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Reviewed, UniProtKB/Swiss-Prot P02724 (GLPA_HUMAN)

Last modified June 16, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glycophorin-A
Alternative name(s):
    PAS-2
    Sialoglycoprotein alpha
    MN sialoglycoprotein
    CD_antigen=CD235a
Gene names
Name: GYPA
Synonyms: GPA
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   LigandSialic acid
   Molecular functionBlood group antigen
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentintegral 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 functionidentical protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-702665,EBI-702665

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.10
Chain20 – 150131Glycophorin-A
PRO_0000012134

Regions

Topological domain20 – 9172Extracellular
Transmembrane92 – 11423
Topological domain115 – 15036Cytoplasmic

Amino acid modifications

Glycosylation211O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation221O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation231O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation291O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation301O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation311O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation321O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation361O-linked (GalNAc...) Ref.15
Glycosylation381O-linked (GalNAc...) Ref.15
Glycosylation411O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation441O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation451N-linked (GlcNAc...) Ref.10 Ref.15
Glycosylation521O-linked (GalNAc...) Ref.15
Glycosylation561O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation631O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation661O-linked (GalNAc...) Ref.10 Ref.15
Glycosylation691O-linked (GalNAc...) Ref.10 Ref.15

Natural variations

Natural variant201S → L Determines blood group M.
VAR_003190
Natural variant241G → E Determines blood group N.
VAR_003191

Experimental info

Sequence conflict131A → E in CAA30843. Ref.4
Sequence conflict301S → T AA sequence Ref.10
Sequence conflict361T → S AA sequence Ref.10
Sequence conflict1331T → R in AAA88044. Ref.3

Secondary structure

... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02724-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 55673CCB36FA99CC

FASTA15016,273
        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 

« Hide

References

« Hide '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. 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: 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

M12857 mRNA. Translation: AAA88044.1.
AK290561 mRNA. Translation: BAF83250.1.
X08054 mRNA. Translation: CAA30843.1.
M24128 expand/collapse EMBL AC list , 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.
IPIIPI00298800.
PIRA25131. A33931.
RefSeqNP_002090.2.
UniGeneHs.434973

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AFONMR-A/B81-120[»]
1MSRmodel-A/B93-110[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP02724. 1 interaction.

PTM databases

GlycoSuiteDBP02724.

Genome annotation databases

EnsemblENSG00000170180. Homo sapiens. [Contig view]
GeneID2993.

Organism-specific databases

GeneCardsGC04M145249.
H-InvDBHIX0004534.
HGNCHGNC:4702. GYPA.
HPACAB002658.
HPA014811.
MIM111300. gene+phenotype.
PharmGKBPA29080.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP02724.
HOVERGENP02724.

Gene expression databases

ArrayExpressP02724.
BgeeP02724.
CleanExHS_GYPA.
GermOnlineENSG00000170180. Homo sapiens.

Family and domain databases

InterProIPR001195. Glycophorin.
IPR018938. Glycophorin_CS.
[Graphical view]
PANTHERPTHR13813. Glycophorin_A_B. 1 hit.
PfamPF01102. Glycophorin_A. 1 hit.
[Graphical view]
PIRSFPIRSF002466. Glycophorin. 1 hit.
PROSITEPS00312. GLYCOPHORIN_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameGLPA_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 4

Human chromosome 4: 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents