GLPA_HUMAN
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 03-AUG-2022, entry version 222.
DE RecName: Full=Glycophorin-A;
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; 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 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 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 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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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) (MNS38)
RT are associated with GPA amino acid substitutions.";
RL Transfusion 40:555-559(2000).
RN [42]
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 arise
RT 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 the
CC erythrocyte. The N-terminal glycosylated segment, which lies outside
CC the erythrocyte membrane, has MN blood group receptors. Appears to be
CC important for the function of SLC4A1 and is required for high activity
CC of SLC4A1. May be involved in translocation of SLC4A1 to the plasma
CC membrane. Is a receptor for influenza virus. Is a receptor for
CC Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175);
CC binding of EBA-175 is dependent on sialic acid residues of the O-linked
CC glycans. Appears to be a receptor for Hepatitis A virus (HAV).
CC {ECO:0000269|PubMed:10926825, ECO:0000269|PubMed:12813056,
CC ECO:0000269|PubMed:14604989, ECO:0000269|PubMed:15331714,
CC ECO:0000269|PubMed:19438409, ECO:0000269|PubMed:8009226}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11313283,
CC ECO:0000269|PubMed:1463744}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Streptococcus gordonii
CC hsa protein. {ECO:0000269|PubMed:18380804}.
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 PDBsum; 1AFO; -.
DR PDBsum; 2KPE; -.
DR PDBsum; 2KPF; -.
DR PDBsum; 5EH4; -.
DR PDBsum; 5EH6; -.
DR AlphaFoldDB; P02724; -.
DR BMRB; P02724; -.
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 (gp) 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 GlyGen; P02724; 19 sites, 4 N-linked glycans (1 site), 25 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; P02724; -.
DR PeptideAtlas; P02724; -.
DR PRIDE; P02724; -.
DR ProteomicsDB; 51556; -. [P02724-1]
DR ProteomicsDB; 7281; -.
DR ProteomicsDB; 7282; -.
DR ABCD; P02724; 17 sequenced antibodies.
DR Antibodypedia; 3054; 2068 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 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; 1548637at2759; -.
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; 8 hits in 1065 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 109 other tissues.
DR ExpressionAtlas; P02724; baseline and differential.
DR Genevisible; P02724; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 InterPro; IPR001195; Glycophorin.
DR InterPro; IPR018938; Glycophorin_CS.
DR PANTHER; PTHR13813; PTHR13813; 1.
DR PIRSF; PIRSF002466; Glycophorin; 1.
DR PROSITE; PS00312; GLYCOPHORIN_A; 1.
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
