[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2734312 [NCBI, ExPASy, EBI, Israel, Japan] Kudo S., Fukuda M.; "Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences."; Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-145. PubMed=3456608 [NCBI, ExPASy, EBI, Israel, Japan] Siebert P.D., Fukuda M.; "Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure."; Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3196288 [NCBI, ExPASy, EBI, Israel, Japan] Tate C.G., Tanner M.J.A.; "Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta."; Biochem. J. 254:743-750(1988).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Blood; DOI=10.1093/nar/18.19.5829; PubMed=2216775 [NCBI, ExPASy, EBI, Israel, Japan] Jawad K., Burness T.H.; "The mechanism of production of multiple mRNAs for human glycophorin A."; Nucleic Acids Res. 18:5829-5836(1990).
[5]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Blood; PubMed=7798177 [NCBI, ExPASy, EBI, Israel, Japan] Kudo S., Onda M., Fukuda M.; "Characterization of glycophorin A transcripts: control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals."; J. Biochem. 116:183-192(1994).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Bone marrow, and Lung; 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).
[7]	NUCLEOTIDE SEQUENCE OF 3-150. DOI=10.1016/S0338-4535(86)80019-8; PubMed=3809885 [NCBI, ExPASy, EBI, Israel, Japan] Siebert P.D., Fukuda M.; "Molecular biological study of the structure and expression of human glycophorin A."; Rev. Fr. Transfus. Immunohematol. 29:251-266(1986).
[8]	NUCLEOTIDE SEQUENCE OF 23-150. PubMed=3345758 [NCBI, ExPASy, EBI, Israel, Japan] Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P.; "Characterization of cDNA clones for human glycophorin A. Use for gene localization and for analysis of normal of glycophorin-A-deficient (Finnish type) genomic DNA."; Eur. J. Biochem. 172:147-153(1988).
[9]	PROTEIN SEQUENCE OF 20-150. PubMed=1059087 [NCBI, ExPASy, EBI, Israel, Japan] Tomita M., Marchesi V.T.; "Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin."; Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975).
[10]	SEQUENCE REVISION TO 81-120. Furthmayr H., Galardy R., Tomita M., Marchesi V.T.; Submitted (JUN-1977) to the PIR data bank.
[11]	STRUCTURE BY NMR. DOI=10.1007/BF01025303; PubMed=2386609 [NCBI, ExPASy, EBI, Israel, Japan] Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M.; "One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla."; J. Protein Chem. 9:129-136(1990).
[12]	STRUCTURE BY NMR OF 81-120. DOI=10.1126/science.276.5309.131; PubMed=9082985 [NCBI, ExPASy, EBI, Israel, Japan] Mackenzie K.R., Prestegard J.H., Engelman D.M.; "A transmembrane helix dimer: structure and implications."; Science 276:131-133(1997).
[13]	3D-STRUCTURE MODELING OF 93-110. DOI=10.1002/(SICI)1097-0134(199611)26:3<257::AID-PROT2>3.3.CO;2-O; PubMed=8953647 [NCBI, ExPASy, EBI, Israel, Japan] Adams P.D., Engelman D.M., Bruenger A.T.; "Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching."; Proteins 26:257-261(1996).
[14]	GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31; SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56; SER-63; SER-66 AND THR-69, AND PARTIAL PROTEIN SEQUENCE. DOI=10.1093/glycob/3.5.429; PubMed=8286855 [NCBI, ExPASy, EBI, Israel, Japan] Pisano A., Redmond J.W., Williams K.L., Gooley A.A.; "Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A."; Glycobiology 3:429-435(1993).

Comments

FUNCTION: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors and also binds influenza virus.
INTERACTION:
Self; NbExp=2; IntAct=EBI-702665, EBI-702665;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
POLYMORPHISM: Along with GYPB, GYPA is responsible for the MNS blood group system.
SIMILARITY: Belongs to the glycophorin A family.
WEB RESOURCE: Name=BGMUT; Note=Blood group antigen gene mutation database"; URL="http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=mns";.

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

M12857; AAA88044.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X08054; CAA30843.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24128; AAA52768.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24123; AAA52768.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24134; AAA52768.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24124; AAA52768.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24126; AAA52768.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M24127; AAA52768.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L31860; AAA88051.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005319; AAH05319.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013328; AAH13328.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X51798; CAA36095.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36281; AAA52624.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A33931; A25131.

UniGene

Hs.434973

3D structure databases

PDB

1AFO; NMR; -; A/B=81-120.	[ExPASy / RCSB / EBI]
1MSR; Model; -; A/B=93-110.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AFO; -.
1MSR; -.

ModBase

P02724.

Protein-protein interaction databases

IntAct

P02724; -.

PTM databases

GlycoSuiteDB

P02724; -.

Organism-specific databases

HIX0004534; -.

HGNC:4702; GYPA.

CAB002658; -.
HPA014811; -.

MIM

111300; gene+phenotype. [NCBI / EBI]

PharmGKB

PA29080; -.

GeneCards

P02724.

Gene expression databases

ArrayExpress

P02724; -.

CleanEx

HS_GYPA; -.

GermOnline

ENSG00000170180; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005624;	Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0005886;	Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR016350; Glycophorin.
IPR001195; Glycophorin_A_B.
Graphical view of domain structure.

PANTHER

PTHR13813; Glycophorin_A_B; 1.

Pfam

PF01102; Glycophorin_A; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF002466; Glycophorin; 1.

PROSITE

PS00312; GLYCOPHORIN_A; 1.

ProtoNet

P02724.

Genome annotation databases

Ensembl

ENSG00000170180; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

P02724; -.

HOVERGEN

P02724; -.

Other

SOURCE

GYPA; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Blood group antigen; Direct protein sequencing; Glycoprotein; Membrane; Polymorphism; Sialic acid; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 150`	`131`	`Glycophorin-A.`	`PRO_0000012134`
`TOPO_DOM`	`20 91`	`72`	`Extracellular.`
`TRANSMEM`	`92 114`	`23`
`TOPO_DOM`	`115 150`	`36`	`Cytoplasmic.`
`CARBOHYD`	`21 21`		`O-linked (GalNAc...).`
`CARBOHYD`	`22 22`		`O-linked (GalNAc...).`
`CARBOHYD`	`23 23`		`O-linked (GalNAc...).`
`CARBOHYD`	`29 29`		`O-linked (GalNAc...).`
`CARBOHYD`	`30 30`		`O-linked (GalNAc...).`
`CARBOHYD`	`31 31`		`O-linked (GalNAc...).`
`CARBOHYD`	`32 32`		`O-linked (GalNAc...).`
`CARBOHYD`	`36 36`		`O-linked (GalNAc...).`
`CARBOHYD`	`38 38`		`O-linked (GalNAc...).`
`CARBOHYD`	`41 41`		`O-linked (GalNAc...).`
`CARBOHYD`	`44 44`		`O-linked (GalNAc...).`
`CARBOHYD`	`45 45`		`N-linked (GlcNAc...).`
`CARBOHYD`	`52 52`		`O-linked (GalNAc...).`
`CARBOHYD`	`56 56`		`O-linked (GalNAc...).`
`CARBOHYD`	`63 63`		`O-linked (GalNAc...).`
`CARBOHYD`	`66 66`		`O-linked (GalNAc...).`
`CARBOHYD`	`69 69`		`O-linked (GalNAc...).`
`VARIANT`	`20 20`	`1`	`S -> L (determines blood group M).`	`VAR_003190`
`VARIANT`	`24 24`	`1`	`G -> E (determines blood group N).`	`VAR_003191`
`CONFLICT`	`13 13`		`A -> E (in Ref. 3; CAA30843).`
`CONFLICT`	`30 30`		`S -> T (in Ref. 9; AA sequence).`
`CONFLICT`	`36 36`		`T -> S (in Ref. 9; AA sequence).`
`CONFLICT`	`133 133`		`T -> R (in Ref. 2; AAA88044).`
`HELIX`	`91 117`	`27`

Sequence information

Length: 150 AA [This is the length of the unprocessed precursor]

Molecular weight: 16273 Da [This is the MW of the unprocessed precursor]

CRC64: 55673CCB36FA99CC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYGKIIFVLL LSAIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH 

        70         80         90        100        110        120 
EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK 

       130        140        150 
SPSDVKPLPS PDTDVPLSSV EIENPETSDQ

P02724 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools