ID GLPA_HUMAN Reviewed; 150 AA. AC P02724; A8K3E6; Q9BS51; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 07-JUL-2009, entry version 107. DE RecName: Full=Glycophorin-A; DE AltName: Full=PAS-2; DE AltName: Full=Sialoglycoprotein alpha; DE AltName: Full=MN sialoglycoprotein; DE AltName: CD_antigen=CD235a; DE Flags: Precursor; GN Name=GYPA; Synonyms=GPA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89282822; PubMed=2734312; DOI=10.1073/pnas.86.12.4619; RA Kudo S., Fukuda M.; RT "Structural organization of glycophorin A and B genes: glycophorin B RT gene evolved by homologous recombination at Alu repeat sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4619-4623(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-145. RX MEDLINE=86149364; PubMed=3456608; DOI=10.1073/pnas.83.6.1665; RA Siebert P.D., Fukuda M.; RT "Isolation and characterization of human glycophorin A cDNA clones by RT a synthetic oligonucleotide approach: nucleotide sequence and mRNA RT structure."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1665-1669(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89061610; PubMed=3196288; RA Tate C.G., Tanner M.J.A.; RT "Isolation of cDNA clones for human erythrocyte membrane RT sialoglycoproteins alpha and delta."; RL Biochem. J. 254:743-750(1988). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=91016923; PubMed=2216775; DOI=10.1093/nar/18.19.5829; RA Jawad K., Burness T.H.; RT "The mechanism of production of multiple mRNAs for human glycophorin RT A."; RL Nucleic Acids Res. 18:5829-5836(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=95096015; PubMed=7798177; RA Kudo S., Onda M., Fukuda M.; RT "Characterization of glycophorin A transcripts: control by the common RT erythroid-specific promoter and alternative usage of different RT polyadenylation signals."; RL J. Biochem. 116:183-192(1994). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE OF 3-150. RX MEDLINE=87119742; PubMed=3809885; DOI=10.1016/S0338-4535(86)80019-8; RA Siebert P.D., Fukuda M.; RT "Molecular biological study of the structure and expression of human RT glycophorin A."; RL Rev. Fr. Transfus. Immunohematol. 29:251-266(1986). RN [9] RP NUCLEOTIDE SEQUENCE OF 23-150. RX MEDLINE=88151980; PubMed=3345758; RX DOI=10.1111/j.1432-1033.1988.tb13866.x; RA Rahuel C., London J., D'Auriol L., Mattei M.-G., Tournamille C., RA Skrzynia C., Lebouc Y., Galibert F., Cartron J.-P.; RT "Characterization of cDNA clones for human glycophorin A. Use for gene RT localization and for analysis of normal of glycophorin-A-deficient RT (Finnish type) genomic DNA."; RL Eur. J. Biochem. 172:147-153(1988). RN [10] RP PROTEIN SEQUENCE OF 20-150. RX MEDLINE=76053044; PubMed=1059087; DOI=10.1073/pnas.72.8.2964; RA Tomita M., Marchesi V.T.; RT "Amino-acid sequence and oligosaccharide attachment sites of human RT erythrocyte glycophorin."; RL Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975). RN [11] RP SEQUENCE REVISION TO 81-120. RA Furthmayr H., Galardy R., Tomita M., Marchesi V.T.; RL Submitted (JUN-1977) to the PIR data bank. RN [12] RP STRUCTURE BY NMR. RX MEDLINE=90351548; PubMed=2386609; DOI=10.1007/BF01025303; RA Dill K., Hu S.H., Berman E., Pavia A.A., Lacombe J.M.; RT "One- and two-dimensional NMR studies of the N-terminal portion of RT glycophorin A at 11.7 Tesla."; RL J. Protein Chem. 9:129-136(1990). RN [13] RP STRUCTURE BY NMR OF 81-120. RX MEDLINE=97238926; PubMed=9082985; DOI=10.1126/science.276.5309.131; RA Mackenzie K.R., Prestegard J.H., Engelman D.M.; RT "A transmembrane helix dimer: structure and implications."; RL Science 276:131-133(1997). RN [14] RP 3D-STRUCTURE MODELING OF 93-110. RX MEDLINE=97111896; PubMed=8953647; RX DOI=10.1002/(SICI)1097-0134(199611)26:3<257::AID-PROT2>3.3.CO;2-O; RA Adams P.D., Engelman D.M., Bruenger A.T.; RT "Improved prediction for the structure of the dimeric transmembrane RT domain of glycophorin A obtained through global searching."; RL Proteins 26:257-261(1996). RN [15] RP GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31; RP SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56; RP SER-63; SER-66 AND THR-69, AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=94115083; PubMed=8286855; DOI=10.1093/glycob/3.5.429; RA Pisano A., Redmond J.W., Williams K.L., Gooley A.A.; RT "Glycosylation sites identified by solid-phase Edman degradation: O- RT linked glycosylation motifs on human glycophorin A."; RL Glycobiology 3:429-435(1993). CC -!- FUNCTION: Glycophorin A is the major intrinsic membrane protein of CC the erythrocyte. The N-terminal glycosylated segment, which lies CC outside the erythrocyte membrane, has MN blood group receptors and CC also binds influenza virus. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-702665, EBI-702665; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- POLYMORPHISM: Along with GYPB, GYPA is responsible for the MNS CC blood group system. CC -!- SIMILARITY: Belongs to the glycophorin-A family. CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene CC mutation database; CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=mns"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M12857; AAA88044.1; -; mRNA. DR EMBL; AK290561; BAF83250.1; -; mRNA. DR EMBL; X08054; CAA30843.1; -; mRNA. DR EMBL; M24128; AAA52768.1; -; Genomic_DNA. DR EMBL; M24123; AAA52768.1; JOINED; Genomic_DNA. DR EMBL; M24134; AAA52768.1; JOINED; Genomic_DNA. DR EMBL; M24124; AAA52768.1; JOINED; Genomic_DNA. DR EMBL; M24126; AAA52768.1; JOINED; Genomic_DNA. DR EMBL; M24127; AAA52768.1; JOINED; Genomic_DNA. DR EMBL; L31860; AAA88051.1; -; mRNA. DR EMBL; BC005319; AAH05319.1; -; mRNA. DR EMBL; BC013328; AAH13328.1; -; mRNA. DR EMBL; X51798; CAA36095.1; -; mRNA. DR EMBL; M36281; AAA52624.1; -; mRNA. DR IPI; IPI00298800; -. DR PIR; A33931; A25131. DR RefSeq; NP_002090.2; -. DR UniGene; Hs.434973; -. DR PDB; 1AFO; NMR; -; A/B=81-120. DR PDB; 1MSR; Model; -; A/B=93-110. DR PDBsum; 1AFO; -. DR PDBsum; 1MSR; -. DR IntAct; P02724; 1. DR GlycoSuiteDB; P02724; -. DR Ensembl; ENSG00000170180; Homo sapiens. DR GeneID; 2993; -. DR GeneCards; GC04M145249; -. DR H-InvDB; HIX0004534; -. DR HGNC; HGNC:4702; GYPA. DR HPA; CAB002658; -. DR HPA; HPA014811; -. DR MIM; 111300; gene+phenotype. DR PharmGKB; PA29080; -. DR HOGENOM; P02724; -. DR HOVERGEN; P02724; -. DR ArrayExpress; P02724; -. DR Bgee; P02724; -. DR CleanEx; HS_GYPA; -. DR GermOnline; ENSG00000170180; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR InterPro; IPR001195; Glycophorin. DR InterPro; IPR018938; Glycophorin_CS. DR PANTHER; PTHR13813; Glycophorin_A_B; 1. DR Pfam; PF01102; Glycophorin_A; 1. DR PIRSF; PIRSF002466; Glycophorin; 1. DR PROSITE; PS00312; GLYCOPHORIN_A; 1. PE 1: Evidence at protein level; KW 3D-structure; Blood group antigen; Cell membrane; Complete proteome; KW Direct protein sequencing; Glycoprotein; Membrane; Polymorphism; KW Sialic acid; Signal; Transmembrane. FT SIGNAL 1 19 FT CHAIN 20 150 Glycophorin-A. FT /FTId=PRO_0000012134. FT TOPO_DOM 20 91 Extracellular. FT TRANSMEM 92 114 FT TOPO_DOM 115 150 Cytoplasmic. FT CARBOHYD 21 21 O-linked (GalNAc...). FT CARBOHYD 22 22 O-linked (GalNAc...). FT CARBOHYD 23 23 O-linked (GalNAc...). FT CARBOHYD 29 29 O-linked (GalNAc...). FT CARBOHYD 30 30 O-linked (GalNAc...). FT CARBOHYD 31 31 O-linked (GalNAc...). FT CARBOHYD 32 32 O-linked (GalNAc...). FT CARBOHYD 36 36 O-linked (GalNAc...). FT CARBOHYD 38 38 O-linked (GalNAc...). FT CARBOHYD 41 41 O-linked (GalNAc...). FT CARBOHYD 44 44 O-linked (GalNAc...). FT CARBOHYD 45 45 N-linked (GlcNAc...). FT CARBOHYD 52 52 O-linked (GalNAc...). FT CARBOHYD 56 56 O-linked (GalNAc...). FT CARBOHYD 63 63 O-linked (GalNAc...). FT CARBOHYD 66 66 O-linked (GalNAc...). FT CARBOHYD 69 69 O-linked (GalNAc...). FT VARIANT 20 20 S -> L (determines blood group M). FT /FTId=VAR_003190. FT VARIANT 24 24 G -> E (determines blood group N). FT /FTId=VAR_003191. FT CONFLICT 13 13 A -> E (in Ref. 4; CAA30843). FT CONFLICT 30 30 S -> T (in Ref. 10; AA sequence). FT CONFLICT 36 36 T -> S (in Ref. 10; AA sequence). FT CONFLICT 133 133 T -> R (in Ref. 3; AAA88044). FT HELIX 91 117 SQ SEQUENCE 150 AA; 16273 MW; 55673CCB36FA99CC CRC64; MYGKIIFVLL LSAIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ //