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Database: UniProt
Entry: A0A2K6V4P6_SAIBB
LinkDB: A0A2K6V4P6_SAIBB
Original site: A0A2K6V4P6_SAIBB 
ID   A0A2K6V4P6_SAIBB        Unreviewed;       368 AA.
AC   A0A2K6V4P6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Protocadherin 1 {ECO:0000313|Ensembl:ENSSBOP00000039143.1};
GN   Name=PCDH1 {ECO:0000313|Ensembl:ENSSBOP00000039143.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000039143.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000039143.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6V4P6; -.
DR   Ensembl; ENSSBOT00000056102.1; ENSSBOP00000039143.1; ENSSBOG00000035615.1.
DR   GeneTree; ENSGT00940000155521; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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; 2.
DR   Gene3D; 2.60.40.60; Cadherins; 3.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF247; PROTOCADHERIN-1; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
DR   PROSITE; PS00232; CADHERIN_1; 1.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..368
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014424782"
FT   DOMAIN          76..154
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          155..266
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          297..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  39985 MW;  6D8E4961469D9F68 CRC64;
     LLILAPARMG PLRRSPGPGG QRLLLSSMLL AVLLLLAPSP GHATRVVYKV LEEQPPNTLI
     GSLAADYGFP DVGHLYKLEV GAPYLRVDGK TGDIFTTETS IDREGLRECQ NQLPGEPCIL
     EFEVSITDLV QNGSPRLLEG QIEVQDINDN TPNFASPVIT LAIPENTNIG SLFPIPLASD
     RDAGPNGVAS YELQAGPEAQ ELFGLQVAED QEEKQPQLIV MGNLDRERWD SYDLTIKVQD
     GGSPPRASSA LLRVTVLDTN DNAPKFERPS YEAELSENSP IGHSVIQLPH RRVTFSATSQ
     AQELQDPSQH SYYDSGLEES ETPSSKSSSG PRLGPLALPE DHYERTTPDG SIGEMEHPEN
     EPAGRSRP
//
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