LOCUS       NP_037349               1829 aa            linear   ROD 24-JUN-2024
DEFINITION  afadin [Rattus norvegicus].
ACCESSION   NP_037349
VERSION     NP_037349.1
DBSOURCE    REFSEQ: accession NM_013217.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1829)
  AUTHORS   Maruo,T., Mizutani,K., Miyata,M., Kuriu,T., Sakakibara,S.,
            Takahashi,H., Kida,D., Maesaka,K., Sugaya,T., Sakane,A., Sasaki,T.,
            Takai,Y. and Mandai,K.
  TITLE     s-Afadin binds to MAGUIN/Cnksr2 and regulates the localization of
            the AMPA receptor and glutamatergic synaptic response in
            hippocampal neurons
  JOURNAL   J Biol Chem 299 (4), 103040 (2023)
   PUBMED   36803960
REFERENCE   2  (residues 1 to 1829)
  AUTHORS   Matsuda,T., Namura,A. and Oinuma,I.
  TITLE     Dynamic spatiotemporal patterns of alternative splicing of an
            F-actin scaffold protein, afadin, during murine development
  JOURNAL   Gene 689, 56-68 (2019)
   PUBMED   30572094
  REMARK    GeneRIF: Spatiotemporal and dynamic alternative splicing produces
            differential expression patterns of afadin isoforms and alternative
            splicing of afadin is controlled by the neuron-specific
            regulator(s) whose activity is triggered and dynamically altered
            during neuronal differentiation and maturation.
REFERENCE   3  (residues 1 to 1829)
  AUTHORS   Sellers,K.J., Watson,I.A., Gresz,R.E., Raval,P. and Srivastava,D.P.
  TITLE     Cyto-nuclear shuttling of afadin is required for rapid
            estradiol-mediated modifications of histone H3
  JOURNAL   Neuropharmacology 143, 153-162 (2018)
   PUBMED   30268521
  REMARK    GeneRIF: Study found that afadin undergoes a bi-directional
            trafficking to both synaptic and nuclear compartment in response to
            acute 17beta-estradiol (estradiol) treatment, in mixed sex neuronal
            cultures derived from fetal cortex. Nuclear accumulation of afadin
            was coincidental with an increase in the phosphorylation of histone
            H3 at serine 10 (H3S10p). This epigenetic modification is
            associated with the remodeling of chromatin.
REFERENCE   4  (residues 1 to 1829)
  AUTHORS   Shah,J., Rouaud,F., Guerrera,D., Vasileva,E., Popov,L.M.,
            Kelley,W.L., Rubinstein,E., Carette,J.E., Amieva,M.R. and Citi,S.
  TITLE     A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
            Promote alpha-Toxin Cytotoxicity
  JOURNAL   Cell Rep 25 (8), 2132-2147 (2018)
   PUBMED   30463011
REFERENCE   5  (residues 1 to 1829)
  AUTHORS   Perez White,B.E., Ventrella,R., Kaplan,N., Cable,C.J., Thomas,P.M.
            and Getsios,S.
  TITLE     EphA2 proteomics in human keratinocytes reveals a novel association
            with afadin and epidermal tight junctions
  JOURNAL   J Cell Sci 130 (1), 111-118 (2017)
   PUBMED   27815408
REFERENCE   6  (residues 1 to 1829)
  AUTHORS   Kawabe,H., Hata,Y., Takeuchi,M., Ide,N., Mizoguchi,A. and Takai,Y.
  TITLE     nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that
            interacts with synapse-associated protein 90/postsynaptic
            density-95-associated protein (SAPAP)
  JOURNAL   J Biol Chem 274 (43), 30914-30918 (1999)
   PUBMED   10521485
REFERENCE   7  (residues 1 to 1829)
  AUTHORS   Takahashi,K., Nakanishi,H., Miyahara,M., Mandai,K., Satoh,K.,
            Satoh,A., Nishioka,H., Aoki,J., Nomoto,A., Mizoguchi,A. and
            Takai,Y.
  TITLE     Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited
            to cadherin-based adherens junctions through interaction with
            Afadin, a PDZ domain-containing protein
  JOURNAL   J Cell Biol 145 (3), 539-549 (1999)
   PUBMED   10225955
REFERENCE   8  (residues 1 to 1829)
  AUTHORS   Hock,B., Bohme,B., Karn,T., Yamamoto,T., Kaibuchi,K., Holtrich,U.,
            Holland,S., Pawson,T., Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     PDZ-domain-mediated interaction of the Eph-related receptor
            tyrosine kinase EphB3 and the ras-binding protein AF6 depends on
            the kinase activity of the receptor
  JOURNAL   Proc Natl Acad Sci U S A 95 (17), 9779-9784 (1998)
   PUBMED   9707552
REFERENCE   9  (residues 1 to 1829)
  AUTHORS   Mandai,K., Nakanishi,H., Satoh,A., Obaishi,H., Wada,M.,
            Nishioka,H., Itoh,M., Mizoguchi,A., Aoki,T., Fujimoto,T.,
            Matsuda,Y., Tsukita,S. and Takai,Y.
  TITLE     Afadin: A novel actin filament-binding protein with one PDZ domain
            localized at cadherin-based cell-to-cell adherens junction
  JOURNAL   J Cell Biol 139 (2), 517-528 (1997)
   PUBMED   9334353
  REMARK    Erratum:[J Cell Biol 1997 Nov 17;139(4):1060]
REFERENCE   10 (residues 1 to 1829)
  AUTHORS   Nakano,K., Matuda,S., Yamanaka,T., Tsubouchi,H., Nakagawa,S.,
            Titani,K., Ohta,S. and Miyata,T.
  TITLE     Purification and molecular cloning of succinyltransferase of the
            rat alpha-ketoglutarate dehydrogenase complex. Absence of a
            sequence motif of the putative E3 and/or E1 binding site
  JOURNAL   J Biol Chem 266 (28), 19013-19017 (1991)
   PUBMED   1918017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            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##
            Transcript exon combination :: U83230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1829
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..1829
                     /product="afadin"
                     /note="protein Af-6; myeloid/lymphoid or mixed
                     lineage-leukemia translocation to 4 homolog;
                     myeloid/lymphoid or mixed-lineage leukemia (trithorax
                     homolog, Drosophila); translocated to, 4; myeloid/lymphoid
                     or mixed-lineage leukemia; translocated to, 4"
                     /calculated_mol_wt=207548
     Region          20..131
                     /region_name="RA1_Afadin"
                     /note="Ras-associating (RA) domain 1 found in Afadin;
                     cd01782"
                     /db_xref="CDD:340480"
     Site            order(44,58,78)
                     /site_type="other"
                     /note="RA - Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340480"
     Region          129..196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          247..347
                     /region_name="RA2_Afadin"
                     /note="Ras-associating (RA) domain 2 found in Afadin;
                     cd01781"
                     /db_xref="CDD:340479"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          356..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Region          384..502
                     /region_name="FHA_AFDN"
                     /note="forkhead associated (FHA) domain found in afadin
                     and similar proteins; cd22711"
                     /db_xref="CDD:438763"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          539..595
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          611..939
                     /region_name="Myo5p-like_CBD_afadin"
                     /note="cargo binding domain of myosin 5-like of afadin;
                     cd15471"
                     /db_xref="CDD:271255"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          1012..1099
                     /region_name="PDZ_AFDN-like"
                     /note="PDZ domain of afadin (AFDN), and related domains;
                     cd06789"
                     /db_xref="CDD:467251"
     Site            order(1024..1030,1045,1048,1078,1082,1085..1086)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467251"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          1114..1230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Site            1114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1218
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1239
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          1300..1533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          <1484..1677
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Site            1506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          1574..1724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Region          1603..>1685
                     /region_name="MAP7"
                     /note="MAP7 (E-MAP-115) family; pfam05672"
                     /db_xref="CDD:461709"
     Site            1701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55196; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Region          1742..1829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35889.1)"
     Site            1779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     Site            1812
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (O35889.1)"
     CDS             1..1829
                     /gene="Afdn"
                     /gene_synonym="Af6; Mllt4"
                     /coded_by="NM_013217.3:129..5618"
                     /db_xref="GeneID:26955"
                     /db_xref="RGD:708561"
ORIGIN      
        1 msaggrdeer rkladiihhw nanrldlfei sqptedlefh gvmrfyfqdk aagnfatkci
       61 rvsstattqd vietlaekfr pdmrmlsspk yslyevhvsg errldidekp lvvqlnwnkd
      121 dregrfvlkn endaipakka qsngpekqek egviqnfkrt lskkekkekk krekealrqa
      181 sdkeerpsqg ddsensrlaa evykdmpets ftrtisnpev vmkrrrqqkl ekrmqefrss
      241 dgrpdsggtl riyadslkpn ipyktillst tdpadfavae slekygleke npkdyciarv
      301 mlppgaqhsd ergakeiild ddecplqifr ewpsdkgilv fqlkrrppdy ipkkmkkhve
      361 gkplkgkdra dgsgygsalp peklpylvel spgrrnhfay ysyhtyedgs dsrdkpklyr
      421 lqlsvtevgt ekfddnsiql fgpgiqphhc dltnmdgvvt vtprsmdaet yvdgqriset
      481 tmlqsgmrlq fgtshvfkfv dpiqdhvlsk rsvdgglmvk gprhkpgavq ettfelggdi
      541 hsgtalpasr sttrldsdrv ssasstaerg mvkpmirldq eqdyrrresr tqdaagpelm
      601 lpasiefres sedsflsaii nytnsstvhf klsptyvlym acryvlssqh rpdisptert
      661 hkaiavvnkm vsmmegviqe vdqvdqkqkn iagalafwma nasellnfik qdrdlsritl
      721 daqdvlahlv qmafkylvhc lqselnnymp aflddpeens lqrpkiddvl htltgamsll
      781 rrcrvnaalt iqlfsqlfhf inmwlfnrlv tdpdsglcsh ywgaiirqql ghieawaekq
      841 glelaadchl srivqattll tmdkyvpddi pninstcfkl nslqlqallq nyhcapdepf
      901 iptdlienvv avaentadel arsdgrdvql eedpdlqlpf llpedgyscd vvrnipnglq
      961 efldplcqrg fcrlvphtrs pgtwtiyfeg adyeshlmre nteltqplrk epevitvtlk
     1021 kqngmglsiv aakgagqdkl giyvksvvkg gaadvdgrla agdqllsvdg rslvglsqer
     1081 aaelmtrtss vvtlevakqg aiyhglatll nqpspmmqri sdrrgsgkpr pksegfelyn
     1141 nsaqngspes pqmpwteyse pkklpgddrl mknradhrss pnvanqppsp ggkspytsgt
     1201 aakitsvstg nlcteeqtpp prpeaypipt qtytreyftf pasksqdrma pvqnqwpnye
     1261 ekphmhtesd hasiaiqrvt rsqeelreek vyqlerhrve sgmdrkcdsd mwinqsssve
     1321 sstssqehln hssksvtpas tltksgpgrw ktpaavlptp vavsqpirtd lppppppppa
     1381 hytsdfdgis mdlplppppa nqaapqsaqv aaaerkkree hqrwyekeka rleeererkr
     1441 reqerklgqm rtqslnpasf splatqakpe kpstlqrpqe tvirelqpqq qprtierrdl
     1501 qyitiskeel ssgdslspdp wkrdarekle kqqqmhivdm lskeihelqn kgdrtaeesd
     1561 rlrklmlewq fqkrlqeskq kdedddeeed ddvdtmlimq rleaerrarl qdeerrrqqq
     1621 leemrkreve drvrqeedgr hqeeervkrd aeekrrqeeg yysrleaerr rqheeaarrl
     1681 lepeepglsr pplpqdyepp sqssapsapp pppqrnasyl ktqvlspdsl ftakfvaydd
     1741 ddeeenyvpa gpnsysgsag ttagtydapr dtreklsrsq dadlpgssga penltfrerq
     1801 rlfsqgqdvs dkvkasrklt elenelntk
//
