ID A0A2D0SHP3_ICTPU Unreviewed; 1106 AA.
AC A0A2D0SHP3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cadherin-11 isoform X1 {ECO:0000313|RefSeq:XP_017341795.1};
GN Name=LOC108275466 {ECO:0000313|RefSeq:XP_017341795.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017341795.1};
RN [1] {ECO:0000313|RefSeq:XP_017341795.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017341795.1};
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}.
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DR RefSeq; XP_017341795.1; XM_017486306.3.
DR AlphaFoldDB; A0A2D0SHP3; -.
DR GeneID; 108275466; -.
DR KEGG; ipu:108275466; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000221080; Chromosome 15.
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; 4.
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:SF272; CADHERIN-24; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1106
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012519581"
FT TRANSMEM 712..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..235
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 236..344
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 345..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..563
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 563..681
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 31..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 120945 MW; A1571979FCDB85B8 CRC64;
MLISRSVLLV LSSCVCLSVC VENADAPALR TATERQGNSS SPTETFQSRQ RDAFKQEQED
KQQPRSSRRD QIKGSVSEST ASALSLQQSS KNSKLGLKTN TTIHSTDIPK SLSFQEVLNG
TVRLSRRRRS WIWNQFFVIE EYSGPEPVLL GRLRSSVDRG DGRVLYVLSG EGAGSVFVID
GRTGNIHVTK PLDREQKDQY RLVATATDQR TGRVLEASSQ FTIRVQDIND NPPVFKHTHY
IASVPERASA GTAVIQVTAT DADDQSYGNS AKLVYSVIQG QQYFTVDPQS GVLRTAVSDM
DREQQSQYIV VLEARDMAGH QGGLTGTTTI TVHLSDVNDS PPRFTQRVWT FSVSELALPG
AEVGRVSATD ADVGENARLE FTISDGDGGE MFNITGLNQE GVIILNQGLD FETRSSYTLS
VEVQNPSVDM RFLRGGVFKD EAVVRISVLN ADEPPHFTRS HYTLNITENC RAPCSVGRVH
AVDPDTGHST SIEYSIVPAS DPKAVFRISP VSGLITAVKV LDREREQWHN ITVTAAQRDS
PNQVTRVGVA IETLDVNDNP PELDGPYETA VCDTSTAGQV VQVIRAIDRD EISSGSPVHF
SVSAHSSRSL NFTTHARGNH TANLLLLSSL KPIPRPASSP LHTVKVPIIL RDRASELSST
GTVTVTLCPC QNGGMWVEER RRGMDGWRSG DGEVLMEWER QMVCLSLPRS SMLLGFSSAT
MLAILACSSV LIVVVVLSLS MRRKKSDSLS PVEDDEIREN IITYDDEGGG EEDTAAFDIT
ALKSVPHAIH TRGVGSVPLY GPLCYSIHTA SGSLFGGGES RLDRDKPAHT LPSGYTLNIE
LLEPGSTLTE PAEEWKSPDQ NRPEDSDDII LKKSQTGSDV IAQDQTPLVL NDSADHPVAS
HTAHLHSSVS SSVAPDEITP PHSTGISTAP FRTMEGTLLR AGGGIHLTRT PFMYLNTGQD
CIQHLVGLRV GGRSFFRPDL GGVAVPLTLS IEELLQHRLA RVTFDPMQPP YDSLQMYEHE
GAESETASLS SLESEGDGGM EGEGLIDWGP KFNKLLEIFR ERELKKDGQT KEEETEERQI
HGEQQKSVEE VDGKQEVRNE LDSRKD
//
