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P04921 (GLPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycophorin-C
Alternative name(s):
Glycoconnectin
Glycophorin-D
Short name=GPD
Glycoprotein beta
PAS-2'
Sialoglycoprotein D
CD_antigen=CD236
Gene names
Name:GYPC
Synonyms:GLPC, GPC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Protein existenceEvidence 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 and IsoGPC are ubiquitously expressed. Ref.5

Post-translational modification

O-glycosylated with core 1 or possibly core 8 glycans. Ref.13 Ref.20

Polymorphism

GYPC is responsible for the Gerbich blood group system. Deletion of exon 3 in GYPC changes the serologic phenotype of the Gerbich blood group system, resulting in Ge negativity. Ge negative individuals are protected against severe malaria due to erythrocytes resistance to Plasmodium falciparum invasion [MIM:611162].

Sequence similarities

Belongs to the glycophorin-C family.

Sequence caution

The sequence CAA32093.1 differs from that shown. Reason: Frameshift at position 35.

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: P04921-3)

Also known as: IsoGPC;

The sequence of this isoform differs from the canonical sequence as follows:
     18-36: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 128128Glycophorin-C
PRO_0000149050

Regions

Topological domain1 – 5757Extracellular
Transmembrane58 – 8124Helical; Signal-anchor for type III membrane protein
Topological domain82 – 12847Cytoplasmic

Sites

Site81Not glycosylated; in variant Webb antigen

Amino acid modifications

Modified residue1041Phosphoserine Ref.19
Glycosylation31O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation41O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation61O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation81N-linked (GlcNAc...) Ref.13
Glycosylation91O-linked (GalNAc...) Ref.13
Glycosylation101O-linked (GalNAc...) Ref.13
Glycosylation151O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation241O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation261O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation271O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation281O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation311O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation321O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation331O-linked (GalNAc...) Ref.10 Ref.13
Glycosylation421O-linked (GalNAc...) Ref.10 Ref.13 Ref.20

Natural variations

Alternative sequence1 – 2121Missing in isoform Glycophorin-D.
VSP_001777
Alternative sequence18 – 3619Missing in isoform 3.
VSP_054790
Natural variant81N → S in Webb (WB) antigen.
VAR_003193
Natural variant141L → F in Duch (DH(a)) antigen.
VAR_003194
Natural variant231A → S in Ahonen (AN(a)) antigen.
VAR_003195
Natural variant1241K → E. Ref.7
Corresponds to variant rs28370000 [ dbSNP | Ensembl ].
VAR_021342

Sequences

Sequence LengthMass (Da)Tools
Isoform Glycophorin-C [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: C9C654009A5642D5

FASTA12813,811
        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 

« Hide

Isoform Glycophorin-D [UniParc].

Checksum: B7D025DEF0555290
Show »

FASTA10711,499
Isoform 3 (IsoGPC) [UniParc].

Checksum: 226D848E8D619180
Show »

FASTA10911,910

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYCOPHORIN-C).
Tissue: Liver.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Spleen.
[6]"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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN-C).
[7]SeattleSNPs variation discovery resource
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-124.
[8]"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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYCOPHORIN-C).
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 49-88.
[11]"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.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-48.
Tissue: Blood.
[13]"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] [Europe PMC] [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.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-91.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE.
[18]"Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations."
Maier A.G., Duraisingh M.T., Reeder J.C., Patel S.S., Kazura J.W., Zimmerman P.A., Cowman A.F.
Nat. Med. 9:87-92(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, INVOLVEMENT IN PROTECTION AGAINST MALARIA.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-42, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP ANTIGEN WB.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP ANTIGEN DH(A).
[23]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
M11802 mRNA. Translation: AAA60023.1.
M36284 mRNA. Translation: AAA52625.1.
X12496 mRNA. Translation: CAA31016.1.
M28335 mRNA. Translation: AAA52574.1.
X51973 mRNA. Translation: CAA36235.1.
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.
CCDSCCDS2136.1. [P04921-1]
CCDS58724.1. [P04921-2]
PIRGFHUC. A92573.
RefSeqNP_001243513.1. NM_001256584.1. [P04921-2]
NP_002092.1. NM_002101.4. [P04921-1]
NP_058131.1. NM_016815.3. [P04921-3]
UniGeneHs.59138.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJYNMR-B117-126[»]
ProteinModelPortalP04921.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109250. 1 interaction.
IntActP04921. 1 interaction.
MINTMINT-1527497.
STRING9606.ENSP00000259254.

PTM databases

PhosphoSiteP04921.

Polymorphism databases

DMDM121407.

Proteomic databases

PaxDbP04921.
PRIDEP04921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259254; ENSP00000259254; ENSG00000136732. [P04921-1]
ENST00000356887; ENSP00000349354; ENSG00000136732. [P04921-2]
ENST00000409836; ENSP00000386904; ENSG00000136732.
GeneID2995.
KEGGhsa:2995.
UCSCuc002tnq.4. human. [P04921-1]

Organism-specific databases

CTD2995.
GeneCardsGC02P127413.
HGNCHGNC:4704. GYPC.
HPACAB009445.
HPA008965.
MIM110750. gene+phenotype.
611162. phenotype.
neXtProtNX_P04921.
Orphanet98864. Common hereditary elliptocytosis.
PharmGKBPA29082.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146330.
HOGENOMHOG000112742.
HOVERGENHBG094619.
InParanoidP04921.
KOK06576.
OMAMHTTTIA.
OrthoDBEOG7VDXSF.
PhylomeDBP04921.
TreeFamTF337016.

Gene expression databases

ArrayExpressP04921.
BgeeP04921.
CleanExHS_GYPC.
GenevestigatorP04921.

Family and domain databases

InterProIPR003585. Neurexin-like.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04921.
GenomeRNAi2995.
NextBio11870.
PROP04921.
SOURCESearch...

Entry information

Entry nameGLPC_HUMAN
AccessionPrimary (citable) accession number: P04921
Secondary accession number(s): B2R522, Q53SV9, Q92642
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries