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Database: UniProt
Entry: A0A340Y8A4_LIPVE
LinkDB: A0A340Y8A4_LIPVE
Original site: A0A340Y8A4_LIPVE 
ID   A0A340Y8A4_LIPVE        Unreviewed;      1038 AA.
AC   A0A340Y8A4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Protocadherin-1 isoform X2 {ECO:0000313|RefSeq:XP_007468004.1};
GN   Name=PCDH1 {ECO:0000313|RefSeq:XP_007468004.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007468004.1};
RN   [1] {ECO:0000313|RefSeq:XP_007468004.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_007468004.1; XM_007467942.1.
DR   AlphaFoldDB; A0A340Y8A4; -.
DR   GeneID; 103083177; -.
DR   CTD; 5097; -.
DR   OrthoDB; 5353710at2759; -.
DR   Proteomes; UP000265300; 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; 7.
DR   Gene3D; 2.60.40.60; Cadherins; 7.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR013585; Protocadherin.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF247; PROTOCADHERIN-1; 1.
DR   Pfam; PF00028; Cadherin; 6.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF08374; Protocadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 7.
DR   PROSITE; PS00232; CADHERIN_1; 4.
DR   PROSITE; PS50268; CADHERIN_2; 7.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..1038
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016313556"
FT   TRANSMEM        831..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..146
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          147..258
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          259..365
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          374..484
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          485..590
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          591..693
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          711..822
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          871..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  112489 MW;  0C97247FDE720DAE CRC64;
     MGSLRRSPGP GGRRLLLPAS LLALLLLLAP SPGHATRVVY KVPEEQPPNT LIGSLAADYG
     FPDVGHLYKL EVGAPYLRVD GKTGDIFTTE TSIDREGLRE CQNQLPGEPC ILEFEVSITD
     LVQNGSPRLL EGQIEVQDIN DNTPNFASPV ITLPIPENTN IGSLFSIPVA SDRDAGPNGV
     ASYELQVGPE AQELFGLQVA EDQDGKQPQL IVMGNLDRER LDSYDLTIKV QDGGNPPRAS
     SALLRVTVLD TNDNAPKFER PSYEAELSEN SPIGHSVIQV KANDSDQGAN AEIDYTFHQV
     PEVVRRLLRL DRNTGLITVQ GPVDREDLST LRFSVLAKDR GTNPKSARAQ VVVTVKDMND
     NAPTIEIRGI GLVTHQDGMA NISEDVAEET AVALVQVSDR DEGENAAVTC VVAGDVPFQL
     RQASETGSDS RKKYFLQTTT PLDYEKVKDY TIEIVAVDSG NPPLSSTNSL KVQVVDVNDN
     APVFTQSITE VAFPENNKPG EVVAEVTASD ADSGSNAELV YSLEPEPAAK GLFTISPETG
     EIRVKTSLDR EQRESYELKV VAADRGSPSL QGTATVLVNV LDCNDNDPKF MLSGYNFSVM
     ENMPALSPVG MVTVIDGDKG ENARVQLTVE QDNGDFVIQN GTGTILSSLS FDREQQSTYT
     FQLKAVDGGV PPRSAYVGVT INVLDENDNA PFITAPSNTS HRLLTPQTRL GETVSQVTAE
     DIDSGVNAEL TYSIAGGNPY GLFQIGSHSG AITLEKEIER RHHGLHRLVV KVTDRGKPPR
     YGTALVHLYV NDTLANRTLL ETLLGHSLDT PLDIDIAGDP EYERSKQRGN ILFGVVAGVV
     AVALLIALAV LVRYCRQREA KSGYQAGKKE TKDLYAPKPS SKVSKGNKSK GKKSKSPKPV
     KPVEDEDEAG LQKSLKFNLM SDAPGDSPRI HLPLNYPPGS PDLGRHYRSN SPLPSIQLQP
     QSPSASKKHQ VVQDLPPANT FVGTGDTTST GSEQYSDYSY RTNPPKYPSK QVGQPLRLSM
     PRPPPHPYHG AIWTEVWE
//
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