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Database: UniProt
Entry: P02724
LinkDB: P02724
Original site: P02724 
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   02-JUN-2021, entry version 218.
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;
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;
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;
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";
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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; 1MSR; Model; -; A/B=93-110.
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; 1MSR; -.
DR   PDBsum; 2KPE; -.
DR   PDBsum; 2KPF; -.
DR   PDBsum; 5EH4; -.
DR   PDBsum; 5EH6; -.
DR   BMRB; P02724; -.
DR   SMR; P02724; -.
DR   BioGRID; 109248; 35.
DR   IntAct; P02724; 43.
DR   STRING; 9606.ENSP00000354003; -.
DR   BindingDB; P02724; -.
DR   ChEMBL; CHEMBL5806; -.
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; 17 sites, 13 O-linked glycans (16 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; 2063 antibodies.
DR   DNASU; 2993; -.
DR   Ensembl; ENST00000324022; ENSP00000324483; ENSG00000170180. [P02724-3]
DR   Ensembl; ENST00000642713; ENSP00000494092; ENSG00000170180. [P02724-2]
DR   Ensembl; ENST00000646447; ENSP00000495922; ENSG00000170180. [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:ENSG00000170180.19; -.
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   BioGRID-ORCS; 2993; 6 hits in 986 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 116 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   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
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
//
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