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UniProtKB/Swiss-Prot entry P02724


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GLPA_HUMAN
Primary accession number P02724
Secondary accession numbers A8K3E6 Q9BS51
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 106)
Name and origin of the protein
Protein name Glycophorin-A [Precursor]
Synonyms PAS-2
Sialoglycoprotein alpha
MN sialoglycoprotein
CD235a antigen
Gene name
Name: GYPA
Synonyms: GPA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.86.12.4619; 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 [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-145.
DOI=10.1073/pnas.83.6.1665; 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).
[4]
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).
[5]
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).
[6]
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).
[7]
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).
[8]
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).
[9]
NUCLEOTIDE SEQUENCE OF 23-150.
DOI=10.1111/j.1432-1033.1988.tb13866.x; 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).
[10]
PROTEIN SEQUENCE OF 20-150.
DOI=10.1073/pnas.72.8.2964; 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).
[11]
SEQUENCE REVISION TO 81-120.
Furthmayr H., Galardy R., Tomita M., Marchesi V.T.;
Submitted (JUN-1977) to the PIR data bank.
[12]
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).
[13]
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).
[14]
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).
[15]
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
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]
AK290561; BAF83250.1; -; 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]
IPI IPI00298800; -.
PIR A33931; A25131.
RefSeq NP_002090.2; -.
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; 1.
PTM databases
GlycoSuiteDB P02724; -.
Organism-specific databases
GeneCards GC04M145249; -.
H-InvDB HIX0004534; -.
HGNC HGNC:4702; GYPA.
GenAtlas GYPA.
HPA CAB002658; -.
HPA014811; -.
MIM 111300; gene+phenotype. [NCBI / EBI]
PharmGKB PA29080; -.
Gene expression databases
ArrayExpress P02724; -.
Bgee P02724; -.
CleanEx HS_GYPA; -.
GermOnline ENSG00000170180; Homo sapiens.
Ontologies
GO
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 IPR001195; Glycophorin.
IPR018938; Glycophorin_CS.
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.
Genome annotation databases
Ensembl ENSG00000170180; Homo sapiens. [Contig view]
GeneID 2993; -.
Phylogenomic databases
HOGENOM P02724; -.
HOVERGEN P02724; -.
Other
SOURCE GYPA; Homo sapiens.
ProtoNet P02724.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood group antigen; Cell membrane; Direct protein sequencing; Glycoprotein; Membrane; Polymorphism; Sialic acid; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   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. 4; CAA30843). 
CONFLICT   30    30        S -> T (in Ref. 10; AA sequence). 
CONFLICT   36    36        T -> S (in Ref. 10; AA sequence). 
CONFLICT   133   133        T -> R (in Ref. 3; 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

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BLAST logo BLAST submission on ExPASy/SIB
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