ID GLPA_HUMAN Reviewed; 150 AA. AC P02724; A8K3E6; Q9BS51; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 13-OCT-2009, entry version 111. 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 [MRNA], AND VARIANT ALA-13. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS N LEU-20 AND GLU-24. 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-13. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-13. 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-13. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS N LEU-20 RP AND GLU-24. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-13, AND VARIANTS N RP LEU-20 AND GLU-24. 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-145, AND VARIANT ALA-13. 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] 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 [13] RP PARTIAL PROTEIN SEQUENCE, AND VARIANT M(C) GLU-24. RX PubMed=6166001; DOI=10.1073/pnas.78.1.631; RA Furthmayr H., Metaxas M.N., Metaxas-Buhler M.; RT "Mg and Mc: mutations within the amino-terminal region of glycophorin RT A."; RL Proc. Natl. Acad. Sci. U.S.A. 78:631-635(1981). RN [14] RP PARTIAL PROTEIN SEQUENCE, AND VARIANT M(G) ASN-23. RX PubMed=6940143; DOI=10.1073/pnas.78.2.747; RA Blumenfeld O.O., Adamany A.M., Puglia K.V.; RT "Amino acid and carbohydrate structural variants of glycoprotein RT products (M-N glycoproteins) of the M-N allelic locus."; RL Proc. Natl. Acad. Sci. U.S.A. 78:747-751(1981). RN [15] RP GLYCOSYLATION. RX PubMed=5350948; RA Thomas D.B., Winzler R.J.; RT "Structural studies on human erythrocyte glycoproteins. Alkali-labile RT oligosaccharides."; RL J. Biol. Chem. 244:5943-5946(1969). RN [16] RP GLYCOSYLATION. RX PubMed=3624241; RA Fukuda M., Lauffenburger M., Sasaki H., Rogers M.E., Dell A.; RT "Structures of novel sialylated O-linked oligosaccharides isolated RT from human erythrocyte glycophorins."; RL J. Biol. Chem. 262:11952-11957(1987). RN [17] RP SUBUNIT. RX PubMed=1463744; DOI=10.1021/bi00166a003; RA Treutlein H.R., Lemmon M.A., Engelman D.M., Brunger A.T.; RT "The glycophorin A transmembrane domain dimer: sequence-specific RT propensity for a right-handed supercoil of helices."; RL Biochemistry 31:12726-12732(1992). RN [18] 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). RN [19] RP FUNCTION AS RECEPTOR FOR PLASMODIUM EBA-175. RX PubMed=8009226; DOI=10.1126/science.8009226; RA Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., Miller L.H.; RT "Receptor and ligand domains for invasion of erythrocytes by RT Plasmodium falciparum."; RL Science 264:1941-1944(1994). RN [20] RP GLYCOSYLATION (AB BLOOD GROUP ANTIGENS). RX PubMed=10912628; RA Podbielska M., Krotkiewski H.; RT "Identification of blood group A and B antigens in human RT glycophorin."; RL Arch. Immunol. Ther. Exp. 48:211-221(2000). RN [21] RP FUNCTION, AND MUTAGENESIS OF LEU-94; ILE-95; GLY-98 AND GLY-102. RX PubMed=10926825; DOI=10.1042/0264-6021:3500053; RA Young M.T., Beckmann R., Toye A.M., Tanner M.J.; RT "Red-cell glycophorin A-band 3 interactions associated with the RT movement of band 3 to the cell surface."; RL Biochem. J. 350:53-60(2000). RN [22] RP SUBUNIT. RX PubMed=11313283; DOI=10.1182/blood.V97.9.2872; RA Auffray I., Marfatia S., de Jong K., Lee G., Huang C.H., Paszty C., RA Tanner M.J., Mohandas N., Chasis J.A.; RT "Glycophorin A dimerization and band 3 interaction during erythroid RT membrane biogenesis: in vivo studies in human glycophorin A transgenic RT mice."; RL Blood 97:2872-2878(2001). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=11402026; DOI=10.1074/jbc.M101889200; RA Gerber D., Shai Y.; RT "In vivo detection of hetero-association of glycophorin-A and its RT mutants within the membrane."; RL J. Biol. Chem. 276:31229-31232(2001). RN [24] RP FUNCTION, AND MUTAGENESIS OF PHE-87; SER-88; PRO-90 AND GLU-91. RX PubMed=12813056; DOI=10.1074/jbc.M302527200; RA Young M.T., Tanner M.J.; RT "Distinct regions of human glycophorin A enhance human red cell anion RT exchanger (band 3; AE1) transport function and surface trafficking."; RL J. Biol. Chem. 278:32954-32961(2003). RN [25] RP REVIEW, AND VARIANTS. RA Reid M.E., Christine Lomas-Francis C.; RT "The blood group system."; RL (In) Reid M.E., Christine Lomas-Francis C. (eds.); RL The blood group antigen factsbook, pp.29-104, Academic Press, Oxford RL (2004). RN [26] RP GLYCOSYLATION, AND MASS SPECTROMETRY. RX PubMed=15313217; DOI=10.1016/j.abb.2004.06.018; RA Podbielska M., Fredriksson S.A., Nilsson B., Lisowska E., RA Krotkiewski H.; RT "ABH blood group antigens in O-glycans of human glycophorin A."; RL Arch. Biochem. Biophys. 429:145-153(2004). RN [27] RP FUNCTION. RX PubMed=14604989; DOI=10.1074/jbc.M309826200; RA Bruce L.J., Pan R.J., Cope D.L., Uchikawa M., Gunn R.B., Cherry R.J., RA Tanner M.J.; RT "Altered structure and anion transport properties of band 3 (AE1, RT SLC4A1) in human red cells lacking glycophorin A."; RL J. Biol. Chem. 279:2414-2420(2004). RN [28] RP FUNCTION AS RECEPTOR FOR FOR HEPATITIS A VIRUS. RX PubMed=15331714; DOI=10.1128/JVI.78.18.9807-9813.2004; RA Sanchez G., Aragones L., Costafreda M.I., Ribes E., Bosch A., RA Pinto R.M.; RT "Capsid region involved in hepatitis A virus binding to glycophorin A RT of the erythrocyte membrane."; RL J. Virol. 78:9807-9813(2004). RN [29] RP INTERACTION WITH STREPTOCOCCUS GORDONII HSA PROTEIN. RX PubMed=18380804; DOI=10.1111/j.1348-0421.2008.00015.x; RA Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., RA Konishi K.; RT "Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3- RT linked sialic acid on glycophorin A of the erythrocyte membrane."; RL Microbiol. Immunol. 52:69-77(2008). RN [30] RP FUNCTION. RX PubMed=19438409; DOI=10.1042/BJ20090345; RA Pang A.J., Reithmeier R.A.; RT "Interaction of anion exchanger 1 and glycophorin A in human RT erythroleukaemic K562 cells."; RL Biochem. J. 421:345-356(2009). RN [31] 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 [32] 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 [33] 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 [34] RP VARIANT ENEH/VW MET-47. RX MEDLINE=92305340; PubMed=1611092; RA Huang C.-H., Spruell P., Moulds J.J., Blumenfeld O.O.; RT "Molecular basis for the human erythrocyte glycophorin specifying the RT Miltenberger class I (MiI) phenotype."; RL Blood 80:257-263(1992). RN [35] RP VARIANT ENEH/HUT ANTIGEN LYS-47. RX PubMed=1421409; RA Huang C.H., Skov F., Daniels G., Tippett P., Blumenfeld O.O.; RT "Molecular analysis of human glycophorin MiIX gene shows a silent RT segment transfer and untemplated mutation resulting from gene RT conversion via sequence repeats."; RL Blood 80:2379-2387(1992). RN [36] RP VARIANT ERIK ARG-78. RX PubMed=8245024; RA Huang C.H., Reid M., Daniels G., Blumenfeld O.O.; RT "Alteration of splice site selection by an exon mutation in the human RT glycophorin A gene."; RL J. Biol. Chem. 268:25902-25908(1993). RN [37] RP VARIANT ENEP/HAG PRO-84. RX PubMed=10354388; DOI=10.1046/j.1365-3148.1999.00185.x; RA Poole J., Banks J., Bruce L.J., Ring S.M., Levene C., Stern H., RA Overbeeke M.A., Tanner M.J.; RT "Glycophorin A mutation Ala65 --> Pro gives rise to a novel pair of RT MNS alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression: RT direct evidence for GPA/band 3 interaction necessary for normal Wrb RT expression."; RL Transfus. Med. 9:167-174(1999). RN [38] RP VARIANTS NY(A) GLU-46 AND OS(A) SER-73. RX PubMed=10827258; DOI=10.1046/j.1537-2995.2000.40050555.x; RA Daniels G.L., Bruce L.J., Mawby W.J., Green C.A., Petty A., Okubo Y., RA Kornstad L., Tanner M.J.; RT "The low-frequency MNS blood group antigens Ny(a) (MNS18) and Os(a) RT (MNS38) are associated with GPA amino acid substitutions."; RL Transfusion 40:555-559(2000). RN [39] RP VARIANTS VR TYR-66 AND MT(A) ILE-77. RX PubMed=10729812; DOI=10.1159/000031149; RA Storry J.R., Coghlan G., Poole J., Figueroa D., Reid M.E.; RT "The MNS blood group antigens, Vr (MNS12) and Mt(a) (MNS14), each RT arise from an amino acid substitution on glycophorin A."; RL Vox Sang. 78:52-56(2000). 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. CC Appears to be important for the function of SLC4A1 and is required CC for high activity of SLC4A1. May be involved in translocation of CC SLC4A1 to the plasma membrane. Is a receptor for influenza virus. CC Is a receptor for Plasmodium falciparum erythrocyte-binding CC antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic CC acid residues of the O-linked glycans. Appears to be a receptor CC for Hepatitis A virus (HAV). CC -!- SUBUNIT: Homodimer. Interacts with Streptococcus gordonii hsa CC protein. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-702665, EBI-702665; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Note=Appears to be colocalized with SLC4A1. CC -!- PTM: The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1- CC 3)-[NeuAc-alpha-(2-6)]-GalNacOH (about 78 %) and NeuAc-alpha-(2- CC 3)-Gal-beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include CC NeuAc-alpha-(2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH CC NeuAc-alpha-(2-8)-NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About CC 1% of all O-linked glycans carry blood group A, B and H CC determinants. They derive from a type-2 precursor core structure, CC Gal-beta-(1,3)-GlcNAc-beta-1-R, and the antigens are synthesized CC by addition of fucose (H antigen-specific) and then N- CC acetylgalactosamine (A antigen-specific) or galactose (B antigen- CC specific). Specifically O-linked-glycans are NeuAc-alpha-(2-3)- CC Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1-2)]- CC Gal-beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and CC NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)- CC [Fuc-alpha-(1-2)]-Gal-beta (1 %, O antigen-, A antigen- and B CC antigen-specific). CC -!- POLYMORPHISM: Along with GYPB, GYPA is responsible for the MNS CC blood group system. The molecular basis of the GPA M/N bloodgroup CC antigen is a variation at positions 20 and 24. Ser-20 and Gly-24 CC correspond to M (shown); 'Leu-20' and 'Glu-24' correspond to N. CC -!- MISCELLANEOUS: Involved in several unequal homologous CC recombinations or gene conversion events, predominantly with GYPB CC and more rarely with GYPE. The resulting fusion proteins are CC observed in different phenotypes and encode low incidence CC bloodgroup antigens. 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; 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; X51798; CAA36095.1; -; mRNA. DR EMBL; L31860; AAA88051.1; -; mRNA. DR EMBL; AK290561; BAF83250.1; -; mRNA. DR EMBL; AC107223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005319; AAH05319.1; -; mRNA. DR EMBL; BC013328; AAH13328.1; -; mRNA. DR EMBL; M36281; AAA52624.1; ALT_INIT; 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 STRING; P02724; -. DR GlycoSuiteDB; P02724; -. DR Ensembl; ENST00000283126; ENSP00000283126; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000283128; ENSP00000283128; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000306959; ENSP00000306419; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000324022; ENSP00000324483; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000360771; ENSP00000354003; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000394119; ENSP00000377677; ENSG00000170180; Homo sapiens. DR Ensembl; ENST00000429670; ENSP00000394200; ENSG00000170180; Homo sapiens. DR GeneID; 2993; -. DR KEGG; hsa:2993; -. DR CTD; 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 Genevestigator; P02724; -. DR GermOnline; ENSG00000170180; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. 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; Host-virus interaction; KW Membrane; Polymorphism; 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 13 13 E -> A (in dbSNP:rs4449373). FT /FTId=VAR_058911. FT VARIANT 13 13 E -> G (in dbSNP:rs4449373). FT /FTId=VAR_059977. FT VARIANT 20 20 S -> L (in N antigen and M(g) antigen). FT /FTId=VAR_003190. FT VARIANT 23 23 T -> N (in M(g) antigen). FT /FTId=VAR_058912. FT VARIANT 24 24 G -> D (in dbSNP:rs7658293). FT /FTId=VAR_058913. FT VARIANT 24 24 G -> E (in N antigen, in M(c) antigen and FT in M(g) antigen). FT /FTId=VAR_003191. FT VARIANT 46 46 D -> E (in Ny(a) antigen). FT /FTId=VAR_058914. FT VARIANT 47 47 T -> K (in ENEH/Hut antigen). FT /FTId=VAR_058915. FT VARIANT 47 47 T -> M (in ENEH/Vw antigen). FT /FTId=VAR_058916. FT VARIANT 50 50 R -> W (in Or antigen). FT /FTId=VAR_058917. FT VARIANT 66 66 S -> Y (in Vr antigen). FT /FTId=VAR_058918. FT VARIANT 73 73 P -> S (in Os(a) antigen). FT /FTId=VAR_058919. FT VARIANT 76 76 E -> K (in Ri(a) antigen). FT /FTId=VAR_058920. FT VARIANT 77 77 T -> I (in Mt(a) antigen). FT /FTId=VAR_058921. FT VARIANT 78 78 G -> R (in ERIK antigen). FT /FTId=VAR_058922. FT VARIANT 82 82 Q -> K (in ENAV/MARS antigen). FT /FTId=VAR_058923. FT VARIANT 84 84 A -> P (in ENEP/HAG antigen). FT /FTId=VAR_058924. FT MUTAGEN 87 87 F->C: Diminishes dimerization. FT MUTAGEN 88 88 S->C: Diminishes dimerization. FT MUTAGEN 90 90 P->C: Diminishes dimerization. FT MUTAGEN 91 91 E->C: Diminishes dimerization. FT MUTAGEN 94 94 L->I: Diminishes dimerization. FT MUTAGEN 95 95 I->A: Diminishes dimerization. FT MUTAGEN 98 98 G->L: Diminishes dimerization. FT MUTAGEN 102 102 G->L: Abolishes dimerization. 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. 1; AAA88044). FT HELIX 91 117 SQ SEQUENCE 150 AA; 16331 MW; 48A5450E22FA99C9 CRC64; MYGKIIFVLL LSEIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ //