LOCUS       NP_001025159            4351 aa            linear   ROD 28-APR-2025
DEFINITION  protocadherin Fat 2 precursor [Mus musculus].
ACCESSION   NP_001025159 NP_001074772 XP_147546
VERSION     NP_001025159.1
DBSOURCE    REFSEQ: accession NM_001029988.2
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 4351)
  AUTHORS   Khang,R., Jo,A., Kang,H., Kim,H., Kwag,E., Lee,J.Y., Koo,O.,
            Park,J., Kim,H.K., Jo,D.G., Hwang,I., Ahn,J.Y., Lee,Y., Choi,J.Y.,
            Lee,Y.S. and Shin,J.H.
  TITLE     Loss of zinc-finger protein 212 leads to Purkinje cell death and
            locomotive abnormalities with phospholipase D3 downregulation
  JOURNAL   Sci Rep 11 (1), 22745 (2021)
   PUBMED   34815492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4351)
  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   3  (residues 1 to 4351)
  AUTHORS   Capecchi,M.R. and Pozner,A.
  TITLE     ASPM regulates symmetric stem cell division by tuning Cyclin E
            ubiquitination
  JOURNAL   Nat Commun 6, 8763 (2015)
   PUBMED   26581405
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 4351)
  AUTHORS   Miyagaki,Y., Kanemori,Y. and Baba,T.
  TITLE     Possible involvement of mitogen- and stress-activated protein
            kinase 1, MSK1, in metaphase-II arrest through phosphorylation of
            EMI2 in mouse oocytes
  JOURNAL   Dev Biol 359 (1), 73-81 (2011)
   PUBMED   21924255
REFERENCE   5  (residues 1 to 4351)
  AUTHORS   Barlow,J.L., Drynan,L.F., Hewett,D.R., Holmes,L.R.,
            Lorenzo-Abalde,S., Lane,A.L., Jolin,H.E., Pannell,R.,
            Middleton,A.J., Wong,S.H., Warren,A.J., Wainscoat,J.S.,
            Boultwood,J. and McKenzie,A.N.
  TITLE     A p53-dependent mechanism underlies macrocytic anemia in a mouse
            model of human 5q- syndrome
  JOURNAL   Nat Med 16 (1), 59-66 (2010)
   PUBMED   19966810
REFERENCE   6  (residues 1 to 4351)
  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
REFERENCE   7  (residues 1 to 4351)
  AUTHORS   Wu,Q.
  TITLE     Comparative genomics and diversifying selection of the clustered
            vertebrate protocadherin genes
  JOURNAL   Genetics 169 (4), 2179-2188 (2005)
   PUBMED   15744052
REFERENCE   8  (residues 1 to 4351)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AL713870.26,
            AK173031.1 and AK132523.1.
            
            On or before Feb 11, 2007 this sequence version replaced
            NP_001074772.1, XP_147546.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4351
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 32.5 cM"
     Protein         1..4351
                     /product="protocadherin Fat 2 precursor"
                     /note="protocadherin Fat 2"
                     /calculated_mol_wt=478218
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1911
     mat_peptide     19..4351
                     /product="Protocadherin Fat 2. /id=PRO_0000406601"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F226.1)"
                     /calculated_mol_wt=478218
     Region          38..143
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            order(44..45,108,110,140,142..143)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          152..249
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          366..454
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(373..374,422,424,450,452..453)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          462..560
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(469..470,521,523,556,558..559)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          570..661
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          719..815
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(726..727,779,781,812,814..815)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          825..921
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(831..832,882,884,917,919..920)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          931..1026
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(936..937,988,990,1022,1024..1025)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            996
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          1036..1133
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1043..1044,1096,1098,1129,1131..1132)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1141..1238
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1148..1149,1201,1203,1234,1236..1237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          1247..1335
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            1276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          1353..1444
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1360..1361,1409,1411,1440,1442..1443)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1417
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          1452..1551
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1459..1460,1513,1515,1547,1549..1550)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1560..1650
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          1664..1754
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1671..1672,1719,1721,1750,1752..1753)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1762..1867
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1769..1770,1829,1831,1864,1866..1867)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1877..1959
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            1899
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          1972..2066
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1979..1980,2029,2031,2062,2064..2065)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            1998
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            2007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2074..2163
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            2165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2176..2268
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2182..2183,2232,2234,2264,2266..2267)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2276..2375
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2283..2284,2338,2340,2371,2373..2374)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            2368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2383..2475
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            2430
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            2470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2485..2581
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2492..2493,2544,2546,2577,2579..2580)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            2547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2590..2683
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            2597
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          2697..2795
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2703..2704,2757,2759,2791,2793..2794)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2803..2904
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2810..2811,2866,2868,2900,2902..2903)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          2913..3009
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(2919..2920,2975,2977,3005,3007..3008)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          3018..3111
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3024..3025,3076,3078,3107,3109..3110)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          3122..3211
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            3127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3226..3319
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3231..3232,3282,3284,3315,3317..3318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3328..3424
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(3334..3335,3387,3389,3420,3422..3423)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            3432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3433..3524
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          3544..3621
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            3603
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3770
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3774
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3802..3923
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            3815
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3875
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Site            3906
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3953..3986
                     /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            3991
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          3992..4022
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            4051..4071
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F226.1)"
     Region          4313..4340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5F226.1)"
     CDS             1..4351
                     /gene="Fat2"
                     /gene_synonym="EMI2; Fath2; Gm523; mKIAA0811"
                     /coded_by="NM_001029988.2:12..13067"
                     /db_xref="CCDS:CCDS36157.1"
                     /db_xref="GeneID:245827"
                     /db_xref="MGI:MGI:2685369"
ORIGIN      
        1 mtlvllgvam vllhraacek pleetitplt wrfthslyna tiyensapkt yvespvkmgm
       61 ylaephwvvk yriisgdaag vfkteehvvg nfcflrirtk ssntallnre vrdsytlvvq
      121 asdkslefea ltqvvvhild qndlkplfsp psyrftised rplkspickv tatdadlgqn
      181 aefyyafnar sevfaihpts gvvtvagkln vtwrgkyelq vlavdrmrki segngfgnla
      241 plviyvepvh rkppvitlvv lnppegdegd iyatvtvdtn gsgaevdsle vvggdpgkyf
      301 kvlksyaqgn efnlvavrdi nwaehlhgfn islqthsrsr fpsrsiiraf hlppytlanl
      361 rfekavyrvk lsefsppgsr valvrvttal ptlryalkps sgstvfklna rtglitttkp
      421 vdfheqnqyq lhvktslgqa tttviidivd cnnhapvfnr ssyegtlden ippgtsvltv
      481 tatdqdhgdn ghitysiagp kavpfsidpy lgvisttksm dyelmkriyt frvrasdwgs
      541 pfrqekevsv slrlknlndn qpmfeevnct vslrqdapvg ksimavsaid mdelqnlkye
      601 ivsgneqdyf hlnhfsgvis lkrsfmnlta vrptvyslki tasdgknyas pttlkvtvvk
      661 dprsevpvqc dktgvlthit ktilqsaglq gqemgeedft slgnyqinhh apqfedhfpq
      721 sidileqvpv ntplahlaat dpdpgfhgrl vyviadgnee gcfdieletg lltvaaaldy
      781 ettsfyvlnv tvydlgtppk sswklltvtv kdwndkpprf ppggyqltis edtevgttva
      841 elktrdtdse dngrvrytll tptekfslhp ltgelvvtgq ldresepqyi lkaeardqpt
      901 kghqlfsvtd vivtledind nppqcitehs slkvpedmpl gtvltfldas dpdlgpagev
      961 kyilvddvhg tfrvdpmtga lslekeldfe rragynlsfw asdsgrplar rtlchvevlv
     1021 mdvnenlhsp hfssfvyqgq vqenspagtq vmvvtaqddd sgldgelqyf lragtgleaf
     1081 sinqdtgmle tlapldreft pyywltvlav drgsvplsav tevyievtdi ndnipsmsrp
     1141 vfypsvkeda plgtsvlqle awdpdfssqg kltfnltsgn hmghfivhpf tgllstakql
     1201 drenkdeyvl evtvqdngdp plrstsrvvv cvldvndnsp mfshklfnvr lserlsplsp
     1261 epvyrlvasd pdeglngsit ysieesdees fridpvtgvv sssstfaage yniltikatd
     1321 sgqpalstsv rlhiewipqp rpssiplsfd eshysfavme tdpvnhmlgv isvegrpglf
     1381 wfhisdgdkd mdfdiekttg siviarpldt rrkssynltv evtdgfhtia tqvhilmian
     1441 inhhrpqflq dhydirvpqd tlpgvellrv qatdqdhgkg liytihssrd pgsanlfqld
     1501 pssgvlvtvg tldlhsgpsq hiltvmvrdq empikrnfvw vtihvedgnl hsphftqpry
     1561 eanvpdtttp gtellqvrav dadrganaev hysflkgnse gffnidsllg iitvaqrldh
     1621 vhlnrhaltv kaedqgspqr hdlamvvvhv hpsdssapif skdeyfieip esvpigspil
     1681 lisaasssdv tyelregnkn svfsmnsysg listqkrldh ekvssyqlki rgsnmagvft
     1741 evvalvyiid endnapaflk stfvghisea aplhslilge dnsplviras dsdqeansll
     1801 vykilepeal kffkidpsmg tltitseldy ettplfqfsi yvhdqgtpil faprsarvii
     1861 hvrdvndspp rfseqiyeva vvepihpgme lltvqaednd skvtysikts ntdeavtihp
     1921 itgqisvvnp aalrlfpkln irafdglyqd tavvkisltq aldkslqfdq diyrarvten
     1981 tphsnvlvil gvhgnhlndt lsyfllngtd lfhmvksagv lqtrgvtfdr eqqdthevav
     2041 evrdnrvprr vaqalvrvsv edvndnipef qhlpyytviq dgtepgdvlf qvsatdkdlg
     2101 angtvtygfa edyayfridp yvgdislkkp fdyqalnkyh lrvtardagt pplqtevevh
     2161 vtvrnksnpl fqspyykvkv penitlytpi lhtqarspeg lrliynivee eplmlfttdf
     2221 ktgvltvtgp ldyesknkhv ftvratdtal gsfseatvev lvedindnpp tfsqlvysts
     2281 vsegspaqtp viqllasdqd sgqnqdvsyq ivedgsdvsk ffringstge mftiqeldye
     2341 ahqhfrvkvr atdrgdpplt getlvvvnvs dindnppefr epqyeanvse latcghlvlk
     2401 vqaldpdigd tsrleylils gnqdrhfsin stsgiismfn lckkqldssy nlrvgasdgv
     2461 fqatvpvyin ttnankyspe fqqnvyeael aenakvgtkv iellaidkds gpygtvdyti
     2521 inklagerff inpsgqittl qkldrenste rviaikimar dgggkvafct vkiiltdend
     2581 napqfkasgy tvsipsnvsr dspiiqvlay dadegrnadv tysvdstedl aeeiievnpt
     2641 tgvvkvkesl vglenkavdf nikaqdggpp hwdslvpvrl qvvpneiplp kfseplytfs
     2701 asedlpegse igsvkavaaq dpiiyslvqg ttpesnsddv fsldqdtgvl kvkkamdhes
     2761 tkwyqidlma hcphedtdlv slvsvniqve dvndnrpvfe adpykaflte nmpggttviq
     2821 vtandqdtgs dgqvsyrlsv epgsnihqlf avdsesgwit tlqeldcetq qtyrfyvvaf
     2881 dhgqtiqlss qalvevsitd endnpprfas edyrgsvven nepgelvatl ktldadiseq
     2941 nrqvtcyite gdplgqfsis qvgdewrits rktldrehia kyllritasd gkfqasvpve
     3001 vfvldindns pqcsqllytg kvredvtpgh filkvsaidv dmdtnaqity slhgpgaqef
     3061 kldphtgelt tlsvldrerk dvynlvakat dgggqscqae vtlhiedvnd naprffpshc
     3121 avavfdnttv ktpvavvfar dpdqgvnaqv vysltdsadg qfsidatsgv irlekplqvr
     3181 sssaveltvr asdlgtpipl stlgtvtvsi vgledylpif lnsehstqvp edalidmevl
     3241 ylatltrpgs ektgyhitgg neqgkfrlda htgilyvngs ldfetnpkyf lsiecsrkss
     3301 sslsdvttiv invtdvnehh prfthdlytv rvlenaivgd viltvsasdd dgpvnsvity
     3361 slvggnqlgh ftidpkkgkl qvakaldweq tpsyslrira tdsgqpplhe dtevavevvd
     3421 vndnpprffq lnystavqen spigikvlql ilddpdspqn gppyffrite gntgsvfrvt
     3481 pdgwlvtags lsrraqewyq lhievsdsgl pplssstlvr vhiteqsryp pstlpleifi
     3541 tkgeeefqgg mvgkihatdr dpqdtltysl dregslgkyf tvgasdgkii asqglprgry
     3601 lfnvtvsdgt fttttgvhvh vwhmgqeapq qavwlgfhql tpeelvsdhw rnlqrflsni
     3661 ldikranihl aslqpaevta gvdvllafeg hsgtsydlqe lasaiahsak emehsvgiqm
     3721 rsalpvvpcq gpscqdqtcq etvsleprvg psystarlsi ltprhhlgkn cscngttwrf
     3781 sgqsymryrp leaqnwqihf ylktlqpwal lmftnetasi slklangflh leyrcpggfy
     3841 gnlsshrpvn dgqwhsmlle erdtsvhllv ditdntslvi peecqglrte rhlllgglvp
     3901 snpssnvslg fegcldavvv nserlellgh rkkmagylet walsqccwpg ttcsqnpcln
     3961 ggscspalgs gylcrcpplf sgrncelgre nctsapcqeg gtcvsspegt scscphpytg
     4021 drcemeargc sgghclitpe ikrgdwgqqe flviivalpl liiatvglll ycrrckshkp
     4081 vamedpdlla rsigvdtqas paieldplna gscndlnqle psktsvpnel vtfgpsskqr
     4141 pmvcsvpprl ppavvsshpg hepiikrtws geelvypsga avwpptysrk ehweyphpea
     4201 mqgplppspr rhvspavmpd paglyggfpf plelenkrap lpprysnqnl edlipprpps
     4261 prehllapcl neytaisyyh sqfrqggggp claeggykgv smrlsragps yadcevnggp
     4321 apgrsqprap pnyegsdmve sdygsceevm f
//
