ID A0A3Q1F5B8_9TELE Unreviewed; 905 AA.
AC A0A3Q1F5B8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cadherin-4 {ECO:0000256|ARBA:ARBA00041040};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000002540.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000002540.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3Q1F5B8; -.
DR STRING; 80966.ENSAPOP00000002540; -.
DR Ensembl; ENSAPOT00000013272.1; ENSAPOP00000002540.1; ENSAPOG00000004289.1.
DR GeneTree; ENSGT00940000158073; -.
DR InParanoid; A0A3Q1F5B8; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0021545; P:cranial nerve development; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0048925; P:lateral line system development; IEA:Ensembl.
DR GO; GO:0042478; P:regulation of eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 4.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF81; CADHERIN-4; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..265
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 266..380
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 381..495
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 496..603
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 602..709
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 276..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 99562 MW; 01423521CE68C05C CRC64;
KFSGALSSSV QTVCSVFVYS SVGSVLLPIT ASAWQKYCYL QIEWVFEDCQ RSREVGFFSS
DPNFSVRPDG TVYAEQEVAN LSEPVQFMVT ARGLHDPHIW ETTVKLALAG HPHPLPLTKI
GIEEMLSRVW ESQPRVIKFP RKHQRGSSSN GLRRQKRDWV IPPINVPENS RGPFPHMLVR
IRSDQDKDVG IRYSITGAGA DQPPSGIYNI DPISGNMFVT QPLDREERAS FHLRAHAVDM
NGNQVENPID LYIYVIDMND NRPEFQNQVY NGSVAEGSKP GSSVMQVTAT DSDDSTTANG
MVRYRILSQT PHSPIPNMFT INSETGDIVT VAAGLDREKV SQYTIIVQAT DMEGNLNFGL
SNTATALISI TDINDNPPEL TVRTFSGEVP ENKVNVVVTN LTVVDRDQPH SPNWNAVYRI
VSGDPSGHFT IRTNPITNEG MLTVVKPVDF EMNRAFMLTV VVSNQAHLAS GIQSSLQSTA
GVTISVQDVN EPPVFPVNPK TIRFEEGVPA GTTLTVFAAQ DPDHFVHQSV RYSKLSDPAN
WLKINRTNGQ ITTMALLDRE SMYVKNNVYE ATFLAFDSGS PQASGTGTLQ IYLIDVNDNA
PVLIPREAQV CERARPNSKI NITASDADAD PNVGPFVFEL PSFPASVRRN WTISRLSGDY
AQLRLRIPYL EAGVYEIPVI VSDSGNPPLT NRSVIRVKVC PCDDNGDCSA TGAVAAAGLG
TGAIIAILIC IIILLSMVLL FVVWMKRREK ERQAKPLLID PEDDVRDNIL KYDEEGGGEE
DQDYDLSQLQ QPESLEHIIN KPSGVRRVDE RPVIAESQYP VRPSLPHPGD IGDFINDGLR
AADNDPTAPP YDSLLVFDYE GSGSTAGSVS SLNSTSSGDQ DYDYLNDWGP RFKKLADLYG
GGDDD
//
