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   07-OCT-2020, entry version 142.
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   BioGRID; 117487; 61.
DR   CORUM; Q9BWH6; -.
DR   IntAct; Q9BWH6; 16.
DR   MINT; Q9BWH6; -.
DR   STRING; 9606.ENSP00000306123; -.
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; 117 antibodies.
DR   DNASU; 26015; -.
DR   Ensembl; ENST00000304330; ENSP00000306123; ENSG00000103932. [Q9BWH6-1]
DR   Ensembl; ENST00000562303; ENSP00000455363; ENSG00000103932. [Q9BWH6-2]
DR   GeneID; 26015; -.
DR   KEGG; hsa:26015; -.
DR   UCSC; uc001zod.5; human. [Q9BWH6-1]
DR   CTD; 26015; -.
DR   DisGeNET; 26015; -.
DR   EuPathDB; HostDB:ENSG00000103932.11; -.
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   eggNOG; KOG1894; Eukaryota.
DR   eggNOG; KOG4732; Eukaryota.
DR   GeneTree; ENSGT00390000007594; -.
DR   HOGENOM; CLU_005296_1_0_1; -.
DR   InParanoid; Q9BWH6; -.
DR   KO; K20826; -.
DR   OMA; LRPRWCP; -.
DR   PhylomeDB; Q9BWH6; -.
DR   TreeFam; TF324391; -.
DR   PathwayCommons; Q9BWH6; -.
DR   BioGRID-ORCS; 26015; 710 hits in 883 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 169 other tissues.
DR   ExpressionAtlas; Q9BWH6; baseline and differential.
DR   Genevisible; Q9BWH6; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase 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; Polymorphism;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1393
FT                   /note="RNA polymerase II-associated protein 1"
FT                   /id="PRO_0000284841"
FT   COMPBIAS        827..1286
FT                   /note="Leu-rich"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         321
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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
//