CENPA_HUMAN
ID CENPA_HUMAN Reviewed; 140 AA.
AC P49450; D6W544; Q53T74; Q9BVW2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Histone H3-like centromeric protein A;
DE AltName: Full=Centromere autoantigen A;
DE AltName: Full=Centromere protein A;
DE Short=CENP-A;
GN Name=CENPA;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP REGION.
RX PubMed=7962047; DOI=10.1083/jcb.127.3.581;
RA Sullivan K.F., Hechenberger M., Masri K.;
RT "Human CENP-A contains a histone H3 related histone fold domain that is
RT required for targeting to the centromere.";
RL J. Cell Biol. 127:581-592(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33, FUNCTION, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=9024683; DOI=10.1083/jcb.136.3.501;
RA Shelby R.D., Vafa O., Sullivan K.F.;
RT "Assembly of CENP-A into centromeric chromatin requires a cooperative array
RT of nucleosomal DNA contact sites.";
RL J. Cell Biol. 136:501-513(1997).
RN [7]
RP IDENTIFICATION OF AUTOANTIGENIC EPITOPES.
RX PubMed=10759786; DOI=10.1046/j.1365-2249.2000.01189.x;
RA Muro Y., Azuma N., Onouchi H., Kunimatsu M., Tomita Y., Sasaki M.,
RA Sugimoto K.;
RT "Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted
RT to the N-terminal region, which has no homology with histone H3.";
RL Clin. Exp. Immunol. 120:218-223(2000).
RN [8]
RP UBIQUITINATION, AND INTERACTION WITH HHV-1 ICP0 (MICROBIAL INFECTION).
RX PubMed=11053442; DOI=10.1074/jbc.m008547200;
RA Lomonte P., Sullivan K.F., Everett R.D.;
RT "Degradation of nucleosome-associated centromeric histone H3-like protein
RT CENP-A induced by herpes simplex virus type 1 protein ICP0.";
RL J. Biol. Chem. 276:5829-5835(2001).
RN [9]
RP PHOSPHORYLATION AT SER-7, MUTAGENESIS OF SER-7, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11756469; DOI=10.1083/jcb.200108125;
RA Zeitlin S.G., Shelby R.D., Sullivan K.F.;
RT "CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role
RT in completion of cytokinesis.";
RL J. Cell Biol. 155:1147-1157(2001).
RN [10]
RP PHOSPHORYLATION AT SER-7, MUTAGENESIS OF SER-7, FUNCTION, INTERACTION WITH
RP AURKA, AND SUBCELLULAR LOCATION.
RX PubMed=14667408; DOI=10.1016/s1534-5807(03)00364-2;
RA Kunitoku N., Sasayama T., Marumoto T., Zhang D., Honda S., Kobayashi O.,
RA Hatakeyama K., Ushio Y., Saya H., Hirota T.;
RT "CENP-A phosphorylation by Aurora-A in prophase is required for enrichment
RT of Aurora-B at inner centromeres and for kinetochore function.";
RL Dev. Cell 5:853-864(2003).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15702419; DOI=10.1007/s10577-005-5377-4;
RA Irvine D.V., Amor D.J., Perry J., Sirvent N., Pedeutour F., Choo K.H.,
RA Saffery R.;
RT "Chromosome size and origin as determinants of the level of CENP-A
RT incorporation into human centromeres.";
RL Chromosome Res. 12:805-815(2004).
RN [12]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15475964; DOI=10.1038/nsmb845;
RA Sullivan B.A., Karpen G.H.;
RT "Centromeric chromatin exhibits a histone modification pattern that is
RT distinct from both euchromatin and heterochromatin.";
RL Nat. Struct. Mol. Biol. 11:1076-1083(2004).
RN [13]
RP SUBUNIT, DOMAIN CATD, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15282608; DOI=10.1038/nature02766;
RA Black B.E., Foltz D.R., Chakravarthy S., Luger K., Woods V.L. Jr.,
RA Cleveland D.W.;
RT "Structural determinants for generating centromeric chromatin.";
RL Nature 430:578-582(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-NAC
RP COMPLEX WITH CENPC; CENPH; CENPM; CENPN; CENPT AND CENPU.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [16]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17651496; DOI=10.1186/gb-2007-8-7-r148;
RA Alonso A., Fritz B., Hasson D., Abrusan G., Cheung F., Yoda K.,
RA Radlwimmer B., Ladurner A.G., Warburton P.E.;
RT "Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A
RT chromatin at human neocentromeres.";
RL Genome Biol. 8:R148.1-R148.19(2007).
RN [17]
RP PHOSPHORYLATION AT SER-7.
RX PubMed=18239465; DOI=10.4161/cc.7.6.5563;
RA Slattery S.D., Moore R.V., Brinkley B.R., Hall R.M.;
RT "Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and
RT Borealin during mitosis.";
RL Cell Cycle 7:787-795(2008).
RN [18]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18072184; DOI=10.1002/cbic.200700358;
RA Orthaus S., Biskup C., Hoffmann B., Hoischen C., Ohndorf S., Benndorf K.,
RA Diekmann S.;
RT "Assembly of the inner kinetochore proteins CENP-A and CENP-B in living
RT human cells.";
RL ChemBioChem 9:77-92(2008).
RN [19]
RP INTERACTION WITH CENPT.
RX PubMed=19412974; DOI=10.1002/jbio.200810014;
RA Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.;
RT "Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-
RT A and CENP-B.";
RL J. Biophotonics 1:245-254(2008).
RN [20]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19114591; DOI=10.1083/jcb.200804078;
RA Marshall O.J., Marshall A.T., Choo K.H.A.;
RT "Three-dimensional localization of CENP-A suggests a complex higher order
RT structure of centromeric chromatin.";
RL J. Cell Biol. 183:1193-1202(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP INTERACTION WITH HJURP.
RX PubMed=19410544; DOI=10.1016/j.cell.2009.02.039;
RA Foltz D.R., Jansen L.E.T., Bailey A.O., Yates J.R. III, Bassett E.A.,
RA Wood S., Black B.E., Cleveland D.W.;
RT "Centromere-specific assembly of CENP-A nucleosomes is mediated by HJURP.";
RL Cell 137:472-484(2009).
RN [23]
RP INTERACTION WITH HJURP.
RX PubMed=19410545; DOI=10.1016/j.cell.2009.02.040;
RA Dunleavy E.M., Roche D., Tagami H., Lacoste N., Ray-Gallet D., Nakamura Y.,
RA Daigo Y., Nakatani Y., Almouzni-Pettinotti G.;
RT "HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-
RT A at centromeres.";
RL Cell 137:485-497(2009).
RN [24]
RP IDENTIFICATION IN COMPLEX WITH CENPT AND CENPW.
RX PubMed=19533040; DOI=10.1007/s10059-009-0083-2;
RA Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.;
RT "Cancer-upregulated gene 2 (CUG2), a new component of centromere complex,
RT is required for kinetochore function.";
RL Mol. Cells 27:697-701(2009).
RN [25]
RP INTERACTION WITH CENPN.
RX PubMed=19543270; DOI=10.1038/ncb1899;
RA Carroll C.W., Silva M.C.C., Godek K.M., Jansen L.E.T., Straight A.F.;
RT "Centromere assembly requires the direct recognition of CENP-A nucleosomes
RT by CENP-N.";
RL Nat. Cell Biol. 11:896-902(2009).
RN [26]
RP INTERACTION WITH CENPC.
RX PubMed=19503796; DOI=10.1371/journal.pone.0005832;
RA Trazzi S., Perini G., Bernardoni R., Zoli M., Reese J.C., Musacchio A.,
RA Della Valle G.;
RT "The C-terminal domain of CENP-C displays multiple and critical functions
RT for mammalian centromere formation.";
RL PLoS ONE 4:E5832-E5832(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-19 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-17 AND SER-19, MUTAGENESIS OF SER-17 AND SER-19,
RP METHYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, SUBUNIT, AND
RP INTERACTION WITH HJURP.
RX PubMed=23818633; DOI=10.1073/pnas.1300325110;
RA Bailey A.O., Panchenko T., Sathyan K.M., Petkowski J.J., Pai P.J.,
RA Bai D.L., Russell D.H., Macara I.G., Shabanowitz J., Hunt D.F., Black B.E.,
RA Foltz D.R.;
RT "Posttranslational modification of CENP-A influences the conformation of
RT centromeric chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11827-11832(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, 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 [31]
RP DEVELOPMENTAL STAGE.
RX PubMed=24522885; DOI=10.1098/rsob.130229;
RA Dornblut C., Quinn N., Monajambashi S., Prendergast L., van Vuuren C.,
RA Muench S., Deng W., Leonhardt H., Cardoso M.C., Hoischen C., Diekmann S.,
RA Sullivan K.F.;
RT "A CENP-S/X complex assembles at the centromere in S and G2 phases of the
RT human cell cycle.";
RL Open Biol. 4:130229-130229(2014).
RN [32]
RP FUNCTION, PHOSPHORYLATION AT SER-68, MUTAGENESIS OF SER-68, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH HJURP; CDK1; PPP1CA AND RBBP7.
RX PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
RA Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S., Cui L.,
RA Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G., Zhang X.,
RA Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
RT "Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-
RT dependent deposition at centromeres.";
RL Dev. Cell 32:68-81(2015).
RN [33]
RP FUNCTION, ELECTRON MICROSCOPY OF NUCLEOSOME, SUBUNIT, DOMAIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [34]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26878239; DOI=10.1038/nsmb.3175;
RA Falk S.J., Lee J., Sekulic N., Sennett M.A., Lee T.H., Black B.E.;
RT "CENP-C directs a structural transition of CENP-A nucleosomes mainly
RT through sliding of DNA gyres.";
RL Nat. Struct. Mol. Biol. 23:204-208(2016).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND MUTAGENESIS OF HIS-104 AND LEU-112.
RX PubMed=20739937; DOI=10.1038/nature09323;
RA Sekulic N., Bassett E.A., Rogers D.J., Black B.E.;
RT "The structure of (CENP-A-H4)(2) reveals physical features that mark
RT centromeres.";
RL Nature 467:347-351(2010).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HJURP AND HISTONE H4,
RP FUNCTION, AND SUBUNIT.
RX PubMed=21478274; DOI=10.1101/gad.2045111;
RA Hu H., Liu Y., Wang M., Fang J., Huang H., Yang N., Li Y., Wang J., Yao X.,
RA Shi Y., Li G., Xu R.M.;
RT "Structure of a CENP-A-histone H4 heterodimer in complex with chaperone
RT HJURP.";
RL Genes Dev. 25:901-906(2011).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF NUCLEOSOME, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 80-ARG-GLY-81.
RX PubMed=21743476; DOI=10.1038/nature10258;
RA Tachiwana H., Kagawa W., Shiga T., Osakabe A., Miya Y., Saito K.,
RA Hayashi-Takanaka Y., Oda T., Sato M., Park S.Y., Kimura H., Kurumizaka H.;
RT "Crystal structure of the human centromeric nucleosome containing CENP-A.";
RL Nature 476:232-235(2011).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF NUCLEOSOME CONTAINING BOTH CENPA
RP AND HISTONE H3, AND SUBUNIT.
RX PubMed=25408271; DOI=10.1038/srep07115;
RA Arimura Y., Shirayama K., Horikoshi N., Fujita R., Taguchi H., Kagawa W.,
RA Fukagawa T., Almouzni G., Kurumizaka H.;
RT "Crystal structure and stable property of the cancer-associated heterotypic
RT nucleosome containing CENP-A and H3.3.";
RL Sci. Rep. 4:7115-7115(2014).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 3-10 IN COMPLEX WITH NTMT1, AND
RP METHYLATION AT GLY-2.
RX PubMed=26543159; DOI=10.1101/gad.270926.115;
RA Wu R., Yue Y., Zheng X., Li H.;
RT "Molecular basis for histone N-terminal methylation by NRMT1.";
RL Genes Dev. 29:2337-2342(2015).
CC -!- FUNCTION: Histone H3-like nucleosomal protein that is specifically
CC found in centromeric nucleosomes (PubMed:7962047, PubMed:9024683,
CC PubMed:11756469, PubMed:14667408, PubMed:15702419, PubMed:15475964,
CC PubMed:15282608, PubMed:17651496, PubMed:19114591, PubMed:27499292,
CC PubMed:20739937). Replaces conventional H3 in the nucleosome core of
CC centromeric chromatin at the inner plate of the kinetochore
CC (PubMed:18072184). The presence of CENPA subtly modifies the nucleosome
CC structure and the way DNA is wrapped around the nucleosome and gives
CC rise to protruding DNA ends that are less well-ordered and rigid
CC compared to nucleosomes containing histone H3 (PubMed:27499292,
CC PubMed:26878239). May serve as an epigenetic mark that propagates
CC centromere identity through replication and cell division
CC (PubMed:15475964, PubMed:15282608, PubMed:26878239, PubMed:20739937,
CC PubMed:21478274). Required for recruitment and assembly of kinetochore
CC proteins, and as a consequence required for progress through mitosis,
CC chromosome segregation and cytokinesis (PubMed:11756469,
CC PubMed:14667408, PubMed:18072184, PubMed:23818633, PubMed:25556658,
CC PubMed:27499292). {ECO:0000269|PubMed:11756469,
CC ECO:0000269|PubMed:14667408, ECO:0000269|PubMed:15282608,
CC ECO:0000269|PubMed:15475964, ECO:0000269|PubMed:15702419,
CC ECO:0000269|PubMed:17651496, ECO:0000269|PubMed:18072184,
CC ECO:0000269|PubMed:19114591, ECO:0000269|PubMed:21478274,
CC ECO:0000269|PubMed:23818633, ECO:0000269|PubMed:25556658,
CC ECO:0000269|PubMed:26878239, ECO:0000269|PubMed:27499292,
CC ECO:0000269|PubMed:7962047, ECO:0000269|PubMed:9024683,
CC ECO:0000305|PubMed:20739937}.
CC -!- SUBUNIT: Component of centromeric nucleosomes, where DNA is wrapped
CC around a histone octamer core (PubMed:23818633, PubMed:26878239,
CC PubMed:20739937, PubMed:21743476). The octamer contains two molecules
CC each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer
CC and two H2A-H2B heterodimers (PubMed:23818633, PubMed:26878239,
CC PubMed:20739937, PubMed:21743476). CENPA modulates the DNA-binding
CC characteristics of nucleosomes so that protruding DNA ends have higher
CC flexibility than in nucleosomes containing conventional histone H3
CC (PubMed:27499292, PubMed:21743476). Inhibits binding of histone H1 to
CC nucleosomes, since histone H1 binds preferentially to rigid DNA linkers
CC that protrude from nucleosomes (PubMed:27499292). Nucleosomes
CC containing CENPA also contain histone H2A variants such as MACROH2A and
CC H2A.Z/H2AZ1 (Probable). The CENPA-H4 heterotetramer is more compact and
CC structurally more rigid than corresponding H3-H4 heterotetramers
CC (PubMed:15282608, PubMed:20739937). Can assemble into nucleosomes that
CC contain both CENPA and histone H3.3; these nucleosomes interact with a
CC single CENPC chain (PubMed:25408271). Heterotrimer composed of HJURP,
CC CENPA and histone H4, where HJURP interacts with the dimer formed by
CC CENPA and histone H4 and prevents tetramerization of CENPA and H4
CC (PubMed:21478274). Component of the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU
CC (PubMed:16622419). Interacts (via CATD domain) with HJURP; the
CC interaction is direct and is required for its localization to
CC centromeres (PubMed:15282608, PubMed:19410544, PubMed:19410545,
CC PubMed:23818633, PubMed:25556658). Interacts with CENPC, CENPN and
CC CENPT; interaction is direct. Part of a centromere complex consisting
CC of CENPA, CENPT and CENPW (PubMed:19533040). Identified in centromere
CC complexes containing histones H2A, H2B and H4, and at least CENPA,
CC CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
CC (PubMed:27499292). Can self-associate (PubMed:9024683). The CENPA-H4
CC heterotetramer can bind DNA by itself (in vitro) (PubMed:20739937).
CC Interacts with CDK1, PPP1CA and RBBP7 (PubMed:25556658).
CC {ECO:0000269|PubMed:15282608, ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:19410544, ECO:0000269|PubMed:19410545,
CC ECO:0000269|PubMed:19412974, ECO:0000269|PubMed:19503796,
CC ECO:0000269|PubMed:19533040, ECO:0000269|PubMed:19543270,
CC ECO:0000269|PubMed:20739937, ECO:0000269|PubMed:21478274,
CC ECO:0000269|PubMed:21743476, ECO:0000269|PubMed:23818633,
CC ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26878239,
CC ECO:0000269|PubMed:27499292, ECO:0000269|PubMed:9024683, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts directly with herpes virus
CC HHV-1 protein ICP0. {ECO:0000269|PubMed:11053442}.
CC -!- INTERACTION:
CC P49450; Q03188: CENPC; NbExp=4; IntAct=EBI-1751979, EBI-295799;
CC P49450; P62805: H4C9; NbExp=6; IntAct=EBI-1751979, EBI-302023;
CC P49450; Q8NCD3: HJURP; NbExp=15; IntAct=EBI-1751979, EBI-719429;
CC P49450; Q8NCD3-1: HJURP; NbExp=2; IntAct=EBI-1751979, EBI-15825976;
CC P49450; P49736: MCM2; NbExp=3; IntAct=EBI-1751979, EBI-374819;
CC P49450; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1751979, EBI-748974;
CC P49450-1; P62805: H4C9; NbExp=2; IntAct=EBI-15826012, EBI-302023;
CC P49450-1; Q8NCD3: HJURP; NbExp=3; IntAct=EBI-15826012, EBI-719429;
CC P49450-1; P06748-1: NPM1; NbExp=3; IntAct=EBI-15826012, EBI-354150;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14667408,
CC ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:9024683}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:18072184,
CC ECO:0000269|PubMed:19114591, ECO:0000269|PubMed:23818633}. Chromosome,
CC centromere {ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:15282608,
CC ECO:0000269|PubMed:15475964, ECO:0000269|PubMed:15702419,
CC ECO:0000269|PubMed:17651496, ECO:0000269|PubMed:18072184,
CC ECO:0000269|PubMed:20739937, ECO:0000269|PubMed:21743476,
CC ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:27499292,
CC ECO:0000269|PubMed:7962047, ECO:0000269|PubMed:9024683}. Note=Localizes
CC exclusively in the kinetochore domain of centromeres. Occupies a
CC compact domain at the inner kinetochore plate stretching across 2
CC thirds of the length of the constriction but encompassing only one
CC third of the constriction width and height (PubMed:19114591).
CC Phosphorylation at Ser-68 during early mitosis abolishes association
CC with chromatin and centromeres and results in dispersed nuclear
CC location (PubMed:25556658). {ECO:0000269|PubMed:19114591,
CC ECO:0000269|PubMed:25556658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49450-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49450-2; Sequence=VSP_020430;
CC -!- DEVELOPMENTAL STAGE: Expression varies across the cell cycle, with high
CC levels in G2 phase (at the mRNA level). {ECO:0000269|PubMed:24522885}.
CC -!- DOMAIN: The CATD (CENPA targeting domain) region is responsible for the
CC more compact structure of nucleosomes containing CENPA
CC (PubMed:15282608). It is necessary and sufficient to mediate the
CC localization into centromeres (PubMed:7962047, PubMed:15282608).
CC {ECO:0000269|PubMed:15282608, ECO:0000269|PubMed:7962047}.
CC -!- PTM: Ubiquitinated (Probable). Interaction with herpes virus HSV-1 ICP0
CC protein, leads to its degradation by the proteasome pathway.
CC {ECO:0000269|PubMed:11053442, ECO:0000305}.
CC -!- PTM: Trimethylated by NTMT1 at the N-terminal glycine after cleavage of
CC Met-1. Methylation is low before incorporation into nucleosomes and
CC increases with cell cycle progression, with the highest levels in
CC mitotic nucleosomes. {ECO:0000269|PubMed:23818633}.
CC -!- PTM: Phosphorylated by CDK1 at Ser-68 during early mitosis; this
CC abolishes association with chromatin and centromeres, prevents
CC interaction with HJURP and thereby prevents premature assembly of CENPA
CC into centromeres (PubMed:25556658). Dephosphorylated at Ser-68 by
CC PPP1CA during late mitosis (PubMed:25556658). Phosphorylation of Ser-7
CC by AURKA and AURKB during prophase is required for localization of
CC AURKA and AURKB at inner centromere and is essential for normal
CC cytokinesis (PubMed:11756469, PubMed:14667408, PubMed:18239465).
CC Initial phosphorylation during prophase is mediated by AURKA and is
CC maintained by AURKB. {ECO:0000269|PubMed:11756469,
CC ECO:0000269|PubMed:14667408, ECO:0000269|PubMed:18239465,
CC ECO:0000269|PubMed:25556658}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:O35216}.
CC -!- MISCELLANEOUS: Antibodies against CENPA are present in sera from
CC patients with autoimmune diseases that developed autoantibodies against
CC centrosomal proteins.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; U14518; AAA57416.1; -; mRNA.
DR EMBL; BT007246; AAP35910.1; -; mRNA.
DR EMBL; AC011740; AAX93267.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00669.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00670.1; -; Genomic_DNA.
DR EMBL; BC000881; AAH00881.1; -; mRNA.
DR EMBL; BC002703; AAH02703.1; -; mRNA.
DR EMBL; U82609; AAB47505.1; -; Genomic_DNA.
DR CCDS; CCDS1729.1; -. [P49450-1]
DR CCDS; CCDS42662.1; -. [P49450-2]
DR PIR; I38855; I38855.
DR RefSeq; NP_001035891.1; NM_001042426.1. [P49450-2]
DR RefSeq; NP_001800.1; NM_001809.3. [P49450-1]
DR PDB; 3AN2; X-ray; 3.60 A; A/E=1-140.
DR PDB; 3NQJ; X-ray; 2.10 A; A=60-140.
DR PDB; 3NQU; X-ray; 2.50 A; A=1-140.
DR PDB; 3R45; X-ray; 2.60 A; A=1-140.
DR PDB; 3WTP; X-ray; 2.67 A; A=1-140.
DR PDB; 5CVD; X-ray; 1.30 A; D/E=3-10.
DR PDB; 5Z23; X-ray; 2.73 A; A/E=75-116.
DR PDB; 6BUZ; EM; 3.92 A; A/E=1-140.
DR PDB; 6C0W; EM; 4.00 A; A/E=1-140.
DR PDB; 6E0C; EM; 2.63 A; A/E=1-140.
DR PDB; 6E0P; EM; 2.60 A; A/E=1-140.
DR PDB; 6KDQ; X-ray; 1.50 A; E/F=2-8.
DR PDB; 6KDS; X-ray; 1.84 A; E=2-7.
DR PDB; 6L49; EM; 18.90 A; A/E=1-140.
DR PDB; 6MUO; EM; 3.60 A; A/E=38-139.
DR PDB; 6MUP; EM; 3.50 A; A/E=38-139.
DR PDB; 6O1D; EM; 3.40 A; A/E=1-140.
DR PDB; 6SE0; EM; 3.80 A; A/E=1-140.
DR PDB; 6SE6; EM; 3.50 A; A/E=1-140.
DR PDB; 6SEE; EM; 4.20 A; A/E=1-140.
DR PDB; 6SEF; EM; 3.70 A; A/E=1-140.
DR PDB; 6SEG; EM; 3.10 A; A/E=1-140.
DR PDB; 6TEM; EM; 3.90 A; A/E=1-140.
DR PDB; 7D20; EM; 3.00 A; A/E=1-140.
DR PDB; 7U46; EM; 2.68 A; A/E=1-140.
DR PDB; 7U47; EM; 7.50 A; A/E/L/P=1-140.
DR PDB; 7U4D; EM; 8.10 A; A/E/L/P=1-140.
DR PDBsum; 3AN2; -.
DR PDBsum; 3NQJ; -.
DR PDBsum; 3NQU; -.
DR PDBsum; 3R45; -.
DR PDBsum; 3WTP; -.
DR PDBsum; 5CVD; -.
DR PDBsum; 5Z23; -.
DR PDBsum; 6BUZ; -.
DR PDBsum; 6C0W; -.
DR PDBsum; 6E0C; -.
DR PDBsum; 6E0P; -.
DR PDBsum; 6KDQ; -.
DR PDBsum; 6KDS; -.
DR PDBsum; 6L49; -.
DR PDBsum; 6MUO; -.
DR PDBsum; 6MUP; -.
DR PDBsum; 6O1D; -.
DR PDBsum; 6SE0; -.
DR PDBsum; 6SE6; -.
DR PDBsum; 6SEE; -.
DR PDBsum; 6SEF; -.
DR PDBsum; 6SEG; -.
DR PDBsum; 6TEM; -.
DR PDBsum; 7D20; -.
DR PDBsum; 7U46; -.
DR PDBsum; 7U47; -.
DR PDBsum; 7U4D; -.
DR AlphaFoldDB; P49450; -.
DR SMR; P49450; -.
DR BioGRID; 107487; 373.
DR ComplexPortal; CPX-5647; CENP-A nucleosome complex.
DR CORUM; P49450; -.
DR DIP; DIP-52297N; -.
DR IntAct; P49450; 51.
DR STRING; 9606.ENSP00000336868; -.
DR iPTMnet; P49450; -.
DR PhosphoSitePlus; P49450; -.
DR BioMuta; CENPA; -.
DR DMDM; 1345726; -.
DR EPD; P49450; -.
DR jPOST; P49450; -.
DR MassIVE; P49450; -.
DR PaxDb; P49450; -.
DR PeptideAtlas; P49450; -.
DR PRIDE; P49450; -.
DR ProteomicsDB; 56013; -. [P49450-1]
DR ProteomicsDB; 56014; -. [P49450-2]
DR Antibodypedia; 3643; 544 antibodies from 36 providers.
DR DNASU; 1058; -.
DR Ensembl; ENST00000233505.12; ENSP00000233505.8; ENSG00000115163.15. [P49450-2]
DR Ensembl; ENST00000335756.9; ENSP00000336868.4; ENSG00000115163.15. [P49450-1]
DR GeneID; 1058; -.
DR KEGG; hsa:1058; -.
DR MANE-Select; ENST00000335756.9; ENSP00000336868.4; NM_001809.4; NP_001800.1.
DR UCSC; uc002rhr.4; human. [P49450-1]
DR CTD; 1058; -.
DR DisGeNET; 1058; -.
DR GeneCards; CENPA; -.
DR HGNC; HGNC:1851; CENPA.
DR HPA; ENSG00000115163; Tissue enhanced (lymphoid).
DR MIM; 117139; gene.
DR neXtProt; NX_P49450; -.
DR OpenTargets; ENSG00000115163; -.
DR PharmGKB; PA26396; -.
DR VEuPathDB; HostDB:ENSG00000115163; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_3_2_1; -.
DR InParanoid; P49450; -.
DR OMA; VHLFEDC; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P49450; -.
DR TreeFam; TF354293; -.
DR PathwayCommons; P49450; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P49450; -.
DR SIGNOR; P49450; -.
DR BioGRID-ORCS; 1058; 651 hits in 1079 CRISPR screens.
DR ChiTaRS; CENPA; human.
DR EvolutionaryTrace; P49450; -.
DR GeneWiki; CENPA; -.
DR GenomeRNAi; 1058; -.
DR Pharos; P49450; Tbio.
DR PRO; PR:P49450; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P49450; protein.
DR Bgee; ENSG00000115163; Expressed in oocyte and 139 other tissues.
DR ExpressionAtlas; P49450; baseline and differential.
DR Genevisible; P49450; HS.
DR GO; GO:0043505; C:CENP-A containing nucleosome; IPI:ComplexPortal.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000939; C:inner kinetochore; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; IDA:BHF-UCL.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0061644; P:protein localization to CENP-A containing chromatin; IC:ComplexPortal.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IDA:BHF-UCL.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00272; -.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Cell cycle;
KW Cell division; Centromere; Chromosome; DNA-binding; Host-virus interaction;
KW Kinetochore; Methylation; Mitosis; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23818633"
FT CHAIN 2..140
FT /note="Histone H3-like centromeric protein A"
FT /id="PRO_0000221373"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..54
FT /note="Important for flexibility of DNA ends that protrude
FT from nucleosomes"
FT /evidence="ECO:0000269|PubMed:27499292"
FT REGION 75..116
FT /note="CATD"
FT /evidence="ECO:0000269|PubMed:15282608,
FT ECO:0000269|PubMed:7962047"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000269|PubMed:23818633,
FT ECO:0000269|PubMed:26543159"
FT MOD_RES 7
FT /note="Phosphoserine; by AURKA and AURKB"
FT /evidence="ECO:0000269|PubMed:11756469,
FT ECO:0000269|PubMed:14667408, ECO:0000269|PubMed:18239465"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23818633,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23818633,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25556658"
FT VAR_SEQ 71..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020430"
FT MUTAGEN 7
FT /note="S->A: Induces a delay at the terminal stage of
FT cytokinesis and chromosome misalignment during mitosis due
FT to a defect in kinetochore attachment to microtubules."
FT /evidence="ECO:0000269|PubMed:11756469,
FT ECO:0000269|PubMed:14667408"
FT MUTAGEN 17
FT /note="S->A: Impaired mitotic chromosome congression and
FT chromosome segregation; when associated with A-19."
FT /evidence="ECO:0000269|PubMed:23818633"
FT MUTAGEN 19
FT /note="S->A: Impaired mitotic chromosome congression and
FT chromosome segregation; when associated with A-17."
FT /evidence="ECO:0000269|PubMed:23818633"
FT MUTAGEN 68
FT /note="S->A: No effect on interaction with HJURP. Impairs
FT localization at centromeres."
FT /evidence="ECO:0000269|PubMed:25556658"
FT MUTAGEN 68
FT /note="S->E,Q: Impairs interaction with HJURP, association
FT with chromatin and localization at centromeres."
FT /evidence="ECO:0000269|PubMed:25556658"
FT MUTAGEN 80..81
FT /note="RG->AA: Impairs retention at centromeres, but not
FT targeting to centromeres."
FT /evidence="ECO:0000269|PubMed:21743476"
FT MUTAGEN 104
FT /note="H->G: Reduces location at centromeres. Abolishes
FT location at centromeres; when associated with C-112."
FT /evidence="ECO:0000269|PubMed:20739937"
FT MUTAGEN 112
FT /note="L->C: No effect on location at centromeres.
FT Abolishes location at centromeres; when associated with G-
FT 104."
FT /evidence="ECO:0000269|PubMed:20739937"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6E0P"
FT HELIX 64..79
FT /evidence="ECO:0007829|PDB:3NQJ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3R45"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:3NQJ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3NQJ"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3NQJ"
FT TURN 134..138
FT /evidence="ECO:0007829|PDB:6E0P"
SQ SEQUENCE 140 AA; 15991 MW; 11A28FEB54486489 CRC64;
MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL
LIRKLPFSRL AREICVKFTR GVDFNWQAQA LLALQEAAEA FLVHLFEDAY LLTLHAGRVT
LFPKDVQLAR RIRGLEEGLG
