ID A0A401PL89_SCYTO Unreviewed; 784 AA.
AC A0A401PL89;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cadherin-20 {ECO:0000256|ARBA:ARBA00040456};
GN ORFNames=scyTo_0002988 {ECO:0000313|EMBL:GCB73906.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB73906.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB73906.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types. {ECO:0000256|ARBA:ARBA00037319}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB73906.1}.
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DR EMBL; BFAA01000781; GCB73906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PL89; -.
DR STRING; 75743.A0A401PL89; -.
DR OMA; HESYICE; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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:SF84; CADHERIN-20; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..784
FT /note="Cadherin-20"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019507721"
FT TRANSMEM 607..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..151
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 152..260
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 261..375
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 376..480
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 480..602
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 784 AA; 87218 MW; D1E6792A9762D4D9 CRC64;
MCNKYLPGVC LLLCLADLMQ VFGVQPVTAV ESSRRDEVFH HRVKRGWVWN QFFVLEEYTG
SEPLYVGKLH SDMDKGEGSV RYILSGDGAG TVFTIDDNTG DIHAVQRLDR EEKTHYTLRA
QALDRWTGRP MEPESEFIIK IQDINDNEPK FLDGPYVASV PEMSPMGTSV IQLTASDADD
PTYGNSARVV YSILQGQPYF SVEARTGIIR TALSNMDREV KDGYQVVVQA KDMGGQMGGL
SGTTTVNITL TDVNDNPPRF PQRLYQMTVM ESAMVGLAVG RVLAQDADEG LNAELSYSFV
DGDGLNVFDI VTDTSNQGGI IILKEPLDFE TKDSYTLTVE GTNTHLDLQF LNFGPFRDTA
RVLLAVEDVD EPPQFDMTFY RVEVYEDVAV GTTIQTVSAK DPDSANNSIR YSIDRSTDPT
RFFYIDIASG ALMIAKSLDR EQLSWHNITI LAMEMKNPTQ IGSVSVTIKV LDINDNAPEF
VKDHESYICE NVKPGQLIQM VSAVDMDNPQ GGHHFYYSLA PETANNPNFT LRDNQDNTAW
ILTRRGGFKH QEQGTYFLPI LIADSGLPMQ SSTSTLTIRV CGCDPNGNVR SCNVEAYSLP
VSLSRGALIA ILSCIFILLV LVLFILTMRR HKKKSLIIDD EENVHENIVR YDDEGGGEED
TEAFDIAALW NPREMQVAKS RRDMLPEIKS LSRYVSQSRT GDDNVNSYIL AKLHDANTDP
CAPPFDSLQT YAFEGNGSVA ESLSSFESAT TDSDLNYDYL TDWGPRFKKL ADMYGGCEGT
EDSL
//
