SENP3_HUMAN
ID SENP3_HUMAN Reviewed; 574 AA.
AC Q9H4L4; Q66K15; Q86VS7; Q96PS4; Q9Y3W9;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sentrin-specific protease 3;
DE EC=3.4.22.-;
DE AltName: Full=SUMO-1-specific protease 3;
DE AltName: Full=Sentrin/SUMO-specific protease SENP3;
GN Name=SENP3 {ECO:0000303|PubMed:16608850, ECO:0000303|PubMed:18259216,
GN ECO:0000312|HGNC:HGNC:17862}; Synonyms=SSP3, SUSP3;
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].
RX PubMed=10806345; DOI=10.1016/s0378-1119(00)00139-6;
RA Yeh E.T.H., Gong L., Kamitani T.;
RT "Ubiquitin-like proteins: new wines in new bottles.";
RL Gene 248:1-14(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S.,
RA Shimbara N., Tanaka K., Chung C.H.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, and Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and 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 IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [7]
RP FUNCTION.
RX PubMed=15743823; DOI=10.1128/mcb.25.6.2273-2287.2005;
RA Gregoire S., Yang X.-J.;
RT "Association with class IIa histone deacetylases upregulates the
RT sumoylation of MEF2 transcription factors.";
RL Mol. Cell. Biol. 25:2273-2287(2005).
RN [8]
RP FUNCTION.
RX PubMed=16608850; DOI=10.1074/jbc.m511658200;
RA Gong L., Yeh E.T.H.;
RT "Characterization of a family of nucleolar SUMO-specific proteases with
RT preference for SUMO-2 or SUMO-3.";
RL J. Biol. Chem. 281:15869-15877(2006).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-532, AND INTERACTION WITH NPM1.
RX PubMed=18259216; DOI=10.1038/embor.2008.3;
RA Haindl M., Harasim T., Eick D., Muller S.;
RT "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of
RT nucleophosmin and is required for rRNA processing.";
RL EMBO Rep. 9:273-279(2008).
RN [10]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH NPM1.
RX PubMed=19015314; DOI=10.1083/jcb.200807185;
RA Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A.,
RA Wilkinson K.D., Dasso M.;
RT "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway
RT through SENP3 and SENP5 proteases.";
RL J. Cell Biol. 183:589-595(2008).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH
RP EP300.
RX PubMed=19680224; DOI=10.1038/emboj.2009.210;
RA Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H.,
RA Li H., Shi G., Cheng J., Tang X., Yi J.;
RT "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress
RT via p300 de-SUMOylation.";
RL EMBO J. 28:2748-2762(2009).
RN [13]
RP FUNCTION, AND INTERACTION WITH CDCA8.
RX PubMed=18946085; DOI=10.1091/mbc.e08-05-0511;
RA Klein U.R., Haindl M., Nigg E.A., Muller S.;
RT "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation
RT cycle on Borealin.";
RL Mol. Biol. Cell 20:410-418(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION, AND IDENTIFICATION IN THE 5FMC COMPLEX.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, 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 [17]
RP INTERACTION WITH CCAR2.
RX PubMed=25406032; DOI=10.1038/ncomms6483;
RA Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W., Ka S.H.,
RA Oh K.H., Jeon Y.J., Chung C.H.;
RT "Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in
RT response to DNA damage.";
RL Nat. Commun. 5:5483-5483(2014).
RN [18]
RP FUNCTION.
RX PubMed=32832608; DOI=10.1126/sciadv.aba7822;
RA Gao S.S., Guan H., Yan S., Hu S., Song M., Guo Z.P., Xie D.F., Liu Y.,
RA Liu X., Zhang S., Zhou P.K.;
RT "TIP60 K430 SUMOylation attenuates its interaction with DNA-PKcs in S-phase
RT cells: Facilitating homologous recombination and emerging target for cancer
RT therapy.";
RL Sci. Adv. 6:eaba7822-eaba7822(2020).
CC -!- FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from
CC sumoylated substrates, but has only weak activity against SUMO1
CC conjugates (PubMed:16608850, PubMed:32832608). Deconjugates SUMO2 from
CC MEF2D, which increases its transcriptional activation capability
CC (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8
CC (PubMed:18946085). Redox sensor that, when redistributed into
CC nucleoplasm, can act as an effector to enhance HIF1A transcriptional
CC activity by desumoylating EP300 (PubMed:19680224). Required for rRNA
CC processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin,
CC NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation
CC status of ZNF148 (PubMed:18259216). Functions as a component of the
CC Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is
CC recruited to ZNF148 by methylated CHTOP, leading to desumoylation of
CC ZNF148 and subsequent transactivation of ZNF148 target genes
CC (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608).
CC {ECO:0000269|PubMed:15743823, ECO:0000269|PubMed:16608850,
CC ECO:0000269|PubMed:18259216, ECO:0000269|PubMed:18946085,
CC ECO:0000269|PubMed:19015314, ECO:0000269|PubMed:19680224,
CC ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:32832608}.
CC -!- ACTIVITY REGULATION: On oxidative stress, SENP3 degradation is blocked
CC by inhibition of its ubiquitination, which stabilizes it as it
CC accumulates in the nucleoplasm. {ECO:0000269|PubMed:19680224}.
CC -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
CC as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (PubMed:15960975). Interacts with EP300, NPM1 and CDCA8
CC (PubMed:19015314, PubMed:18946085, PubMed:18259216, PubMed:19680224).
CC Component of the 5FMC complex, at least composed of PELP1, LAS1L,
CC TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and
CC ZNF148 (PubMed:22872859). Interacts with NOL9 (By similarity).
CC Interacts with CCAR2 (PubMed:25406032). {ECO:0000250|UniProtKB:Q9EP97,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:18259216,
CC ECO:0000269|PubMed:18946085, ECO:0000269|PubMed:19015314,
CC ECO:0000269|PubMed:19680224, ECO:0000269|PubMed:22872859,
CC ECO:0000269|PubMed:25406032}.
CC -!- INTERACTION:
CC Q9H4L4; Q96LK0: CEP19; NbExp=3; IntAct=EBI-2880236, EBI-741885;
CC Q9H4L4; P06748: NPM1; NbExp=6; IntAct=EBI-2880236, EBI-78579;
CC Q9H4L4; Q8IZL8: PELP1; NbExp=5; IntAct=EBI-2880236, EBI-716449;
CC Q9H4L4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2880236, EBI-5235340;
CC Q9H4L4; Q9NXF1: TEX10; NbExp=2; IntAct=EBI-2880236, EBI-2371062;
CC Q9H4L4; P0CG48: UBC; NbExp=2; IntAct=EBI-2880236, EBI-3390054;
CC Q9H4L4; Q9BV38: WDR18; NbExp=4; IntAct=EBI-2880236, EBI-727429;
CC Q9H4L4; O76024: WFS1; NbExp=3; IntAct=EBI-2880236, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19680224}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:19015314,
CC ECO:0000269|PubMed:19680224}. Cytoplasm {ECO:0000250|UniProtKB:Q9EP97}.
CC Note=Redistributes between the nucleolus and the nucleoplasm in
CC response to mild oxidative stress (PubMed:19680224). Mainly found in
CC the nucleoplasm, with low levels detected in the cytoplasmic and
CC chromatin fractions (By similarity). {ECO:0000250|UniProtKB:Q9EP97,
CC ECO:0000269|PubMed:19680224}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AY008763; AAG33252.1; -; mRNA.
DR EMBL; AF199459; AAL25652.1; -; mRNA.
DR EMBL; AL050283; CAB43384.2; -; mRNA.
DR EMBL; AL834294; CAD38967.1; -; mRNA.
DR EMBL; BC048306; AAH48306.1; -; mRNA.
DR EMBL; BC080658; AAH80658.1; -; mRNA.
DR CCDS; CCDS73958.1; -.
DR PIR; T08759; T08759.
DR RefSeq; NP_056485.2; NM_015670.5.
DR AlphaFoldDB; Q9H4L4; -.
DR SMR; Q9H4L4; -.
DR BioGRID; 117594; 308.
DR CORUM; Q9H4L4; -.
DR DIP; DIP-47511N; -.
DR IntAct; Q9H4L4; 48.
DR MINT; Q9H4L4; -.
DR STRING; 9606.ENSP00000314029; -.
DR MEROPS; C48.003; -.
DR iPTMnet; Q9H4L4; -.
DR PhosphoSitePlus; Q9H4L4; -.
DR SwissPalm; Q9H4L4; -.
DR BioMuta; SENP3; -.
DR DMDM; 119370525; -.
DR EPD; Q9H4L4; -.
DR jPOST; Q9H4L4; -.
DR MassIVE; Q9H4L4; -.
DR MaxQB; Q9H4L4; -.
DR PaxDb; Q9H4L4; -.
DR PeptideAtlas; Q9H4L4; -.
DR PRIDE; Q9H4L4; -.
DR ProteomicsDB; 80851; -.
DR Antibodypedia; 24161; 249 antibodies from 31 providers.
DR DNASU; 26168; -.
DR Ensembl; ENST00000321337.12; ENSP00000314029.8; ENSG00000161956.13.
DR Ensembl; ENST00000429205.6; ENSP00000403712.2; ENSG00000161956.13.
DR GeneID; 26168; -.
DR KEGG; hsa:26168; -.
DR MANE-Select; ENST00000321337.12; ENSP00000314029.8; NM_015670.6; NP_056485.2.
DR UCSC; uc032esp.2; human.
DR CTD; 26168; -.
DR DisGeNET; 26168; -.
DR GeneCards; SENP3; -.
DR HGNC; HGNC:17862; SENP3.
DR HPA; ENSG00000161956; Low tissue specificity.
DR MIM; 612844; gene.
DR neXtProt; NX_Q9H4L4; -.
DR OpenTargets; ENSG00000161956; -.
DR PharmGKB; PA134933213; -.
DR VEuPathDB; HostDB:ENSG00000161956; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000156309; -.
DR HOGENOM; CLU_035238_0_0_1; -.
DR InParanoid; Q9H4L4; -.
DR OMA; YCKYLAL; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q9H4L4; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B72; 2681.
DR PathwayCommons; Q9H4L4; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9H4L4; -.
DR SIGNOR; Q9H4L4; -.
DR BioGRID-ORCS; 26168; 14 hits in 267 CRISPR screens.
DR GeneWiki; SENP3; -.
DR GenomeRNAi; 26168; -.
DR Pharos; Q9H4L4; Tbio.
DR PRO; PR:Q9H4L4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H4L4; protein.
DR Bgee; ENSG00000161956; Expressed in right hemisphere of cerebellum and 109 other tissues.
DR ExpressionAtlas; Q9H4L4; baseline and differential.
DR Genevisible; Q9H4L4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; IMP:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR037945; SENP3.
DR InterPro; IPR045577; SENP3_5_cons_dom.
DR PANTHER; PTHR12606:SF16; PTHR12606:SF16; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF19722; SENP3_5_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..574
FT /note="Sentrin-specific protease 3"
FT /id="PRO_0000101721"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..543
FT /note="Protease"
FT MOTIF 125..128
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 153..159
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 74..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 482
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 532
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18259216"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EP97"
FT VARIANT 515
FT /note="W -> R (in dbSNP:rs9972914)"
FT /id="VAR_051544"
FT MUTAGEN 532
FT /note="C->S: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18259216"
FT CONFLICT 30..31
FT /note="ER -> DG (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> T (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> A (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="PS -> AL (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="T -> S (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> Q (in Ref. 1; AAG33252)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="L -> S (in Ref. 5; AAH48306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65010 MW; E495137EE7500741 CRC64;
MKETIQGTGS WGPEPPGPGI PPAYSSPRRE RLRWPPPPKP RLKSGGGFGP DPGSGTTVPA
RRLPVPRPSF DASASEEEEE EEEEEDEDEE EEVAAWRLPP RWSQLGTSQR PRPSRPTHRK
TCSQRRRRAM RAFRMLLYSK STSLTFHWKL WGRHRGRRRG LAHPKNHLSP QQGGATPQVP
SPCCRFDSPR GPPPPRLGLL GALMAEDGVR GSPPVPSGPP MEEDGLRWTP KSPLDPDSGL
LSCTLPNGFG GQSGPEGERS LAPPDASILI SNVCSIGDHV AQELFQGSDL GMAEEAERPG
EKAGQHSPLR EEHVTCVQSI LDEFLQTYGS LIPLSTDEVV EKLEDIFQQE FSTPSRKGLV
LQLIQSYQRM PGNAMVRGFR VAYKRHVLTM DDLGTLYGQN WLNDQVMNMY GDLVMDTVPE
KVHFFNSFFY DKLRTKGYDG VKRWTKNVDI FNKELLLIPI HLEVHWSLIS VDVRRRTITY
FDSQRTLNRR CPKHIAKYLQ AEAVKKDRLD FHQGWKGYFK MNVARQNNDS DCGAFVLQYC
KHLALSQPFS FTQQDMPKLR RQIYKELCHC KLTV
