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GPC5_HUMAN
ID   GPC5_HUMAN              Reviewed;         572 AA.
AC   P78333; B2R726; O60436; Q9BX27;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Glypican-5;
DE   Contains:
DE     RecName: Full=Secreted glypican-5;
DE   Flags: Precursor;
GN   Name=GPC5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9070915; DOI=10.1006/geno.1996.4518;
RA   Veugelers M., Vermeesch J., Reekmans G., Steinfeld R., Marynen P.,
RA   David G.;
RT   "Characterization of glypican-5 and chromosomal localization of human GPC5,
RT   a new member of the glypican gene family.";
RL   Genomics 40:24-30(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9331333; DOI=10.1006/dbio.1997.8690;
RA   Saunders S., Paine-Saunders S., Lander A.D.;
RT   "Expression of the cell surface proteoglycan glypican-5 is developmentally
RT   regulated in kidney, limb, and brain.";
RL   Dev. Biol. 190:78-93(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       P78333; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-2558325, EBI-18924329;
CC       P78333; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-2558325, EBI-3893327;
CC       P78333; Q6PRD1: GPR179; NbExp=2; IntAct=EBI-2558325, EBI-20895185;
CC       P78333; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-2558325, EBI-10694180;
CC       P78333; Q8N488: RYBP; NbExp=3; IntAct=EBI-2558325, EBI-752324;
CC       P78333; Q8C419: Gpr158; Xeno; NbExp=2; IntAct=EBI-2558325, EBI-776313;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}; Extracellular side {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Secreted glypican-5]: Secreted, extracellular
CC       space {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In adult, primarily expressed in the brain. Also
CC       detected in fetal brain, lung and liver. {ECO:0000269|PubMed:9070915,
CC       ECO:0000269|PubMed:9331333}.
CC   -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/GPC5ID45705ch13q31.html";
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DR   EMBL; U66033; AAC51118.1; -; mRNA.
DR   EMBL; AF001462; AAC12261.1; -; mRNA.
DR   EMBL; AK312815; BAG35673.1; -; mRNA.
DR   EMBL; AL157363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL163537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL162456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC039730; AAH39730.1; -; mRNA.
DR   CCDS; CCDS9468.1; -.
DR   RefSeq; NP_004457.1; NM_004466.5.
DR   AlphaFoldDB; P78333; -.
DR   SMR; P78333; -.
DR   BioGRID; 108553; 8.
DR   IntAct; P78333; 10.
DR   STRING; 9606.ENSP00000366267; -.
DR   GlyGen; P78333; 8 sites.
DR   iPTMnet; P78333; -.
DR   PhosphoSitePlus; P78333; -.
DR   BioMuta; GPC5; -.
DR   DMDM; 2829667; -.
DR   jPOST; P78333; -.
DR   MassIVE; P78333; -.
DR   MaxQB; P78333; -.
DR   PaxDb; P78333; -.
DR   PeptideAtlas; P78333; -.
DR   PRIDE; P78333; -.
DR   ProteomicsDB; 57571; -.
DR   Antibodypedia; 24761; 266 antibodies from 33 providers.
DR   DNASU; 2262; -.
DR   Ensembl; ENST00000377067.9; ENSP00000366267.3; ENSG00000179399.15.
DR   GeneID; 2262; -.
DR   KEGG; hsa:2262; -.
DR   MANE-Select; ENST00000377067.9; ENSP00000366267.3; NM_004466.6; NP_004457.1.
DR   UCSC; uc010tif.3; human.
DR   CTD; 2262; -.
DR   DisGeNET; 2262; -.
DR   GeneCards; GPC5; -.
DR   HGNC; HGNC:4453; GPC5.
DR   HPA; ENSG00000179399; Tissue enhanced (brain, kidney, testis).
DR   MIM; 602446; gene.
DR   neXtProt; NX_P78333; -.
DR   OpenTargets; ENSG00000179399; -.
DR   PharmGKB; PA28834; -.
DR   VEuPathDB; HostDB:ENSG00000179399; -.
DR   eggNOG; KOG3821; Eukaryota.
DR   GeneTree; ENSGT01050000244955; -.
DR   InParanoid; P78333; -.
DR   OMA; PKPDKWE; -.
DR   OrthoDB; 1097767at2759; -.
DR   PhylomeDB; P78333; -.
DR   TreeFam; TF105317; -.
DR   PathwayCommons; P78333; -.
DR   Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   Reactome; R-HSA-2024096; HS-GAG degradation.
DR   Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR   Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR   Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR   Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   Reactome; R-HSA-5362798; Release of Hh-Np from the secreting cell.
DR   Reactome; R-HSA-9694614; Attachment and Entry.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; P78333; -.
DR   BioGRID-ORCS; 2262; 15 hits in 1063 CRISPR screens.
DR   ChiTaRS; GPC5; human.
DR   GeneWiki; Glypican_5; -.
DR   GenomeRNAi; 2262; -.
DR   Pharos; P78333; Tbio.
DR   PRO; PR:P78333; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; P78333; protein.
DR   Bgee; ENSG00000179399; Expressed in caudate nucleus and 124 other tissues.
DR   ExpressionAtlas; P78333; baseline and differential.
DR   Genevisible; P78333; HS.
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:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR   InterPro; IPR001863; Glypican.
DR   InterPro; IPR031188; Glypican-5.
DR   InterPro; IPR019803; Glypican_CS.
DR   PANTHER; PTHR10822; PTHR10822; 1.
DR   PANTHER; PTHR10822:SF12; PTHR10822:SF12; 1.
DR   Pfam; PF01153; Glypican; 1.
DR   PROSITE; PS01207; GLYPICAN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Heparan sulfate; Lipoprotein;
KW   Membrane; Proteoglycan; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..?
FT                   /note="Glypican-5"
FT                   /id="PRO_0000012319"
FT   CHAIN           25..?
FT                   /note="Secreted glypican-5"
FT                   /id="PRO_0000333849"
FT   PROPEP          ?..572
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012320"
FT   REGION          355..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        527
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         155
FT                   /note="A -> V (in dbSNP:rs553717)"
FT                   /id="VAR_024228"
FT   CONFLICT        205
FT                   /note="G -> C (in Ref. 2; AAC12261)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="S -> F (in Ref. 2; AAC12261)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   572 AA;  63707 MW;  A17969FE0DD0D308 CRC64;
     MDAQTWPVGF RCLLLLALVG SARSEGVQTC EEVRKLFQWR LLGAVRGLPD SPRAGPDLQV
     CISKKPTCCT RKMEERYQIA ARQDMQQFLQ TSSSTLKFLI SRNAAAFQET LETLIKQAEN
     YTSILFCSTY RNMALEAAAS VQEFFTDVGL YLFGADVNPE EFVNRFFDSL FPLVYNHLIN
     PGVTDSSLEY SECIRMARRD VSPFGNIPQR VMGQMGRSLL PSRTFLQALN LGIEVINTTD
     YLHFSKECSR ALLKMQYCPH CQGLALTKPC MGYCLNVMRG CLAHMAELNP HWHAYIRSLE
     ELSDAMHGTY DIGHVLLNFH LLVNDAVLQA HLNGQKLLEQ VNRICGRPVR TPTQSPRCSF
     DQSKEKHGMK TTTRNSEETL ANRRKEFINS LRLYRSFYGG LADQLCANEL AAADGLPCWN
     GEDIVKSYTQ RVVGNGIKAQ SGNPEVKVKG IDPVINQIID KLKHVVQLLQ GRSPKPDKWE
     LLQLGSGGGM VEQVSGDCDD EDGCGGSGSG EVKRTLKITD WMPDDMNFSD VKQIHQTDTG
     STLDTTGAGC AVATESMTFT LISVVMLLPG IW
 
 
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