Reviewed, UniProtKB/Swiss-Prot P02724 (GLPA_HUMAN)

Names and origin

Protein names

Recommended name:
    Glycophorin-A
Alternative name(s):
    PAS-2
    Sialoglycoprotein alpha
    MN sialoglycoprotein
    CD_antigen=CD235a

Gene names

Name:	GYPA
Synonyms:	GPA

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	150 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Polymorphism	Along with GYPB, GYPA is responsible for the MNS blood group system.
Sequence similarities	Belongs to the glycophorin A family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Ligand	Sialic acid
Molecular function	Blood group antigen
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Ref.3 Traceable author statement. Source: ProtInc plasma membrane Traceable author statement. Source: ProtInc
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-702665,EBI-702665

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.10

Chain

20 – 150

131

Glycophorin-A

PRO_0000012134

Regions

Topological domain

20 – 91

72

Extracellular

Transmembrane

92 – 114

23

Topological domain

115 – 150

36

Cytoplasmic

Amino acid modifications

Glycosylation

21

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

22

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

23

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

29

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

30

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

31

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

32

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

36

1

O-linked (GalNAc...) Ref.15

Glycosylation

38

1

O-linked (GalNAc...) Ref.15

Glycosylation

41

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

44

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

45

1

N-linked (GlcNAc...) Ref.10 Ref.15

Glycosylation

52

1

O-linked (GalNAc...) Ref.15

Glycosylation

56

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

63

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

66

1

O-linked (GalNAc...) Ref.10 Ref.15

Glycosylation

69

1

O-linked (GalNAc...) Ref.10 Ref.15

Natural variations

Natural variant

20

1

S → L Determines blood group M.

VAR_003190

Natural variant

24

1

G → E Determines blood group N.

VAR_003191

Experimental info

Sequence conflict

13

1

A → E in CAA30843. Ref.4

Sequence conflict

30

1

S → T AA sequence Ref.10

Sequence conflict

36

1

T → S AA sequence Ref.10

Sequence conflict

133

1

T → R in AAA88044. Ref.3

Secondary structure

1

.

.

.

150

Helix Strand Turn

Details...

Helix

91 – 117

27

Sequences

	Sequence		Length	Mass (Da)
	P02724-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 55673CCB36FA99CC	FASTA	150	16,273
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural organization of glycophorin A and B genes: glycophorin B gene evolved by homologous recombination at Alu repeat sequences." Kudo S., Fukuda M. Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989) [PubMed: 2734312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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]. Tissue: Kidney.
[3]	"Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure." Siebert P.D., Fukuda M. Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986) [PubMed: 3456608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-145.
[4]	"Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins alpha and delta." Tate C.G., Tanner M.J.A. Biochem. J. 254:743-750(1988) [PubMed: 3196288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"The mechanism of production of multiple mRNAs for human glycophorin A." Jawad K., Burness T.H. Nucleic Acids Res. 18:5829-5836(1990) [PubMed: 2216775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[6]	"Characterization of glycophorin A transcripts: control by the common erythroid-specific promoter and alternative usage of different polyadenylation signals." Kudo S., Onda M., Fukuda M. J. Biochem. 116:183-192(1994) [PubMed: 7798177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[7]	"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]. Tissue: Bone marrow and Lung.
[8]	"Molecular biological study of the structure and expression of human glycophorin A." Siebert P.D., Fukuda M. Rev. Fr. Transfus. Immunohematol. 29:251-266(1986) [PubMed: 3809885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 3-150.
[9]	"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." Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P. Eur. J. Biochem. 172:147-153(1988) [PubMed: 3345758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 23-150.
[10]	"Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin." Tomita M., Marchesi V.T. Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975) [PubMed: 1059087] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-150.
[11]	Furthmayr H., Galardy R., Tomita M., Marchesi V.T. Submitted (JUN-1977) to the PIR data bank Cited for: SEQUENCE REVISION TO 81-120.
[12]	"One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla." Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M. J. Protein Chem. 9:129-136(1990) [PubMed: 2386609] [Abstract] Cited for: STRUCTURE BY NMR.
[13]	"A transmembrane helix dimer: structure and implications." Mackenzie K.R., Prestegard J.H., Engelman D.M. Science 276:131-133(1997) [PubMed: 9082985] [Abstract] Cited for: STRUCTURE BY NMR OF 81-120.
[14]	"Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching." Adams P.D., Engelman D.M., Bruenger A.T. Proteins 26:257-261(1996) [PubMed: 8953647] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 93-110.
[15]	"Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A." Pisano A., Redmond J.W., Williams K.L., Gooley A.A. Glycobiology 3:429-435(1993) [PubMed: 8286855] [Abstract] Cited for: 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, PARTIAL PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Cross-references

Sequence databases

EMBLGenBankDDBJ

M12857 mRNA. Translation: AAA88044.1.
AK290561 mRNA. Translation: BAF83250.1.
X08054 mRNA. Translation: CAA30843.1.
M24128 , M24123, M24134, M24124, M24126, M24127 Genomic DNA. Translation: AAA52768.1.
L31860 mRNA. Translation: AAA88051.1.
BC005319 mRNA. Translation: AAH05319.1.
BC013328 mRNA. Translation: AAH13328.1.
X51798 mRNA. Translation: CAA36095.1.
M36281 mRNA. Translation: AAA52624.1.

IPI

IPI00298800.

PIR

A25131. A33931.

RefSeq

NP_002090.2.

UniGene

Hs.434973

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFO	NMR	-	A/B	81-120	[»]
1MSR	model	-	A/B	93-110	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02724. 1 interaction.

PTM databases

GlycoSuiteDB

P02724.

Genome annotation databases

Ensembl

ENSG00000170180. Homo sapiens. [Contig view]

GeneID

2993.

Organism-specific databases

GeneCards

GC04M145249.

H-InvDB

HIX0004534.

HGNC

HGNC:4702. GYPA.

HPA

CAB002658.
HPA014811.

MIM

111300. gene+phenotype.

PharmGKB

PA29080.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02724.

HOVERGEN

P02724.

Gene expression databases

ArrayExpress

P02724.

Bgee

P02724.

CleanEx

HS_GYPA.

GermOnline

ENSG00000170180. Homo sapiens.

Family and domain databases

InterPro

IPR001195. Glycophorin.
IPR018938. Glycophorin_CS.
[Graphical view]

PANTHER

PTHR13813. Glycophorin_A_B. 1 hit.

Pfam

PF01102. Glycophorin_A. 1 hit.
[Graphical view]

PIRSF

PIRSF002466. Glycophorin. 1 hit.

PROSITE

PS00312. GLYCOPHORIN_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

GLPA_HUMAN

Accession

Primary (citable) accession number: P02724
Secondary accession number(s): A8K3E6, Q9BS51

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)