ID GLPA_HUMAN Reviewed; 150 AA. AC P02724; A8K3E6; B8Q182; B8Q185; Q9BS51; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 27-MAR-2024, entry version 231. DE RecName: Full=Glycophorin-A {ECO:0000305}; DE AltName: Full=MN sialoglycoprotein; DE AltName: Full=PAS-2; DE AltName: Full=Sialoglycoprotein alpha; DE AltName: CD_antigen=CD235a; DE Flags: Precursor; GN Name=GYPA {ECO:0000312|HGNC:HGNC:4702}; Synonyms=GPA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-13. RX 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 a RT 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] (ISOFORM 1), AND VARIANTS N LEU-20 AND GLU-24. RX PubMed=3196288; DOI=10.1042/bj2540743; RA Tate C.G., Tanner M.J.A.; RT "Isolation of cDNA clones for human erythrocyte membrane sialoglycoproteins RT alpha and delta."; RL Biochem. J. 254:743-750(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-13. RX 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 gene RT 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] (ISOFORM 1), AND VARIANT ALA-13. RC TISSUE=Blood; RX 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 A."; RL Nucleic Acids Res. 18:5829-5836(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-13. RC TISSUE=Blood; RX PubMed=7798177; DOI=10.1093/oxfordjournals.jbchem.a124492; 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 [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Blood; RA Hsu K., Huang S.-Y., Chi N., Lin M.; RT "Extensive alternative splicing of glycophorins in Southeast Asian RT populations."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS N LEU-20 AND RP 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-13, AND RP VARIANTS N 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-145 (ISOFORM 1), AND VARIANT ALA-13. RX 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 [11] RP PROTEIN SEQUENCE OF 20-150. RX 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 [12] 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 [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-150. RX PubMed=3345758; 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 (Finnish RT type) genomic DNA."; RL Eur. J. Biochem. 172:147-153(1988). RN [14] 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 A."; RL Proc. Natl. Acad. Sci. U.S.A. 78:631-635(1981). RN [15] 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 products RT (M-N glycoproteins) of the M-N allelic locus."; RL Proc. Natl. Acad. Sci. U.S.A. 78:747-751(1981). RN [16] RP GLYCOSYLATION. RX PubMed=5350948; DOI=10.1016/s0021-9258(18)63563-x; 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 [17] RP POLYMORPHISM, AND INVOLVEMENT IN RESISTANCE TO MALARIA. RX PubMed=7040988; DOI=10.1038/297064a0; RA Pasvol G., Wainscoat J.S., Weatherall D.J.; RT "Erythrocytes deficiency in glycophorin resist invasion by the malarial RT parasite Plasmodium falciparum."; RL Nature 297:64-66(1982). RN [18] RP GLYCOSYLATION. RX PubMed=3624241; DOI=10.1016/s0021-9258(18)45301-x; RA Fukuda M., Lauffenburger M., Sasaki H., Rogers M.E., Dell A.; RT "Structures of novel sialylated O-linked oligosaccharides isolated from RT human erythrocyte glycophorins."; RL J. Biol. Chem. 262:11952-11957(1987). RN [19] 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 propensity RT for a right-handed supercoil of helices."; RL Biochemistry 31:12726-12732(1992). RN [20] RP GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31; SER-32; RP THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56; SER-63; SER-66 AND RP THR-69, AND PARTIAL PROTEIN SEQUENCE. RX 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-linked RT glycosylation motifs on human glycophorin A."; RL Glycobiology 3:429-435(1993). RN [21] RP FUNCTION AS RECEPTOR FOR P.FALCIPARUM 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 Plasmodium RT falciparum."; RL Science 264:1941-1944(1994). RN [22] 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 glycophorin."; RL Arch. Immunol. Ther. Exp. 48:211-221(2000). RN [23] RP FUNCTION, AND MUTAGENESIS OF LEU-94; ILE-95; GLY-98 AND GLY-102. RX PubMed=10926825; DOI=10.1042/bj3500053; RA Young M.T., Beckmann R., Toye A.M., Tanner M.J.; RT "Red-cell glycophorin A-band 3 interactions associated with the movement of RT band 3 to the cell surface."; RL Biochem. J. 350:53-60(2000). RN [24] 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 [25] 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 mutants RT within the membrane."; RL J. Biol. Chem. 276:31229-31232(2001). RN [26] 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 [27] 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 [28] RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15313217; DOI=10.1016/j.abb.2004.06.018; RA Podbielska M., Fredriksson S.A., Nilsson B., Lisowska E., Krotkiewski H.; RT "ABH blood group antigens in O-glycans of human glycophorin A."; RL Arch. Biochem. Biophys. 429:145-153(2004). RN [29] 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, SLC4A1) RT in human red cells lacking glycophorin A."; RL J. Biol. Chem. 279:2414-2420(2004). RN [30] RP FUNCTION AS RECEPTOR 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., Pinto R.M.; RT "Capsid region involved in hepatitis A virus binding to glycophorin A of RT the erythrocyte membrane."; RL J. Virol. 78:9807-9813(2004). RN [31] RP INTERACTION WITH STREPTOCOCCUS GORDONII HSA PROTEIN (MICROBIAL INFECTION). 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-linked RT sialic acid on glycophorin A of the erythrocyte membrane."; RL Microbiol. Immunol. 52:69-77(2008). RN [32] 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 [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133; SER-138 AND SER-148, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [34] RP INTERACTION WITH P.FALCIPARUM MSP1 (MICROBIAL INFECTION). RX PubMed=25778531; DOI=10.1182/blood-2014-11-611707; RA Baldwin M.R., Li X., Hanada T., Liu S.C., Chishti A.H.; RT "Merozoite surface protein 1 recognition of host glycophorin A mediates RT malaria parasite invasion of red blood cells."; RL Blood 125:2704-2711(2015). RN [35] RP STRUCTURE BY NMR. RX 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 [36] RP STRUCTURE BY NMR OF 81-120. RX 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 [37] RP 3D-STRUCTURE MODELING OF 93-110. RX PubMed=8953647; RX DOI=10.1002/(sici)1097-0134(199611)26:3<257::aid-prot2>3.0.co;2-b; RA Adams P.D., Engelman D.M., Bruenger A.T.; RT "Improved prediction for the structure of the dimeric transmembrane domain RT of glycophorin A obtained through global searching."; RL Proteins 26:257-261(1996). RN [38] {ECO:0007744|PDB:7UZ3, ECO:0007744|PDB:7V07, ECO:0007744|PDB:7V0K, ECO:0007744|PDB:7V19, ECO:0007744|PDB:8CRQ, ECO:0007744|PDB:8CRR, ECO:0007744|PDB:8CRT, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL, ECO:0007744|PDB:8CT3, ECO:0007744|PDB:8CTE} RP STRUCTURE BY ELECTRON MICROSCOPY (2.35 ANGSTROMS), FUNCTION, SUBUNIT, RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH SLC4A1. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). RN [39] RP VARIANT ENEH/VW MET-47. RX 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 [40] 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 segment RT transfer and untemplated mutation resulting from gene conversion via RT sequence repeats."; RL Blood 80:2379-2387(1992). RN [41] RP VARIANT ERIK ARG-78. RX PubMed=8245024; DOI=10.1016/s0021-9258(19)74472-x; 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 [42] 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 MNS RT alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression: direct RT evidence for GPA/band 3 interaction necessary for normal Wrb expression."; RL Transfus. Med. 9:167-174(1999). RN [43] RP VARIANTS GLU-46 AND 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) (MNS38) RT are associated with GPA amino acid substitutions."; RL Transfusion 40:555-559(2000). RN [44] RP VARIANTS TYR-66 AND 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 arise RT from an amino acid substitution on glycophorin A."; RL Vox Sang. 78:52-56(2000). CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex CC involved in the stability and shape of the erythrocyte membrane CC (PubMed:35835865). Glycophorin A is the major intrinsic membrane CC protein of the erythrocyte. The N-terminal glycosylated segment, which CC lies outside the erythrocyte membrane, has MN blood group receptors. CC Appears to be important for the function of SLC4A1 and is required for CC high activity of SLC4A1. May be involved in translocation of SLC4A1 to CC the plasma membrane. {ECO:0000269|PubMed:10926825, CC ECO:0000269|PubMed:12813056, ECO:0000269|PubMed:14604989, CC ECO:0000269|PubMed:19438409, ECO:0000269|PubMed:35835865}. CC -!- FUNCTION: (Microbial infection) Appears to be a receptor for Hepatitis CC A virus (HAV). {ECO:0000269|PubMed:15331714}. CC -!- FUNCTION: (Microbial infection) Receptor for P.falciparum erythrocyte- CC binding antigen 175 (EBA-175); binding of EBA-175 is dependent on CC sialic acid residues of the O-linked glycans. CC {ECO:0000269|PubMed:8009226}. CC -!- SUBUNIT: Homodimer (PubMed:11313283, PubMed:1463744, PubMed:35835865). CC Component of the ankyrin-1 complex in the erythrocyte, composed of CC ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 (PubMed:35835865). CC Interacts with SLC4A1; a GYPA monomer is bound at each end of the CC SLC4A1 dimer forming an heterotetramer (PubMed:35835865). CC {ECO:0000269|PubMed:11313283, ECO:0000269|PubMed:1463744, CC ECO:0000269|PubMed:35835865}. CC -!- SUBUNIT: (Microbial infection) Interacts with Streptococcus gordonii CC hsa protein. {ECO:0000269|PubMed:18380804}. CC -!- SUBUNIT: (Microbial infection) Interacts (in a sialic acid-independent CC manner) with P.falciparum MSP1 subunit p83. CC {ECO:0000269|PubMed:25778531}. CC -!- INTERACTION: CC P02724; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-702665, EBI-17439331; CC P02724; O00501: CLDN5; NbExp=3; IntAct=EBI-702665, EBI-18400628; CC P02724; Q15125: EBP; NbExp=3; IntAct=EBI-702665, EBI-3915253; CC P02724; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-702665, EBI-18535450; CC P02724; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-702665, EBI-781551; CC P02724; Q9H8M9: EVA1A; NbExp=3; IntAct=EBI-702665, EBI-715362; CC P02724; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-702665, EBI-18304435; CC P02724; O15552: FFAR2; NbExp=3; IntAct=EBI-702665, EBI-2833872; CC P02724; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-702665, EBI-17231387; CC P02724; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-702665, EBI-13067820; CC P02724; Q8TED1: GPX8; NbExp=3; IntAct=EBI-702665, EBI-11721746; CC P02724; P02724: GYPA; NbExp=4; IntAct=EBI-702665, EBI-702665; CC P02724; Q13651: IL10RA; NbExp=3; IntAct=EBI-702665, EBI-1031656; CC P02724; Q14145: KEAP1; NbExp=4; IntAct=EBI-702665, EBI-751001; CC P02724; Q13571: LAPTM5; NbExp=3; IntAct=EBI-702665, EBI-2865663; CC P02724; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-702665, EBI-716063; CC P02724; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-702665, EBI-3920694; CC P02724; O43765: SGTA; NbExp=3; IntAct=EBI-702665, EBI-347996; CC P02724; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-702665, EBI-744081; CC P02724; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-702665, EBI-18159983; CC P02724; P02730: SLC4A1; NbExp=5; IntAct=EBI-702665, EBI-7576138; CC P02724; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-702665, EBI-12947623; CC P02724; P55061: TMBIM6; NbExp=3; IntAct=EBI-702665, EBI-1045825; CC P02724; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-702665, EBI-8638294; CC P02724; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-702665, EBI-13329239; CC P02724; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-702665, EBI-10982110; CC P02724; V9XTM1: EBA-175; Xeno; NbExp=2; IntAct=EBI-702665, EBI-25648284; CC P02724; Q9N9G9: EBP; Xeno; NbExp=2; IntAct=EBI-702665, EBI-25648255; CC P02724; Q8IBE8: PF3D7_0731500; Xeno; NbExp=2; IntAct=EBI-702665, EBI-781633; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11402026}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:11402026}. CC Note=Appears to be colocalized with SLC4A1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P02724-1; Sequence=Displayed; CC Name=2; CC IsoId=P02724-2; Sequence=VSP_047822; CC Name=3; CC IsoId=P02724-3; Sequence=VSP_047823; CC -!- PTM: The major O-linked glycan are NeuAc-alpha-(2-3)-Gal-beta-(1-3)- CC [NeuAc-alpha-(2-6)]-GalNAcOH (about 78 %) and NeuAc-alpha-(2-3)-Gal- CC beta-(1-3)-GalNAcOH (17 %). Minor O-glycans (5 %) include NeuAc-alpha- CC (2-3)-Gal-beta-(1-3)-[NeuAc-alpha-(2-6)]-GalNAcOH NeuAc-alpha-(2-8)- CC NeuAc-alpha-(2-3)-Gal-beta-(1-3)-GalNAcOH. About 1% of all O-linked CC glycans carry blood group A, B and H determinants. They derive from a CC type-2 precursor core structure, Gal-beta-(1,3)-GlcNAc-beta-1-R, and CC the antigens are synthesized by addition of fucose (H antigen-specific) CC and then N-acetylgalactosamine (A antigen-specific) or galactose (B CC antigen-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)]-Gal- CC beta-(3-1)-GalNAc-alpha (about 1%, B antigen-specific) and NeuAc-alpha- CC (2-3)-Gal-beta-(1-3)-GalNAcOH-(6-1)-GlcNAc-beta-(4-1)-[Fuc-alpha-(1- CC 2)]-Gal-beta (1 %, O antigen-, A antigen- and B antigen-specific). CC {ECO:0000269|PubMed:10912628, ECO:0000269|PubMed:15313217, CC ECO:0000269|PubMed:3624241, ECO:0000269|PubMed:5350948, CC ECO:0000269|PubMed:8286855}. CC -!- POLYMORPHISM: Along with GYPB, GYPA is responsible for the MNS blood CC group system [MIM:111300]. The molecular basis of the GPA M/N CC bloodgroup antigen is a variation at positions 20 and 24. Ser-20 and CC Gly-24 correspond to M (shown); 'Leu-20' and 'Glu-24' correspond to N. CC -!- POLYMORPHISM: GYPA polymorphisms are involved in resistance to malaria CC [MIM:611162]. CC -!- MISCELLANEOUS: Involved in several unequal homologous recombinations or CC gene conversion events, predominantly with GYPB and more rarely with CC GYPE. The resulting fusion proteins are observed in different CC phenotypes and encode low incidence bloodgroup antigens. CC -!- SIMILARITY: Belongs to the glycophorin A family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA52624.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation CC database; CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=mns"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; EU338231; ACA96789.1; -; mRNA. DR EMBL; EU338233; ACA96791.1; -; mRNA. DR EMBL; EU338234; ACA96792.1; -; mRNA. DR EMBL; GU347002; ADU25340.1; -; mRNA. DR EMBL; GU347003; ADU25341.1; -; 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 CCDS; CCDS34069.1; -. [P02724-1] DR CCDS; CCDS82959.1; -. [P02724-3] DR PIR; A33931; A25131. DR RefSeq; NP_001295119.1; NM_001308190.1. [P02724-3] DR RefSeq; NP_002090.4; NM_002099.7. DR RefSeq; XP_016863624.1; XM_017008135.1. [P02724-2] DR PDB; 1AFO; NMR; -; A/B=81-120. DR PDB; 2KPE; NMR; -; A/B=89-117. DR PDB; 2KPF; NMR; -; A/B=80-117. DR PDB; 5EH4; X-ray; 2.81 A; A/B/C/D=89-117. DR PDB; 5EH6; X-ray; 1.92 A; A=89-117. DR PDB; 7UZ3; EM; 2.35 A; B/D=1-150. DR PDB; 7V07; EM; 2.80 A; B/D=1-150. DR PDB; 7V0K; EM; 2.40 A; D/N=1-150. DR PDB; 7V19; EM; 3.30 A; B/D=1-150. DR PDB; 8CRQ; EM; 3.20 A; B/D=1-150. DR PDB; 8CRR; EM; 3.00 A; B/D=1-150. DR PDB; 8CRT; EM; 3.00 A; B/D=1-150. DR PDB; 8CS9; EM; 2.74 A; R/S/T/a/b/c=1-150. DR PDB; 8CSL; EM; 25.00 A; R/S/T/a/b/c=1-150. DR PDB; 8CT3; EM; 3.30 A; B/D=1-150. DR PDB; 8CTE; EM; 2.90 A; D/N=1-150. DR PDBsum; 1AFO; -. DR PDBsum; 2KPE; -. DR PDBsum; 2KPF; -. DR PDBsum; 5EH4; -. DR PDBsum; 5EH6; -. DR PDBsum; 7UZ3; -. DR PDBsum; 7V07; -. DR PDBsum; 7V0K; -. DR PDBsum; 7V19; -. DR PDBsum; 8CRQ; -. DR PDBsum; 8CRR; -. DR PDBsum; 8CRT; -. DR PDBsum; 8CS9; -. DR PDBsum; 8CSL; -. DR PDBsum; 8CT3; -. DR PDBsum; 8CTE; -. DR AlphaFoldDB; P02724; -. DR BMRB; P02724; -. DR EMDB; EMD-26874; -. DR EMDB; EMD-26940; -. DR EMDB; EMD-26943; -. DR EMDB; EMD-26954; -. DR EMDB; EMD-26955; -. DR EMDB; EMD-26956; -. DR EMDB; EMD-26958; -. DR EMDB; EMD-26960; -. DR EMDB; EMD-26965; -. DR EMDB; EMD-26979; -. DR EMDB; EMD-26988; -. DR SMR; P02724; -. DR BioGRID; 109248; 185. DR IntAct; P02724; 43. DR STRING; 9606.ENSP00000354003; -. DR BindingDB; P02724; -. DR ChEMBL; CHEMBL5806; -. DR TCDB; 8.A.168.1.1; the glycophorin (gph) family. DR GlyConnect; 187; 2 N-Linked glycans, 14 O-Linked glycans (1 site). DR GlyConnect; 188; 4 O-Linked glycans. DR GlyConnect; 189; 7 O-Linked glycans (1 site). DR GlyCosmos; P02724; 18 sites, 29 glycans. DR GlyGen; P02724; 19 sites, 4 N-linked glycans (1 site), 26 O-linked glycans (18 sites). DR iPTMnet; P02724; -. DR PhosphoSitePlus; P02724; -. DR BioMuta; GYPA; -. DR DMDM; 259016238; -. DR jPOST; P02724; -. DR MassIVE; P02724; -. DR PaxDb; 9606-ENSP00000354003; -. DR PeptideAtlas; P02724; -. DR ProteomicsDB; 51556; -. [P02724-1] DR ProteomicsDB; 7281; -. DR ProteomicsDB; 7282; -. DR Pumba; P02724; -. DR ABCD; P02724; 17 sequenced antibodies. DR Antibodypedia; 3054; 2241 antibodies from 47 providers. DR DNASU; 2993; -. DR Ensembl; ENST00000324022.14; ENSP00000324483.10; ENSG00000170180.22. [P02724-3] DR Ensembl; ENST00000642713.1; ENSP00000494092.1; ENSG00000170180.22. [P02724-2] DR Ensembl; ENST00000646447.1; ENSP00000495922.1; ENSG00000170180.22. [P02724-2] DR GeneID; 2993; -. DR KEGG; hsa:2993; -. DR UCSC; uc003ijo.5; human. [P02724-1] DR AGR; HGNC:4702; -. DR CTD; 2993; -. DR DisGeNET; 2993; -. DR GeneCards; GYPA; -. DR HGNC; HGNC:4702; GYPA. DR HPA; ENSG00000170180; Tissue enriched (bone). DR MalaCards; GYPA; -. DR MIM; 111300; phenotype. DR MIM; 611162; phenotype. DR MIM; 617922; gene. DR neXtProt; NX_P02724; -. DR OpenTargets; ENSG00000170180; -. DR PharmGKB; PA29080; -. DR VEuPathDB; HostDB:ENSG00000170180; -. DR eggNOG; ENOG502THAT; Eukaryota. DR GeneTree; ENSGT00550000075214; -. DR HOGENOM; CLU_154690_2_1_1; -. DR InParanoid; P02724; -. DR OrthoDB; 5232857at2759; -. DR PhylomeDB; P02724; -. DR TreeFam; TF338555; -. DR PathwayCommons; P02724; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; P02724; -. DR SIGNOR; P02724; -. DR BioGRID-ORCS; 2993; 11 hits in 1142 CRISPR screens. DR ChiTaRS; GYPA; human. DR EvolutionaryTrace; P02724; -. DR GeneWiki; GYPA; -. DR GenomeRNAi; 2993; -. DR Pharos; P02724; Tbio. DR PRO; PR:P02724; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P02724; Protein. DR Bgee; ENSG00000170180; Expressed in trabecular bone tissue and 111 other cell types or tissues. DR ExpressionAtlas; P02724; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR Gene3D; 1.20.5.70; -; 1. DR InterPro; IPR001195; Glycophorin. DR InterPro; IPR018938; Glycophorin_CS. DR InterPro; IPR049535; GYPA_B. DR PANTHER; PTHR13813; GLYCOPHORIN; 1. DR PANTHER; PTHR13813:SF5; GLYCOPHORIN-A; 1. DR Pfam; PF01102; Glycophorin_A; 1. DR PIRSF; PIRSF002466; Glycophorin; 1. DR PROSITE; PS00312; GLYCOPHORIN_A; 1. DR Genevisible; P02724; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood group antigen; Cell membrane; KW Direct protein sequencing; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Sialic acid; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:1059087" FT CHAIN 20..150 FT /note="Glycophorin-A" FT /id="PRO_0000012134" FT TOPO_DOM 20..91 FT /note="Extracellular" FT TRANSMEM 92..114 FT /note="Helical" FT TOPO_DOM 115..150 FT /note="Cytoplasmic" FT REGION 121..150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 133 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 21 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 22 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 23 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 29 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 30 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 31 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 32 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 36 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8286855" FT CARBOHYD 38 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:8286855" FT CARBOHYD 41 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 44 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 45 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 52 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:8286855" FT CARBOHYD 56 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 63 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 66 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT CARBOHYD 69 FT /note="O-linked (GalNAc...) threonine" FT /evidence="ECO:0000269|PubMed:1059087, FT ECO:0000269|PubMed:8286855" FT VAR_SEQ 1..26 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_047822" FT VAR_SEQ 13..45 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_047823" FT VARIANT 13 FT /note="E -> A (in dbSNP:rs4449373)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2216775, FT ECO:0000269|PubMed:2734312, ECO:0000269|PubMed:3456608, FT ECO:0000269|PubMed:3809885, ECO:0000269|PubMed:7798177" FT /id="VAR_058911" FT VARIANT 13 FT /note="E -> G (in dbSNP:rs4449373)" FT /id="VAR_059977" FT VARIANT 20 FT /note="S -> L (in N antigen and M(g) antigen; FT dbSNP:rs7682260)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15815621, ECO:0000269|PubMed:3196288" FT /id="VAR_003190" FT VARIANT 23 FT /note="T -> N (in M(g) antigen)" FT /evidence="ECO:0000269|PubMed:6940143" FT /id="VAR_058912" FT VARIANT 24 FT /note="G -> D (in dbSNP:rs7658293)" FT /id="VAR_058913" FT VARIANT 24 FT /note="G -> E (in N antigen, M(c) antigen and M(g) antigen; FT dbSNP:rs7687256)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15815621, ECO:0000269|PubMed:3196288, FT ECO:0000269|PubMed:6166001" FT /id="VAR_003191" FT VARIANT 46 FT /note="D -> E (in Ny(a) antigen)" FT /evidence="ECO:0000269|PubMed:10827258" FT /id="VAR_058914" FT VARIANT 47 FT /note="T -> K (in ENEH/Hut antigen)" FT /evidence="ECO:0000269|PubMed:1421409" FT /id="VAR_058915" FT VARIANT 47 FT /note="T -> M (in ENEH/Vw antigen)" FT /evidence="ECO:0000269|PubMed:1611092" FT /id="VAR_058916" FT VARIANT 50 FT /note="R -> W (in Or antigen)" FT /id="VAR_058917" FT VARIANT 66 FT /note="S -> Y (in Vr antigen; dbSNP:rs56077914)" FT /evidence="ECO:0000269|PubMed:10729812" FT /id="VAR_058918" FT VARIANT 73 FT /note="P -> S (in Os(a) antigen)" FT /evidence="ECO:0000269|PubMed:10827258" FT /id="VAR_058919" FT VARIANT 76 FT /note="E -> K (in Ri(a) antigen)" FT /id="VAR_058920" FT VARIANT 77 FT /note="T -> I (in Mt(a) antigen; dbSNP:rs56172553)" FT /evidence="ECO:0000269|PubMed:10729812" FT /id="VAR_058921" FT VARIANT 78 FT /note="G -> R (in ERIK antigen; dbSNP:rs1800582)" FT /evidence="ECO:0000269|PubMed:8245024" FT /id="VAR_058922" FT VARIANT 82 FT /note="Q -> K (in ENAV/MARS antigen)" FT /id="VAR_058923" FT VARIANT 84 FT /note="A -> P (in ENEP/HAG antigen)" FT /evidence="ECO:0000269|PubMed:10354388" FT /id="VAR_058924" FT MUTAGEN 87 FT /note="F->C: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:12813056" FT MUTAGEN 88 FT /note="S->C: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:12813056" FT MUTAGEN 90 FT /note="P->C: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:12813056" FT MUTAGEN 91 FT /note="E->C: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:12813056" FT MUTAGEN 94 FT /note="L->I: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:10926825" FT MUTAGEN 95 FT /note="I->A: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:10926825" FT MUTAGEN 98 FT /note="G->L: Diminishes dimerization." FT /evidence="ECO:0000269|PubMed:10926825" FT MUTAGEN 102 FT /note="G->L: Abolishes dimerization." FT /evidence="ECO:0000269|PubMed:10926825" FT CONFLICT 30 FT /note="S -> T (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="T -> S (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="T -> R (in Ref. 1; AAA88044)" FT /evidence="ECO:0000305" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:2KPF" FT HELIX 92..115 FT /evidence="ECO:0007829|PDB:5EH6" SQ SEQUENCE 150 AA; 16331 MW; 48A5450E22FA99C9 CRC64; MYGKIIFVLL LSEIVSISAS STTGVAMHTS TSSSVTKSYI SSQTNDTHKR DTYAATPRAH EVSEISVRTV YPPEEETGER VQLAHHFSEP EITLIIFGVM AGVIGTILLI SYGIRRLIKK SPSDVKPLPS PDTDVPLSSV EIENPETSDQ //