ID A0A1S3KTD5_SALSA Unreviewed; 765 AA.
AC A0A1S3KTD5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cadherin-5 {ECO:0000256|ARBA:ARBA00021701};
DE AltName: Full=Vascular endothelial cadherin {ECO:0000256|ARBA:ARBA00030559};
GN Name=LOC106561987 {ECO:0000313|RefSeq:XP_013981971.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013981971.1};
RN [1] {ECO:0000313|RefSeq:XP_013981971.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013981971.1};
RG RefSeq;
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 RefSeq; XP_013981971.1; XM_014126496.1.
DR AlphaFoldDB; A0A1S3KTD5; -.
DR STRING; 8030.ENSSSAP00000033860; -.
DR PaxDb; 8030-ENSSSAP00000033860; -.
DR GeneID; 106561987; -.
DR KEGG; sasa:106561987; -.
DR OMA; ENDNIAT; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
DR Bgee; ENSSSAG00000041358; Expressed in spleen and 13 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
DR Gene3D; 2.60.40.60; Cadherins; 5.
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; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF89; CADHERIN-5; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..765
FT /note="Cadherin-5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010215552"
FT TRANSMEM 587..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..153
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 153..260
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 261..372
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 373..472
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 471..596
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 765 AA; 85537 MW; 2EB1B4F942D1F3C6 CRC64;
MMRQSAWRQM TGPEMWMGLF ALALTLSLTM AEHMDQRPAL QTSPVLHRHK REWLWNNLYV
EEERPTDKQY YLGKLKSTKS GDRTHYVIEG DGANTIFKVD EKGHIYVAER LDREVKSKYH
LRAKLFDTSN NLVEKVEEFV ILVTDINDND PVFTKSFNAS IKERSKRGTK VIEVTATDAD
DPTTANGELA YTLLEGGDFF NIDSTTGIIT TKYENLDRET QSSYVVVVQA QDLRGLKQGG
TATTSVTIAV SDINDNIATF TKSSYVFSVK EDMKRGQRID TIVLEDRDEI QNKDPIVTIE
PPSDIFEMER SQIKDGNLML KKGLDYETKS SYTFFVHVKE NHLQSPADNK DNPVIKAQVT
IQVIDVDEQP EFSKSIYNFN VIEEMMVNNI GVVSARDPDK ANKAIRYSIE DKNSPIGINP
VTGQLFTVRK LDRELVANHM FQVKAKEEPN GLESFVNVNI LVIDINDNKP ELSIEEIFVC
ENDMAGMVIG TISATDKDDN LPAFSFTLVK PNGNFSVIDN NDNTSNIVLK HGGFSLEDSR
DYVIEIGISD GGRPPMSSIT SLPIKVCRCD NKRIHTQCKA AQLKMGVGVY TLIPILCILT
ILVIVILIAM RKRHQKDALV TLGKSEIHEQ LVTYDEEGGG EMDTNGYDVS ILTSARNDGS
MSVRQGPSLY AMVKKPPTAC KGDMAVMIEV KKDEADHDRD GIPYDTLHIY GYEGPESLAG
SLSSLDSSST GSSLDYDFLN DWGPRFRTLA ELYGVDGSEG SDSLY
//
