Reviewed,
UniProtKB/Swiss-Prot P04921 (GLPC_HUMAN)
Last modified
November 3, 2009.
Version 100.
History...
Clusters with 100%,
90%,
50% identity |
Documents (8) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycophorin-C Alternative name(s): PAS-2' Glycoprotein beta Glycoconnectin Sialoglycoprotein D Glycophorin-D Short name=GPD CD_antigen=CD236 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 128 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells. |
| Subcellular location | Cell membrane; Single-pass type III membrane protein. Note: Linked to the membrane via band 4.1. |
| Tissue specificity | Glycophorin-C is expressed in erythrocytes. Glycophorin-D is ubiquitous. |
| Polymorphism | GYPC is responsible for the Gerbich blood group system. |
| Sequence similarities | Belongs to the glycophorin-C family. |
| Sequence caution | The sequence CAA32093.1 differs from that shown. Reason: Frameshift at position 35. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Transmembrane |
| Ligand | Sialic acid |
| Molecular function | Blood group antigen |
| PTM | Glycoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | organ morphogenesis Ref.1 Traceable author statement. Source: ProtInc protein amino acid N-linked glycosylation Ref.1Traceable author statement. Source: ProtInc protein amino acid O-linked glycosylation Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | cortical cytoskeleton Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.1Traceable author statement. Source: ProtInc |
| Molecular function | protein binding Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Glycophorin-C (identifier: P04921-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Glycophorin-D (identifier: P04921-2) The sequence of this isoform differs from the canonical sequence as follows: 1-21: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 128 | 128 | Glycophorin-C | PRO_0000149050 | |||||
Regions | |||||||||
| Topological domain | 1 – 57 | 57 | Extracellular | ||||||
| Transmembrane | 58 – 81 | 24 | Anchor for type III membrane protein | ||||||
| Topological domain | 82 – 128 | 47 | Cytoplasmic | ||||||
Sites | |||||||||
| Site | 8 | 1 | Not glycosylated; in variant Webb antigen | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 3 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 4 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 6 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 8 | 1 | N-linked (GlcNAc...) Ref.12 | ||||||
| Glycosylation | 9 | 1 | O-linked (GalNAc...) Ref.12 | ||||||
| Glycosylation | 10 | 1 | O-linked (GalNAc...) Ref.12 | ||||||
| Glycosylation | 15 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 24 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 26 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 27 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 28 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 31 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 32 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 33 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
| Glycosylation | 42 | 1 | O-linked (GalNAc...) Ref.12 Ref.9 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 21 | 21 | Missing in isoform Glycophorin-D. | VSP_001777 | |||||
| Natural variant | 8 | 1 | N → S in Webb (WB) antigen. | VAR_003193 | |||||
| Natural variant | 14 | 1 | L → F in Duch (DH(a)) antigen. | VAR_003194 | |||||
| Natural variant | 23 | 1 | A → S in Ahonen (AN(a)) antigen. | VAR_003195 | |||||
| Natural variant | 124 | 1 | K → E: dbSNP rs28370000. Ref.6 | VAR_021342 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C." Colin Y., Rahuel C., London J., Romeo P.-H., D'Auriol L., Galibert F., Cartron J.-P. J. Biol. Chem. 261:229-233(1986) [PubMed: 2416746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Human erythrocyte membrane sialoglycoprotein beta. The cDNA sequence suggests the absence of a cleaved N-terminal signal sequence." High S., Tanner M.J.A. Biochem. J. 243:277-280(1987) [PubMed: 3606576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Structure of human erythrocyte glycophorin C deduced from cDNA analysis." Cartron J.-P., Colin Y., le van Kim C., Rahuel C., Blanchard D., Bloy C., London J. Rev. Fr. Transfus. Immunohematol. 29:267-285(1986) [PubMed: 3544149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [4] | "Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1,-2,3 types. Immunochemical study and genomic analysis with cDNA probes." le van Kim C., Colin Y., Blanchard D., Dahr W., London J., Cartron J.-P. Eur. J. Biochem. 165:571-579(1987) [PubMed: 3595602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [5] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN C). |
| [6] | SeattleSNPs variation discovery resource Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-124. |
| [7] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [9] | "Glycophorins B and C from human erythrocyte membranes. Purification and sequence analysis." Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K., Cartron J.-P. J. Biol. Chem. 262:5808-5811(1987) [PubMed: 3571235] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-88. |
| [10] | "Isolation and structural analysis of glycophorin C." Dahr W., Humel M., Blanchard D., Beyreuther K., Cartron J.-P. Biol. Chem. Hoppe-Seyler 366:777-778(1985) Cited for: PROTEIN SEQUENCE OF 1-87. Tissue: Blood. |
| [11] | "A revision of the N-terminal structure of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes." Dahr W., Beyreuther K. Biol. Chem. Hoppe-Seyler 366:1067-1070(1985) [PubMed: 4074499] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-48. Tissue: Blood. |
| [12] | "N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes." Dahr W., Beyreuther K., Kordowicz M., Krueger J. Eur. J. Biochem. 125:57-62(1982) [PubMed: 7106126] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-48, 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. |
| [13] | "Structural homology between glycophorins C and D of human erythrocytes." El-Maliki B., Blanchard D., Dahr W., Beyreuther K., Cartron J.-P. Eur. J. Biochem. 183:639-643(1989) [PubMed: 2776757] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 30-91. |
| [14] | "An ubiquitous isoform of glycophorin C is produced by alternative splicing." le van Kim C., Mitjavila M.T., Clerget M., Cartron J.-P., Colin Y. Nucleic Acids Res. 18:3076-3076(1990) [PubMed: 2349119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22 AND 42-128. Tissue: Spleen. |
| [15] | "Structure of the promoter region and tissue specificity of the human glycophorin C gene." le van Kim C., Colin Y., Mitjavila M.T., Clerget M., Dubart A., Nakazawa M., Vainchenker W., Cartron J.-P. J. Biol. Chem. 264:20407-20414(1989) [PubMed: 2584223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. |
| [16] | "Rearrangements of the red-cell membrane glycophorin C (sialoglycoprotein beta) gene. A further study of alterations in the glycophorin C gene." High S., Tanner M.J.A., Macdonald E.N., Anstee D.J. Biochem. J. 262:47-54(1989) [PubMed: 2818576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-128. |
| [17] | "Human erythrocyte glycophorin C. Gene structure and rearrangement in genetic variants." Colin Y., le van Kim C., Tsapis A., Clerget M., D'Auriol L., London J., Galibert F., Cartron J.-P. J. Biol. Chem. 264:3773-3780(1989) [PubMed: 2917976] [Abstract] Cited for: GENE STRUCTURE. |
| [18] | "Molecular characterization of erythrocyte glycophorin C variants." Chang S., Reid M.E., Conboy J., Kan Y.W., Mohandas N. Blood 77:644-648(1991) [PubMed: 1991173] [Abstract] Cited for: VARIANT BLOOD GROUP ANTIGEN WB. |
| [19] | "Point mutation in the glycophorin C gene results in the expression of the blood group antigen Dha." King M.J., Avent N.D., Mallinson G., Reid M.E. Vox Sang. 63:56-58(1992) [PubMed: 1413665] [Abstract] Cited for: VARIANT BLOOD GROUP ANTIGEN DH(A). |
| [20] | "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." Daniels G., King M.J., Avent N.D., Khalid G., Reid M.E., Mallinson G., Symthe J., Cedergren B. Blood 82:3198-3203(1993) [PubMed: 8219208] [Abstract] Cited for: VARIANT BLOOD GROUP ANTIGEN AN(A). |
| + | Additional computationally mapped references. |
Web resources
| dbRBC/BGMUT Blood group antigen gene mutation database |
| Wikipedia Glycophorin C entry |
| SeattleSNPs |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M11802 mRNA. Translation: AAA60023.1. M36284 mRNA. Translation: AAA52625.1. X12496 mRNA. Translation: CAA31016.1. X51973 mRNA. Translation: CAA36235.1. M28335 mRNA. Translation: AAA52574.1. AK312032 mRNA. Translation: BAG34969.1. AY838876 Genomic DNA. Translation: AAV80423.1. AC013474 Genomic DNA. Translation: AAY14660.1. BC106051 mRNA. Translation: AAI06052.1. BC104246 mRNA. Translation: AAI04247.1. BC104247 mRNA. Translation: AAI04248.1. X14242 Genomic DNA. Translation: CAA32458.1. M29662 Genomic DNA. Translation: AAA52626.1. X13890, X13892, X13893 Genomic DNA. Translation: CAA32093.1. Frameshift. | |||||||||||||
| IPI | IPI00026299. IPI00218128. | ||||||||||||
| PIR | GFHUC. A92573. | ||||||||||||
| RefSeq | NP_002092.1. NP_058131.1. | ||||||||||||
| UniGene | Hs.59138 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | P04921. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P04921. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000259254; ENSP00000259254; ENSG00000136732; Homo sapiens. [Genome view] ENST00000356887; ENSP00000349354; ENSG00000136732; Homo sapiens. [Genome view] ENST00000409836; ENSP00000386904; ENSG00000136732; Homo sapiens. [Genome view] | ||||||||||||
| GeneID | 2995. | ||||||||||||
| KEGG | hsa:2995. | ||||||||||||
| UCSC | uc002tnq.1. human. uc002tnr.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 2995. | ||||||||||||
| GeneCards | GC02P127129. | ||||||||||||
| H-InvDB | HIX0029926. | ||||||||||||
| HGNC | HGNC:4704. GYPC. | ||||||||||||
| HPA | CAB009445. HPA008965. | ||||||||||||
| MIM | 110750. gene+phenotype. | ||||||||||||
| PharmGKB | PA29082. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P04921. | ||||||||||||
| OMA | SPNSTAW. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P04921. | ||||||||||||
| Bgee | P04921. | ||||||||||||
| CleanEx | HS_GYPC. | ||||||||||||
| Genevestigator | P04921. | ||||||||||||
| GermOnline | ENSG00000136732. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003585. Neurexin-like. [Graphical view] | ||||||||||||
| SMART | SM00294. 4.1m. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 11870. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | GLPC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P04921 Secondary accession number(s): B2R522, Q53SV9, Q92642 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Blood group antigen proteins Nomenclature of blood group antigens and list of entries |
| Human cell differentiation molecules CD nomenclature of surface proteins of human leucocytes and list of entries |
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


