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GPC1_CHICK
ID   GPC1_CHICK              Reviewed;         550 AA.
AC   P50593;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glypican-1;
DE   AltName: Full=Heparan sulfate proteoglycan core protein;
DE   Contains:
DE     RecName: Full=Secreted glypican-1;
DE   Flags: Precursor;
GN   Name=GPC1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Heart;
RX   PubMed=8875073;
RX   DOI=10.1002/(sici)1097-0177(199609)207:1<25::aid-aja3>3.0.co;2-y;
RA   Shi N., Antin P.B., Akimoto K., Morkin E.;
RT   "Expression of avian glypican is developmentally regulated.";
RL   Dev. Dyn. 207:25-34(1996).
CC   -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC       Modulates Wnt-signaling pathway.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Endosome
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular
CC       space {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at stage 7 of embryonic development in
CC       the folding anterior part of the neural plate. At stage 8, high levels
CC       in all four newly formed epithelial somites and in the rostra1 paraxial
CC       mesoderm. Expressed also in the cephlic region of the developing neural
CC       fold. Later expression in the entire limb bud, including mesenchyme and
CC       ectoderm. In the developing brain, first detected at stage 7 in the
CC       anterior portion of the neural folds that are destined to give rise to
CC       the telencephalon. Later in development (stage 25), glypican
CC       transcripts were found in postmitotic cells in the mantle zone.
CC       Expressed by ectodermal and ingressing chick trigeminal placode cells
CC       at the time they differentiate into neurons and assemble into ganglia.
CC       Also expressed in the migrating hindbrain neural crest cells from
CC       rhombomeres 4 and 6 during migration at stage 12.
CC       {ECO:0000269|PubMed:8875073}.
CC   -!- PTM: O-glycosylated with heparan sulfate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA65199.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L29089; AAA65199.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P50593; -.
DR   SMR; P50593; -.
DR   STRING; 9031.ENSGALP00000003684; -.
DR   PaxDb; P50593; -.
DR   VEuPathDB; HostDB:geneid_424770; -.
DR   eggNOG; KOG3821; Eukaryota.
DR   InParanoid; P50593; -.
DR   PhylomeDB; P50593; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IEA:InterPro.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:AgBase.
DR   GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR   GO; GO:1902726; P:positive regulation of skeletal muscle satellite cell differentiation; ISS:AgBase.
DR   GO; GO:1902724; P:positive regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR   GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR   InterPro; IPR001863; Glypican.
DR   InterPro; IPR015502; Glypican-1.
DR   InterPro; IPR019803; Glypican_CS.
DR   PANTHER; PTHR10822; PTHR10822; 1.
DR   PANTHER; PTHR10822:SF8; PTHR10822:SF8; 1.
DR   Pfam; PF01153; Glypican; 1.
DR   PROSITE; PS01207; GLYPICAN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endosome; Glycoprotein; GPI-anchor;
KW   Heparan sulfate; Lipoprotein; Membrane; Proteoglycan; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..524
FT                   /note="Glypican-1"
FT                   /id="PRO_0000012301"
FT   CHAIN           21..?
FT                   /note="Secreted glypican-1"
FT                   /id="PRO_0000333840"
FT   PROPEP          525..550
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012302"
FT   REGION          475..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           524
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..253
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        243..276
FT                   /evidence="ECO:0000250"
FT   DISULFID        265..412
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..398
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  61084 MW;  6B7B796E506BF7FF CRC64;
     MRFFPWGFWL LCVASAPARG DSGSKARSCA EVRQLYGAKG FSLNGVPQAE ISGEHLRICP
     QGYTCCTSEM EENFANKSRS EFEAMMKEAG RSVQTILTAQ YKSFDNYFQD LLNKSEKALY
     DTFPSLYGDL YTQNMKVFKD LYSELRRYYR GSNINLEEAL NEFWTRLLER LFKLMNAQYH
     ITDEYLDCMV KHAEQHKPFG EVPRDLKVKA TRAFIVARSY AQGFLVGSDV VKKVSQVSLS
     HECTRAVMKL MYCPHCRGMA SVKPCSNYCL NVVKGCLANQ ADLNTEWKYL MDALVAVADR
     IDGPYNVDTV IGTIHMRISE AISNLQENKV SITAKVFQGC GNPKVSMKGS SSEDKKRRGK
     VTLEAKSSAV ALEMLVLDAK GNLTALKSYW VTLPGVLCSK KIMASPAEDD KCWNGMTKGS
     YLPEVMGGGL ANQINNPEVE VDITKPDMTI RQQIMQLKIM TNRLGNANIG NDVDFQDASD
     DMSGSGSGDS CPDDVCVKRL SKSPSTRQPE THAIPKQSGH GVIGASSRSL PSAFLLFLSG
     ASIVVQHLWR
 
 
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