Reviewed, UniProtKB/Swiss-Prot P04921 (GLPC_HUMAN)

Names and origin

Protein names

Recommended name:
    Glycophorin-C
Alternative name(s):
    PAS-2'
    Glycoprotein beta
    GLPC
    Glycoconnectin
    Sialoglycoprotein D
    Glycophorin-D
      Short name=GPD
    CD_antigen=CD236

Gene names

Name:	GYPC
Synonyms:	GPC

Organism

Homo sapiens (Human)

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 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 Direct protein sequencing
Gene Ontology (GO)
Biological process	organ morphogenesis Ref.1 Traceable author statement. Source: ProtInc protein amino acid N-linked glycosylation Ref.1 Traceable author statement. Source: ProtInc protein amino acid O-linked glycosylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cortical cytoskeleton Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.1 Traceable 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

	Sequence		Length	Mass (Da)
	Isoform Glycophorin C [UniParc]. Last modified August 13, 1987. Version 1. Checksum: C9C654009A5642D5	FASTA	128	13,811
	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
	Isoform Glycophorin D. Checksum: B7D025DEF0555290	FASTA	107	11,499
	10 20 30 40 50 60 MASASTTMHT TTIAEPDPGM SGWPDGRMET STPTIMDIVV IAGVIAAVAI VLVSLLFVML 70 80 90 100 RYMYRHKGTY HTNEAKGTEF AESADAALQG DPALQDAGDS SRKEYFI

References

	« Hide 'large scale' referencesShow '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. , 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: 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. , 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: 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

EMBLGenBankDDBJ

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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EJY	NMR	-	B	117-128	[»]

ModBase

Search...

Proteomic databases

PRIDE

P04921.

Genome annotation databases

Ensembl

ENSG00000136732. Homo sapiens. [Contig view]

GeneID

2995.

KEGG

hsa:2995.

Organism-specific databases

GeneCards

GC02P127129.

H-InvDB

HIX0029926.

HGNC

HGNC:4704. GYPC.

HPA

CAB009445.
HPA008965.

MIM

110750. gene+phenotype.

PharmGKB

PA29082.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04921.

HOVERGEN

P04921.

OMA

P04921. SPNSTAW.

Gene expression databases

ArrayExpress

P04921.

Bgee

P04921.

CleanEx

HS_GYPC.

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

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)