PR40B_HUMAN
ID PR40B_HUMAN Reviewed; 871 AA.
AC Q6NWY9; O75401; Q6PI09; Q6ZWB3; Q8NCZ1; Q9H5G4; Q9NT95;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pre-mRNA-processing factor 40 homolog B;
DE AltName: Full=Huntingtin yeast partner C;
DE AltName: Full=Huntingtin-interacting protein C;
GN Name=PRPF40B; Synonyms=HYPC;
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 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 494-871 (ISOFORM 3).
RC TISSUE=Caudate nucleus, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 419-871 (ISOFORM 3).
RC TISSUE=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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-785 (ISOFORM 3).
RC TISSUE=Ovary, and Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-179 (ISOFORMS 1/2/3), FUNCTION,
RP INTERACTION WITH HD, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10958656; DOI=10.1093/hmg/9.14.2175;
RA Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H.,
RA Gusella J.F., Vonsattel J.-P., MacDonald M.E.;
RT "Huntingtin's WW domain partners in Huntington's disease post-mortem brain
RT fulfill genetic criteria for direct involvement in Huntington's disease
RT pathogenesis.";
RL Hum. Mol. Genet. 9:2175-2182(2000).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764, AND IDENTIFICATION BY
RP 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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-838, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-838, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in pre-mRNA splicing.
CC {ECO:0000269|PubMed:9700202}.
CC -!- SUBUNIT: Interacts with the N-terminus of HD.
CC {ECO:0000269|PubMed:9700202}.
CC -!- INTERACTION:
CC Q6NWY9; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-11285481, EBI-12121668;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10958656}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6NWY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NWY9-2; Sequence=VSP_029117, VSP_029118;
CC Name=3;
CC IsoId=Q6NWY9-3; Sequence=VSP_029119;
CC Name=4;
CC IsoId=Q6NWY9-4; Sequence=VSP_029116, VSP_029120, VSP_029121;
CC -!- TISSUE SPECIFICITY: Expressed in the striatum and cortex of the brain
CC (at protein level). Highly expressed in testis, fetal kidney and fetal
CC brain. Moderately expressed in pancreas, skeletal muscle, placenta,
CC brain and heart. Weakly expressed in colon, ileum, ovary, prostate,
CC spleen, kidney and fetal lung. {ECO:0000269|PubMed:10958656,
CC ECO:0000269|PubMed:9700202}.
CC -!- SIMILARITY: Belongs to the PRPF40 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB15662.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK027117; BAB15662.1; ALT_FRAME; mRNA.
DR EMBL; AK123353; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL137459; CAB70747.1; -; mRNA.
DR EMBL; AL834216; CAD38898.1; -; mRNA.
DR EMBL; CH471111; EAW58085.1; -; Genomic_DNA.
DR EMBL; BC050398; AAH50398.1; ALT_SEQ; mRNA.
DR EMBL; BC067364; AAH67364.1; -; mRNA.
DR EMBL; AF049525; AAC27503.1; -; mRNA.
DR PIR; T46402; T46402.
DR RefSeq; NP_001026868.2; NM_001031698.2.
DR RefSeq; NP_036404.1; NM_012272.2. [Q6NWY9-2]
DR RefSeq; XP_011536443.1; XM_011538141.1.
DR AlphaFoldDB; Q6NWY9; -.
DR SMR; Q6NWY9; -.
DR BioGRID; 117305; 19.
DR IntAct; Q6NWY9; 10.
DR MINT; Q6NWY9; -.
DR STRING; 9606.ENSP00000448073; -.
DR iPTMnet; Q6NWY9; -.
DR PhosphoSitePlus; Q6NWY9; -.
DR BioMuta; PRPF40B; -.
DR DMDM; 74736936; -.
DR EPD; Q6NWY9; -.
DR jPOST; Q6NWY9; -.
DR MassIVE; Q6NWY9; -.
DR MaxQB; Q6NWY9; -.
DR PaxDb; Q6NWY9; -.
DR PeptideAtlas; Q6NWY9; -.
DR PRIDE; Q6NWY9; -.
DR ProteomicsDB; 66741; -. [Q6NWY9-1]
DR ProteomicsDB; 66742; -. [Q6NWY9-2]
DR ProteomicsDB; 66743; -. [Q6NWY9-3]
DR Antibodypedia; 42895; 34 antibodies from 15 providers.
DR DNASU; 25766; -.
DR Ensembl; ENST00000261897.5; ENSP00000261897.1; ENSG00000110844.14. [Q6NWY9-2]
DR Ensembl; ENST00000380281.5; ENSP00000369634.1; ENSG00000110844.14. [Q6NWY9-1]
DR GeneID; 25766; -.
DR KEGG; hsa:25766; -.
DR UCSC; uc058nrq.1; human. [Q6NWY9-1]
DR CTD; 25766; -.
DR DisGeNET; 25766; -.
DR GeneCards; PRPF40B; -.
DR HGNC; HGNC:25031; PRPF40B.
DR HPA; ENSG00000110844; Low tissue specificity.
DR neXtProt; NX_Q6NWY9; -.
DR OpenTargets; ENSG00000110844; -.
DR PharmGKB; PA143485582; -.
DR VEuPathDB; HostDB:ENSG00000110844; -.
DR eggNOG; KOG0152; Eukaryota.
DR eggNOG; KOG0155; Eukaryota.
DR GeneTree; ENSGT00930000150980; -.
DR InParanoid; Q6NWY9; -.
DR OrthoDB; 1112854at2759; -.
DR PhylomeDB; Q6NWY9; -.
DR TreeFam; TF318732; -.
DR PathwayCommons; Q6NWY9; -.
DR SignaLink; Q6NWY9; -.
DR BioGRID-ORCS; 25766; 30 hits in 1078 CRISPR screens.
DR ChiTaRS; PRPF40B; human.
DR GeneWiki; PRPF40B; -.
DR GenomeRNAi; 25766; -.
DR Pharos; Q6NWY9; Tdark.
DR PRO; PR:Q6NWY9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6NWY9; protein.
DR Bgee; ENSG00000110844; Expressed in right lobe of thyroid gland and 122 other tissues.
DR ExpressionAtlas; Q6NWY9; baseline and differential.
DR Genevisible; Q6NWY9; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 1.10.10.440; -; 5.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR039726; Prp40-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11864; PTHR11864; 1.
DR Pfam; PF01846; FF; 2.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 4.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF81698; SSF81698; 5.
DR PROSITE; PS51676; FF; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..871
FT /note="Pre-mRNA-processing factor 40 homolog B"
FT /id="PRO_0000309282"
FT DOMAIN 92..125
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 133..166
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 276..330
FT /note="FF 1"
FT DOMAIN 340..397
FT /note="FF 2"
FT DOMAIN 410..470
FT /note="FF 3"
FT DOMAIN 490..550
FT /note="FF 4"
FT DOMAIN 554..610
FT /note="FF 5"
FT DOMAIN 625..682
FT /note="FF 6"
FT REGION 171..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..711
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..791
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80W14"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 838
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..7
FT /note="MMPPPFM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029117"
FT VAR_SEQ 1..6
FT /note="MMPPPF -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029116"
FT VAR_SEQ 77..200
FT /note="TAPGADTASSAVAGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKS
FT KAELLLSQCPWKEYKSDTGKPYYYNNQSKESRWTRPKDLDDLEVLVKQEAAGKQQQQLP
FT QTLQPQPPQPQPD -> VSTRGQQVAGSALQSRESDLECRTMTSILSLFSSHPPRSPAA
FT LPTLKSFSPAMYSALLVSHSSPKAYTFSCYSRALSSSLKEHTYPHRATHCGHMNIVLHI
FT LFVPRRVSSTWGSCCAFLCYRSV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029120"
FT VAR_SEQ 201..871
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029121"
FT VAR_SEQ 568..574
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029118"
FT VAR_SEQ 685
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_029119"
SQ SEQUENCE 871 AA; 99358 MW; BB62C95BEFB9D23A CRC64;
MMPPPFMPPP GIPPPFPPMG LPPMSQRPPA IPPMPPGILP PMLPPMGAPP PLTQIPGMVP
PMMPGMLMPA VPVTAATAPG ADTASSAVAG TGPPRALWSE HVAPDGRIYY YNADDKQSVW
EKPSVLKSKA ELLLSQCPWK EYKSDTGKPY YYNNQSKESR WTRPKDLDDL EVLVKQEAAG
KQQQQLPQTL QPQPPQPQPD PPPVPPGPTP VPTGLLEPEP GGSEDCDVLE ATQPLEQGFL
QQLEEGPSSS GQHQPQQEEE ESKPEPERSG LSWSNREKAK QAFKELLRDK AVPSNASWEQ
AMKMVVTDPR YSALPKLSEK KQAFNAYKAQ REKEEKEEAR LRAKEAKQTL QHFLEQHERM
TSTTRYRRAE QTFGELEVWA VVPERDRKEV YDDVLFFLAK KEKEQAKQLR RRNIQALKSI
LDGMSSVNFQ TTWSQAQQYL MDNPSFAQDH QLQNMDKEDA LICFEEHIRA LEREEEEERE
RARLRERRQQ RKNREAFQTF LDELHETGQL HSMSTWMELY PAVSTDVRFA NMLGQPGSTP
LDLFKFYVEE LKARFHDEKK IIKDILKDRG FCVEVNTAFE DFAHVISFDK RAAALDAGNI
KLTFNSLLEK AEAREREREK EEARRMRRRE AAFRSMLRQA VPALELGTAW EEVRERFVCD
SAFEQITLES ERIRLFREFL QVLEQTECQH LHTKGRKHGR KGKKHHHKRS HSPSGSESEE
EELPPPSLRP PKRRRRNPSE SGSEPSSSLD SVESGGAALG GRGSPSSHLL GADHGLRKAK
KPKKKTKKRR HKSNSPESET DPEEKAGKES DEKEQEQDKD RELQQAELPN RSPGFGIKKE
KTGWDTSESE LSEGELERRR RTLLQQLDDH Q
