RPAP1_HUMAN
ID RPAP1_HUMAN Reviewed; 1393 AA.
AC Q9BWH6; Q9H9I2; Q9NSQ5; Q9P2E4; Q9UFS7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RNA polymerase II-associated protein 1;
GN Name=RPAP1; Synonyms=KIAA1403;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS LYS-506
RP AND GLU-825.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-825.
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LYS-506
RP AND GLU-825.
RC TISSUE=Eye;
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 [LARGE SCALE MRNA] OF 761-1393, AND VARIANT GLU-825.
RC TISSUE=Mammary cancer, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
RX PubMed=15282305; DOI=10.1128/mcb.24.16.7043-7058.2004;
RA Jeronimo C., Langelier M.-F., Zeghouf M., Cojocaru M., Bergeron D.,
RA Baali D., Forget D., Mnaimneh S., Davierwala A.P., Pootoolal J., Chandy M.,
RA Canadien V., Beattie B.K., Richards D.P., Workman J.L., Hughes T.R.,
RA Greenblatt J., Coulombe B.;
RT "RPAP1, a novel human RNA polymerase II-associated protein affinity
RT purified with recombinant wild-type and mutated polymerase subunits.";
RL Mol. Cell. Biol. 24:7043-7058(2004).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP RNA POLYMERASE II COMPLEX.
RX PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
RA Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
RA Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
RA Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
RT "Systematic analysis of the protein interaction network for the human
RT transcription machinery reveals the identity of the 7SK capping enzyme.";
RL Mol. Cell 27:262-274(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; THR-321 AND SER-1121, 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 [14]
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 [15]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-525.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Forms an interface between the RNA polymerase II enzyme and
CC chaperone/scaffolding protein, suggesting that it is required to
CC connect RNA polymerase II to regulators of protein complex formation.
CC Required for interaction of the RNA polymerase II complex with
CC acetylated histone H3. {ECO:0000269|PubMed:17643375}.
CC -!- SUBUNIT: Part of an RNA polymerase II complex that contains POLR2A,
CC POLR2B, POLR2C, POLR2D, POLR2E, POLR2F, POLR2G, POLR2H, POLR2I, POLR2J,
CC POLR2K, POLR2L, RPAP1, FCP1 plus the general transcription factors
CC TFIIB and TFIIF. {ECO:0000269|PubMed:15282305,
CC ECO:0000269|PubMed:17643375}.
CC -!- INTERACTION:
CC Q9BWH6; P62875: POLR2L; NbExp=3; IntAct=EBI-1048085, EBI-359527;
CC Q9BWH6; Q9NUX5: POT1; NbExp=2; IntAct=EBI-1048085, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BWH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWH6-2; Sequence=VSP_024680, VSP_024681;
CC Name=3;
CC IsoId=Q9BWH6-3; Sequence=VSP_024679;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RPAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92641.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037824; BAA92641.1; ALT_INIT; mRNA.
DR EMBL; AK022794; BAB14247.1; -; mRNA.
DR EMBL; AC016134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000246; AAH00246.2; -; mRNA.
DR EMBL; AL117479; CAB55952.1; -; mRNA.
DR EMBL; AL157487; CAB75675.2; -; mRNA.
DR CCDS; CCDS10079.1; -. [Q9BWH6-1]
DR PIR; T17262; T17262.
DR PIR; T46928; T46928.
DR RefSeq; NP_056355.2; NM_015540.3. [Q9BWH6-1]
DR RefSeq; XP_005254354.1; XM_005254297.1. [Q9BWH6-1]
DR AlphaFoldDB; Q9BWH6; -.
DR BioGRID; 117487; 110.
DR CORUM; Q9BWH6; -.
DR IntAct; Q9BWH6; 20.
DR MINT; Q9BWH6; -.
DR STRING; 9606.ENSP00000306123; -.
DR GlyGen; Q9BWH6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWH6; -.
DR MetOSite; Q9BWH6; -.
DR PhosphoSitePlus; Q9BWH6; -.
DR BioMuta; RPAP1; -.
DR DMDM; 296452978; -.
DR EPD; Q9BWH6; -.
DR jPOST; Q9BWH6; -.
DR MassIVE; Q9BWH6; -.
DR MaxQB; Q9BWH6; -.
DR PaxDb; Q9BWH6; -.
DR PeptideAtlas; Q9BWH6; -.
DR PRIDE; Q9BWH6; -.
DR ProteomicsDB; 79279; -. [Q9BWH6-1]
DR ProteomicsDB; 79280; -. [Q9BWH6-2]
DR ProteomicsDB; 79281; -. [Q9BWH6-3]
DR Antibodypedia; 42079; 129 antibodies from 25 providers.
DR DNASU; 26015; -.
DR Ensembl; ENST00000304330.9; ENSP00000306123.4; ENSG00000103932.12. [Q9BWH6-1]
DR Ensembl; ENST00000562303.5; ENSP00000455363.1; ENSG00000103932.12. [Q9BWH6-2]
DR GeneID; 26015; -.
DR KEGG; hsa:26015; -.
DR MANE-Select; ENST00000304330.9; ENSP00000306123.4; NM_015540.4; NP_056355.2.
DR UCSC; uc001zod.5; human. [Q9BWH6-1]
DR CTD; 26015; -.
DR DisGeNET; 26015; -.
DR GeneCards; RPAP1; -.
DR HGNC; HGNC:24567; RPAP1.
DR HPA; ENSG00000103932; Low tissue specificity.
DR MIM; 611475; gene.
DR neXtProt; NX_Q9BWH6; -.
DR OpenTargets; ENSG00000103932; -.
DR PharmGKB; PA134914340; -.
DR VEuPathDB; HostDB:ENSG00000103932; -.
DR eggNOG; KOG1894; Eukaryota.
DR eggNOG; KOG4732; Eukaryota.
DR GeneTree; ENSGT00390000007594; -.
DR HOGENOM; CLU_005296_1_0_1; -.
DR InParanoid; Q9BWH6; -.
DR OMA; RMDKAPK; -.
DR PhylomeDB; Q9BWH6; -.
DR TreeFam; TF324391; -.
DR PathwayCommons; Q9BWH6; -.
DR SignaLink; Q9BWH6; -.
DR BioGRID-ORCS; 26015; 744 hits in 1090 CRISPR screens.
DR ChiTaRS; RPAP1; human.
DR GenomeRNAi; 26015; -.
DR Pharos; Q9BWH6; Tdark.
DR PRO; PR:Q9BWH6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BWH6; protein.
DR Bgee; ENSG00000103932; Expressed in hindlimb stylopod muscle and 122 other tissues.
DR ExpressionAtlas; Q9BWH6; baseline and differential.
DR Genevisible; Q9BWH6; HS.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR013929; RNA_pol_II_AP1_C.
DR InterPro; IPR013930; RNA_pol_II_AP1_N.
DR InterPro; IPR039913; RPAP1/Rba50.
DR PANTHER; PTHR21483; PTHR21483; 1.
DR Pfam; PF08620; RPAP1_C; 1.
DR Pfam; PF08621; RPAP1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1393
FT /note="RNA polymerase II-associated protein 1"
FT /id="PRO_0000284841"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..621
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024679"
FT VAR_SEQ 1266..1306
FT /note="LPVSLECYTVPPEDNLALLQLYFRTLVTGALRPRWCPVLYA -> VLSQPSR
FT TCKGTLHWASGAVLSLEELWKTSASSSYLLGALRGLRESMKRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_024680"
FT VAR_SEQ 1307..1393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_024681"
FT VARIANT 165
FT /note="K -> M (in dbSNP:rs2297382)"
FT /id="VAR_057738"
FT VARIANT 429
FT /note="R -> Q (in dbSNP:rs2289741)"
FT /id="VAR_057739"
FT VARIANT 506
FT /note="E -> K (in dbSNP:rs1200345)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_060348"
FT VARIANT 525
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs372712659)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036469"
FT VARIANT 582
FT /note="R -> G (in dbSNP:rs11630901)"
FT /id="VAR_057740"
FT VARIANT 825
FT /note="Q -> E (in dbSNP:rs8027526)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_060349"
FT VARIANT 1108
FT /note="R -> G (in dbSNP:rs7170898)"
FT /id="VAR_060350"
FT CONFLICT 760
FT /note="T -> A (in Ref. 3; BAB14247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1393 AA; 152755 MW; 0DB7C1B49590172F CRC64;
MLSRPKPGES EVDLLHFQSQ FLAAGAAPAV QLVKKGNRGG GDANSDRPPL QDHRDVVMLD
NLPDLPPALV PSPPKRARPS PGHCLPEDED PEERLRRHDQ HITAVLTKII ERDTSSVAVN
LPVPSGVAFP AVFLRSRDTQ GKSATSGKRS IFAQEIAARR IAEAKGPSVG EVVPNVGPPE
GAVTCETPTP RNQGCQLPGS SHSFQGPNLV TGKGLRDQEA EQEAQTIHEE NIARLQAMAP
EEILQEQQRL LAQLDPSLVA FLRSHSHTQE QTGETASEEQ RPGGPSANVT KEEPLMSAFA
SEPRKRDKLE PEAPALALPV TPQKEWLHMD TVELEKLHWT QDLPPVRRQQ TQERMQARFS
LQGELLAPDV DLPTHLGLHH HGEEAERAGY SLQELFHLTR SQVSQQRALA LHVLAQVISR
AQAGEFGDRL AGSVLSLLLD AGFLFLLRFS LDDRVDGVIA TAIRALRALL VAPGDEELLD
STFSWYHGAL TFPLMPSQED KEDEDEDEEC PAGKAKRKSP EEESRPPPDL ARHDVIKGLL
ATSLLPRLRY VLEVTYPGPA VVLDILAVLI RLARHSLESA TRVLECPRLI ETIVREFLPT
SWSPVGAGPT PSLYKVPCAT AMKLLRVLAS AGRNIAARLL SSFDLRSRLC RIIAEAPQEL
ALPPEEAEML STEALRLWAV AASYGQGGYL YRELYPVLMR ALQVVPRELS THPPQPLSMQ
RIASLLTLLT QLTLAAGSTP AETISDSAEA SLSATPSLVT WTQVSGLQPL VEPCLRQTLK
LLSRPEMWRA VGPVPVACLL FLGAYYQAWS QQPSSCPEDW LQDMQRLSEE LLLPLLSQPT
LGSLWDSLRH CSLLCNPLSC VPALEAPPSL VSLGCSGGCP RLSLAGSASP FPFLTALLSL
LNTLAQIHKG LCGQLAAILA APGLQNYFLQ CVAPGAAPHL TPFSAWALRH EYHLQYLALA
LAQKAAALQP LPATHAALYH GMALALLSRL LPGSEYLTHE LLLSCVFRLE FLPERTSGGP
EAADFSDQLS LGSSRVPRCG QGTLLAQACQ DLPSIRNCYL THCSPARASL LASQALHRGE
LQRVPTLLLP MPTEPLLPTD WPFLPLIRLY HRASDTPSGL SPTDTMGTAM RVLQWVLVLE
SWRPQALWAV PPAARLARLM CVFLVDSELF RESPVQHLVA ALLAQLCQPQ VLPNLNLDCR
LPGLTSFPDL YANFLDHFEA VSFGDHLFGA LVLLPLQRRF SVTLRLALFG EHVGALRALS
LPLTQLPVSL ECYTVPPEDN LALLQLYFRT LVTGALRPRW CPVLYAVAVA HVNSFIFSQD
PQSSDEVKAA RRSMLQKTWL LADEGLRQHL LHYKLPNSTL PEGFELYSQL PPLRQHYLQR
LTSTVLQNGV SET
