ID A0A3M0KE86_HIRRU Unreviewed; 882 AA.
AC A0A3M0KE86;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cadherin-1 {ECO:0000256|ARBA:ARBA00023893};
DE AltName: Full=Epithelial cadherin {ECO:0000256|ARBA:ARBA00032684};
GN ORFNames=DUI87_14388 {ECO:0000313|EMBL:RMC09380.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC09380.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC09380.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC09380.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC09380.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RMC09380.1}.
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DR EMBL; QRBI01000116; RMC09380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0KE86; -.
DR STRING; 333673.A0A3M0KE86; -.
DR Proteomes; UP000269221; 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; cd00031; CA_like; 1.
DR CDD; cd11304; Cadherin_repeat; 3.
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:SF319; CADHERIN-1; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 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 SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..882
FT /note="Cadherin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018156955"
FT TRANSMEM 704..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..263
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 264..375
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 376..487
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 488..596
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 112..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 97202 MW; A2B5C41985D9D800 CRC64;
MGRRAGRLVP LCLLLLLLQS GQRLCQRAAS CQPGFSAETF ALTVPRDSVA VGRALGRVSF
VDCGEPRRAA FLPDDTRFKV SRDGTVSATR PLQLQQREIT FAVHTWDATG KKHSAKVTLR
QRRHQHQRRK RMQQDAVPDT LIFPERGHGL QRQKRDWVIP PINCPENERG PFPKNLVQIK
SNKDKETKVF YSITGQGADT IPVGVFIIER ETGWLKVTKP LDREEKDKYV LFSHAVSASG
QPVEDPMEII ITVTDQNDNR PVFTQQVFVG YIEENAKPGT SVMTVSATDA DDAINVNNGI
IGYSILSEEP KGAQDMFTIN AENGIISVIG TGLDRETTPN YTLIIQAADQ EGNGLTNTAT
AIIKVTDAND NPPVFDPTTY EETVDENEVG VLVARLHVTD QDLPGSPAWQ AVYRIRSGDP
QGDFEITTDP KTNDGLLKTA KGLDYETKKR YTLVVSVENA VPFTVALNPA TASVLVLVRD
VNEAPIFIPP VKQVEVMEDV PVGYQITSYT AQDPDKDQSQ KITYRMGSDP AGWLAIDPEN
GIVTAAQPLD RESAHAINST YKAIILAVDN GSPHDATGTG TLLLLLQDVN DNGPVPEPRS
FDICNRQPEE QTLKIIDKDL PPNTYPFKAE LMHGSSSNWT VKIKNPDLVK LSMNKELEPG
EYNIFLKLLD GQNKEQITPV RAQVCSCEGP AKNCERRAFI SGGIGVPAIL GILGGILALL
ILLLLLLLFA RRRKVVKEPL LPPEDDMRDN VYHYDEEGGG EEDQDYDLSQ LHRGLDARPE
VIRNDVAPPL MAAPQYRPRP ANPDEIGNFI DENLKAADTD PTAPPYDSLL VFDYEGSGSE
ATSLSSLNSS ASDGDQDYDY LNDWGGRFRK LAELYGGGEE DD
//
