tledindngp vltvsegevl enkrpgtlvm tlqstdpdlp
     3541 pnqgpfnyyl lstgpatnyf slstagvlst treidreqia dfylsvvtrd sgapqmsstg
     3601 tvhitvldqn dnpsqsrtve ifvnyygnlf pggtlgsvkp qdpdvldsfh csltsgvtsl
     3661 fsipagscdl ssqprstdgt fdltvvssdg vhstvtnnir vffagfsnat idnsillrvg
     3721 vptvkdfltn hylhflrias sqltglgtav qlyaayeenn rtfllaavkr nnnqyvnpsg
     3781 vatffesike illrqsgvkv esvdhdpcih gpcqnggscl rrlavgsalk iqeslpviiv
     3841 aneplqpsqc kcvpgyagsw cevdideclp apchnggtch nlvggfscsc pegftgrace
     3901 rdineclpsp ckhgavcqnf pggfncvckt gytgkmcess vnycecnpcf nggscqsgve
     3961 syychcpfgv fgkhcelnsy gfeelsymef psldpnnnyi yvkfatiksh alllynydnq
     4021 tgeraeflal eiaeerlrfs ynlgsgtykl ttmkkvsdgq fhtviarrag maasltvdsc
     4081 senqepgyct vsnvavsddw tldvqpnrvt vggirslepi lqrrghvesh dfvgcvmefa
     4141 vngrplepsq alaaqgildq cprlegtcar npcqhggtcv dfwswqqcqc megltgkyce
     4201 ksvtpdtals legkgrldyh msqsekreyl ltqsirdttl epfgvnslev kfrtrsengi
     4261 lihiqessny ttvkikngkv hftsdagvag kveriipeay iadghwhtfr iskngsitvl
     4321 svdrihnrdi vhptqdfggi evlsmslggi ppnqahrdtq tgfngciasv lyggeslpfs
     4381 gkhslasisk tdpsvkigcr gpnicasnpc wgdllcinqw yaykcvppgd cashpcqngg
     4441 scepgllsgy tcscpeshtg rtcetvvacl gvlcpqgkvc kagspgghvc vqsqgpdeis
     4501 lplwavpaiv gscatalall vlslilcnqc rgkmpknpke ekkpkekkkk gsenvafddp
     4561 dnippygddl avrkqpegnp kpdiierenp ylifdetdip hnsetipsap laspeqeieh
     4621 ydidnassia psdadiiqhy kqfrshtpkf siqrhsplgf arqspmplga ssltyqpssy
     4681 gqglrtssls hsacptpnpl srhspapfsk psafyrnspa relhlplrdg gtlemhgdpc
     4741 qpgmfnyatr lgrrskspqa mashgsrpgs rlkqpiaqip lessppvgls ieeverlntp
     4801 rprnpsicsa dhgrssseed crrplsrtrn padgipapes ssdsdshdsf tcsemeydre
     4861 kpvvytsrmp klsqvnesda ddednygarl kprryhgrra eggpvgtpaa asgaadstlk
     4921 lgqqagnfnw dnllnwgpgf ghyvdvfkdl aslpekaagn eegksgaakp aakdgeaeqy
     4981 v
//
