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UniProtKB/Swiss-Prot entry P04921


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GLPC_HUMAN
Primary accession number P04921
Secondary accession numbers B2R522 Q53SV9 Q92642
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 95)
Name and origin of the protein
Protein name Glycophorin-C
Synonyms PAS-2'
Glycoprotein beta
GLPC
Glycoconnectin
Sialoglycoprotein D
Glycophorin-D
GPD
CD236 antigen
Gene name
Name: GYPC
Synonyms: GPC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2416746 [NCBI, ExPASy, EBI, Israel, Japan]
Colin Y., Rahuel C., London J., Romeo P.-H., D'Auriol L., Galibert F., Cartron J.-P.;
"Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C.";
J. Biol. Chem. 261:229-233(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3606576 [NCBI, ExPASy, EBI, Israel, Japan]
High S., Tanner M.J.A.;
"Human erythrocyte membrane sialoglycoprotein beta. The cDNA sequence suggests the absence of a cleaved N-terminal signal sequence.";
Biochem. J. 243:277-280(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0338-4535(86)80020-4; PubMed=3544149 [NCBI, ExPASy, EBI, Israel, Japan]
Cartron J.-P., Colin Y., le van Kim C., Rahuel C., Blanchard D., Bloy C., London J.;
"Structure of human erythrocyte glycophorin C deduced from cDNA analysis.";
Rev. Fr. Transfus. Immunohematol. 29:267-285(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1987.tb11478.x; PubMed=3595602 [NCBI, ExPASy, EBI, Israel, Japan]
le van Kim C., Colin Y., Blanchard D., Dahr W., London J., Cartron J.-P.;
"Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1,-2,3 types. Immunochemical study and genomic analysis with cDNA probes.";
Eur. J. Biochem. 165:571-579(1987).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN C).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-124.
SeattleSNPs variation discovery resource;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 49-88.
PubMed=3571235 [NCBI, ExPASy, EBI, Israel, Japan]
Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., Cartron J.-P.;
"Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis.";
J. Biol. Chem. 262:5808-5811(1987).
[10]
PROTEIN SEQUENCE OF 1-87.
TISSUE=Blood;
Dahr W., Humel M., Blanchard D., Beyreuther K., Cartron J.-P.;
"Isolation and structural analysis of glycophorin C.";
Biol. Chem. Hoppe-Seyler 366:777-778(1985).
[11]
PROTEIN SEQUENCE OF 1-48.
TISSUE=Blood;
PubMed=4074499 [NCBI, ExPASy, EBI, Israel, Japan]
Dahr W., Beyreuther K.;
"A revision of the N-terminal structure of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.";
Biol. Chem. Hoppe-Seyler 366:1067-1070(1985).
[12]
PRELIMINARY PROTEIN SEQUENCE OF 1-48, AND GLYCOSYLATION AT SER-3; THR-4; SER-6; ASN-8; SER-9; THR-10; SER-15; SER-24; SER-26; THR-27; THR-28; THR-31; THR-32; THR-33 AND SER-42.
TISSUE=Blood;
DOI=10.1111/j.1432-1033.1982.tb06650.x; PubMed=7106126 [NCBI, ExPASy, EBI, Israel, Japan]
Dahr W., Beyreuther K., Kordowicz M., Krueger J.;
"N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.";
Eur. J. Biochem. 125:57-62(1982).
[13]
PARTIAL PROTEIN SEQUENCE OF 30-91.
DOI=10.1111/j.1432-1033.1989.tb21093.x; PubMed=2776757 [NCBI, ExPASy, EBI, Israel, Japan]
El-Maliki B., Blanchard D., Dahr W., Beyreuther K., Cartron J.-P.;
"Structural homology between glycophorins C and D of human erythrocytes.";
Eur. J. Biochem. 183:639-643(1989).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-22 AND 42-128.
TISSUE=Spleen;
DOI=10.1093/nar/18.10.3076; PubMed=2349119 [NCBI, ExPASy, EBI, Israel, Japan]
le van Kim C., Mitjavila M.T., Clerget M., Cartron J.-P., Colin Y.;
"An ubiquitous isoform of glycophorin C is produced by alternative splicing.";
Nucleic Acids Res. 18:3076-3076(1990).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=2584223 [NCBI, ExPASy, EBI, Israel, Japan]
le van Kim C., Colin Y., Mitjavila M.T., Clerget M., Dubart A., Nakazawa M., Vainchenker W., Cartron J.-P.;
"Structure of the promoter region and tissue specificity of the human glycophorin C gene.";
J. Biol. Chem. 264:20407-20414(1989).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-128.
PubMed=2818576 [NCBI, ExPASy, EBI, Israel, Japan]
High S., Tanner M.J.A., Macdonald E.N., Anstee D.J.;
"Rearrangements of the red-cell membrane glycophorin C (sialoglycoprotein beta) gene. A further study of alterations in the glycophorin C gene.";
Biochem. J. 262:47-54(1989).
[17]
GENE STRUCTURE.
PubMed=2917976 [NCBI, ExPASy, EBI, Israel, Japan]
Colin Y., le van Kim C., Tsapis A., Clerget M., D'Auriol L., London J., Galibert F., Cartron J.-P.;
"Human erythrocyte glycophorin C. Gene structure and rearrangement in genetic variants.";
J. Biol. Chem. 264:3773-3780(1989).
[18]
VARIANT BLOOD GROUP ANTIGEN WB.
PubMed=1991173 [NCBI, ExPASy, EBI, Israel, Japan]
Chang S., Reid M.E., Conboy J., Kan Y.W., Mohandas N.;
"Molecular characterization of erythrocyte glycophorin C variants.";
Blood 77:644-648(1991).
[19]
VARIANT BLOOD GROUP ANTIGEN DH(A).
DOI=10.1111/j.1423-0410.1992.tb01220.x; PubMed=1413665 [NCBI, ExPASy, EBI, Israel, Japan]
King M.J., Avent N.D., Mallinson G., Reid M.E.;
"Point mutation in the glycophorin C gene results in the expression of the blood group antigen Dha.";
Vox Sang. 63:56-58(1992).
[20]
VARIANT BLOOD GROUP ANTIGEN AN(A).
PubMed=8219208 [NCBI, ExPASy, EBI, Israel, Japan]
Daniels G., King M.J., Avent N.D., Khalid G., Reid M.E., Mallinson G., Symthe J., Cedergren B.;
"A point mutation in the GYPC gene results in the expression of the blood group Ana antigen on glycophorin D but not on glycophorin C: further evidence that glycophorin D is a product of the GYPC gene.";
Blood 82:3198-3203(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11802; AAA60023.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36284; AAA52625.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12496; CAA31016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51973; CAA36235.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28335; AAA52574.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312032; BAG34969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY838876; AAV80423.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC013474; AAY14660.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106051; AAI06052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104246; AAI04247.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC104247; AAI04248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14242; CAA32458.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29662; AAA52626.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13890; CAA32093.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13892; CAA32093.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13893; CAA32093.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00026299; -.
IPI00218128; -.
PIR A92573; GFHUC.
RefSeq NP_002092.1; -.
NP_058131.1; -.
UniGene Hs.59138
3D structure databases
PDB
2EJY; NMR; -; B=117-128.[ExPASy / RCSB / EBI]
PDBsum 2EJY; -.
ModBase P04921.
Organism-specific databases
GeneCards GC02P127129; -.
H-InvDB HIX0029926; -.
HGNC HGNC:4704; GYPC.
GenAtlas GYPC.
HPA CAB009445; -.
HPA008965; -.
MIM 110750; gene+phenotype. [NCBI / EBI]
PharmGKB PA29082; -.
Gene expression databases
ArrayExpress P04921; -.
Bgee P04921; -.
CleanEx HS_GYPC; -.
GermOnline ENSG00000136732; Homo sapiens.
Ontologies
GO
GO:0030863; Cellular component: cortical cytoskeleton (inferred from direct assay from UniProtKB).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0009887; Biological process: organ morphogenesis (traceable author statement from ProtInc).
GO:0006487; Biological process: protein amino acid N-linked glycosylation (traceable author statement from ProtInc).
GO:0006493; Biological process: protein amino acid O-linked glycosylation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003585; Neurexin-like.
Graphical view of domain structure.
SMART SM00294; 4.1m; 1.
SMART graphical view of domain structure.
Proteomic databases
PRIDE P04921; -.
Genome annotation databases
Ensembl ENSG00000136732; Homo sapiens. [Contig view]
GeneID 2995; -.
KEGG hsa:2995; -.
Phylogenomic databases
HOGENOM P04921; -.
HOVERGEN P04921; -.
OMA P04921; SPNSTAW.
Other
NextBio 11870; -.
SOURCE GYPC; Homo sapiens.
ProtoNet P04921.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Blood group antigen; Cell membrane; Direct protein sequencing; Glycoprotein; Membrane; Polymorphism; Sialic acid; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   128  128     Glycophorin-C. PRO_0000149050
TOPO_DOM   1    57  57     Extracellular. 
TRANSMEM   58    81  24     Anchor for type III membrane protein. 
TOPO_DOM   82   128  47     Cytoplasmic. 
SITE   8     8  1     Not glycosylated; in variant Webb antigen. 
CARBOHYD   3     3        O-linked (GalNAc...). 
CARBOHYD   4     4        O-linked (GalNAc...). 
CARBOHYD   6     6        O-linked (GalNAc...). 
CARBOHYD   8     8        N-linked (GlcNAc...). 
CARBOHYD   9     9        O-linked (GalNAc...). 
CARBOHYD   10    10        O-linked (GalNAc...). 
CARBOHYD   15    15        O-linked (GalNAc...). 
CARBOHYD   24    24        O-linked (GalNAc...). 
CARBOHYD   26    26        O-linked (GalNAc...). 
CARBOHYD   27    27        O-linked (GalNAc...). 
CARBOHYD   28    28        O-linked (GalNAc...). 
CARBOHYD   31    31        O-linked (GalNAc...). 
CARBOHYD   32    32        O-linked (GalNAc...). 
CARBOHYD   33    33        O-linked (GalNAc...). 
CARBOHYD   42    42        O-linked (GalNAc...). 
VAR_SEQ   1    21        Missing (in isoform Glycophorin D). VSP_001777
VARIANT   8     8  1     N -> S (in Webb (WB) antigen). VAR_003193 
VARIANT   14    14  1     L -> F (in Duch (DH(a)) antigen). VAR_003194 
VARIANT   23    23  1     A -> S (in Ahonen (AN(a)) antigen). VAR_003195 
VARIANT   124   124  1     K -> E (in dbSNP:rs28370000 [NCBI]). VAR_021342 
Sequence information
Length: 128 AA [This is the length of the unprocessed precursor] Molecular weight: 13811 Da [This is the MW of the unprocessed precursor] CRC64: C9C654009A5642D5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWSTRSPNST AWPLSLEPDP GMASASTTMH TTTIAEPDPG MSGWPDGRME TSTPTIMDIV 

        70         80         90        100        110        120 
VIAGVIAAVA IVLVSLLFVM LRYMYRHKGT YHTNEAKGTE FAESADAALQ GDPALQDAGD 


SSRKEYFI 

P04921 in FASTA format

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