UBP32_HUMAN
ID UBP32_HUMAN Reviewed; 1604 AA.
AC Q8NFA0; Q7Z5T3; Q9BX85; Q9Y591;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 32;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 32;
DE AltName: Full=Renal carcinoma antigen NY-REN-60;
DE AltName: Full=Ubiquitin thioesterase 32;
DE AltName: Full=Ubiquitin-specific-processing protease 32;
DE Flags: Precursor;
GN Name=USP32; Synonyms=USP10;
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).
RC TISSUE=Brain;
RX PubMed=12604796; DOI=10.1073/pnas.0437015100;
RA Paulding C.A., Ruvolo M., Haber D.A.;
RT "The Tre2 (USP6) oncogene is a hominoid-specific gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2507-2511(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 331-1604 (ISOFORM 1).
RC TISSUE=Testis;
RA Sha J.H.;
RT "Identification of a novel ubiquitin specific protease gene related to
RT testes development from human testes cDNA library.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 536-1363 (ISOFORM 1), AND IDENTIFICATION AS A
RP RENAL CANCER ANTIGEN.
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [6]
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 [7]
RP ISOPRENYLATION AT CYS-1601.
RX PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
RA Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
RA Eisenhaber F.;
RT "Towards complete sets of farnesylated and geranylgeranylated proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1173, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1372, AND IDENTIFICATION BY
RP 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 [10]
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20549504; DOI=10.1007/s00335-010-9268-4;
RA Akhavantabasi S., Akman H.B., Sapmaz A., Keller J., Petty E.M., Erson A.E.;
RT "USP32 is an active, membrane-bound ubiquitin protease overexpressed in
RT breast cancers.";
RL Mamm. Genome 21:388-397(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1372, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1350; SER-1372; SER-1376 AND
RP SER-1588, AND 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:20549504};
CC -!- INTERACTION:
CC Q8NFA0; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-2511075, EBI-524753;
CC Q8NFA0-2; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-12220239, EBI-17439331;
CC Q8NFA0-2; P42858: HTT; NbExp=18; IntAct=EBI-12220239, EBI-466029;
CC Q8NFA0-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12220239, EBI-16439278;
CC Q8NFA0-2; O43639: NCK2; NbExp=5; IntAct=EBI-12220239, EBI-713635;
CC Q8NFA0-2; O75382: TRIM3; NbExp=3; IntAct=EBI-12220239, EBI-2129889;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:20549504}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NFA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFA0-2; Sequence=VSP_056307, VSP_056308;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF533230; AAM97922.1; -; mRNA.
DR EMBL; AF350251; AAK30207.1; -; mRNA.
DR EMBL; AC003962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC037475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054344; AAH54344.1; -; mRNA.
DR EMBL; AF155116; AAD42882.1; -; mRNA.
DR CCDS; CCDS32697.1; -. [Q8NFA0-1]
DR RefSeq; NP_115971.2; NM_032582.3. [Q8NFA0-1]
DR AlphaFoldDB; Q8NFA0; -.
DR SMR; Q8NFA0; -.
DR BioGRID; 124189; 124.
DR DIP; DIP-53613N; -.
DR IntAct; Q8NFA0; 48.
DR MINT; Q8NFA0; -.
DR STRING; 9606.ENSP00000300896; -.
DR MEROPS; C19.044; -.
DR MEROPS; C19.107; -.
DR iPTMnet; Q8NFA0; -.
DR PhosphoSitePlus; Q8NFA0; -.
DR SwissPalm; Q8NFA0; -.
DR BioMuta; USP32; -.
DR DMDM; 47606649; -.
DR EPD; Q8NFA0; -.
DR jPOST; Q8NFA0; -.
DR MassIVE; Q8NFA0; -.
DR MaxQB; Q8NFA0; -.
DR PaxDb; Q8NFA0; -.
DR PeptideAtlas; Q8NFA0; -.
DR PRIDE; Q8NFA0; -.
DR ProteomicsDB; 69353; -.
DR ProteomicsDB; 73280; -. [Q8NFA0-1]
DR Antibodypedia; 31170; 78 antibodies from 24 providers.
DR DNASU; 84669; -.
DR Ensembl; ENST00000300896.9; ENSP00000300896.3; ENSG00000170832.13. [Q8NFA0-1]
DR Ensembl; ENST00000393003.7; ENSP00000376727.2; ENSG00000170832.13. [Q8NFA0-2]
DR GeneID; 84669; -.
DR KEGG; hsa:84669; -.
DR MANE-Select; ENST00000300896.9; ENSP00000300896.3; NM_032582.4; NP_115971.2.
DR UCSC; uc002iyo.2; human. [Q8NFA0-1]
DR CTD; 84669; -.
DR DisGeNET; 84669; -.
DR GeneCards; USP32; -.
DR HGNC; HGNC:19143; USP32.
DR HPA; ENSG00000170832; Tissue enhanced (testis).
DR MIM; 607740; gene.
DR neXtProt; NX_Q8NFA0; -.
DR OpenTargets; ENSG00000170832; -.
DR PharmGKB; PA134982542; -.
DR VEuPathDB; HostDB:ENSG00000170832; -.
DR eggNOG; KOG0044; Eukaryota.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000155797; -.
DR HOGENOM; CLU_061823_0_0_1; -.
DR InParanoid; Q8NFA0; -.
DR OMA; TQTYRRK; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q8NFA0; -.
DR TreeFam; TF324190; -.
DR PathwayCommons; Q8NFA0; -.
DR SignaLink; Q8NFA0; -.
DR BioGRID-ORCS; 84669; 38 hits in 1123 CRISPR screens.
DR ChiTaRS; USP32; human.
DR GenomeRNAi; 84669; -.
DR Pharos; Q8NFA0; Tbio.
DR PRO; PR:Q8NFA0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8NFA0; protein.
DR Bgee; ENSG00000170832; Expressed in left testis and 193 other tissues.
DR ExpressionAtlas; Q8NFA0; baseline and differential.
DR Genevisible; Q8NFA0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; TAS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Golgi apparatus; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Phosphoprotein; Prenylation;
KW Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1601
FT /note="Ubiquitin carboxyl-terminal hydrolase 32"
FT /id="PRO_0000080663"
FT PROPEP 1602..1604
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396658"
FT DOMAIN 91..126
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 228..263
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 264..299
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 369..585
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 734..1567
FT /note="USP"
FT REGION 1343..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 743
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1526
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1173
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1601
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 1601
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 380..390
FT /note="GWLERESRYGL -> TLETDQIYTRN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056307"
FT VAR_SEQ 391..1604
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056308"
FT VARIANT 76
FT /note="H -> Y (in dbSNP:rs7208980)"
FT /id="VAR_051536"
FT VARIANT 1469
FT /note="A -> G (in dbSNP:rs3207630)"
FT /id="VAR_051537"
FT VARIANT 1568
FT /note="G -> R (in dbSNP:rs1053621)"
FT /id="VAR_051538"
FT VARIANT 1578
FT /note="T -> I (in dbSNP:rs1053625)"
FT /id="VAR_051539"
FT CONFLICT 884
FT /note="H -> R (in Ref. 2; AAK30207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1167
FT /note="C -> S (in Ref. 2; AAK30207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1604 AA; 181656 MW; A621F764B76321E3 CRC64;
MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSY YMGQHCFIRE VLGDGVPPKV
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG KDEEKAKYIF SLFSSESGNY VIREEMERML
HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL FLNKDAFTFS RWLLSGGVYV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW
KDNRTDDIPE LHMDLSDIVE GILNAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QAGHNWFIIS MQWWQQWKEY VKYDANPVVI
EPSSVLNGGK YSFGTAAHPM EQVEDRIGSS LSYVNTTEEK FSDNISTASE ASETAGSGFL
YSATPGADVC FARQHNTSDN NNQCLLGANG NILLHLNPQK PGAIDNQPLV TQEPVKATSL
TLEGGRLKRT PQLIHGRDYE MVPEPVWRAL YHWYGANLAL PRPVIKNSKT DIPELELFPR
YLLFLRQQPA TRTQQSNIWV NMGNVPSPNA PLKRVLAYTG CFSRMQTIKE IHEYLSQRLR
IKEEDMRLWL YNSENYLTLL DDEDHKLEYL KIQDEQHLVI EVRNKDMSWP EEMSFIANSS
KIDRHKVPTE KGATGLSNLG NTCFMNSSIQ CVSNTQPLTQ YFISGRHLYE LNRTNPIGMK
GHMAKCYGDL VQELWSGTQK NVAPLKLRWT IAKYAPRFNG FQQQDSQELL AFLLDGLHED
LNRVHEKPYV ELKDSDGRPD WEVAAEAWDN HLRRNRSIVV DLFHGQLRSQ VKCKTCGHIS
VRFDPFNFLS LPLPMDSYMH LEITVIKLDG TTPVRYGLRL NMDEKYTGLK KQLSDLCGLN
SEQILLAEVH GSNIKNFPQD NQKVRLSVSG FLCAFEIPVP VSPISASSPT QTDFSSSPST
NEMFTLTTNG DLPRPIFIPN GMPNTVVPCG TEKNFTNGMV NGHMPSLPDS PFTGYIIAVH
RKMMRTELYF LSSQKNRPSL FGMPLIVPCT VHTRKKDLYD AVWIQVSRLA SPLPPQEASN
HAQDCDDSMG YQYPFTLRVV QKDGNSCAWC PWYRFCRGCK IDCGEDRAFI GNAYIAVDWD
PTALHLRYQT SQERVVDEHE SVEQSRRAQA EPINLDSCLR AFTSEEELGE NEMYYCSKCK
THCLATKKLD LWRLPPILII HLKRFQFVNG RWIKSQKIVK FPRESFDPSA FLVPRDPALC
QHKPLTPQGD ELSEPRILAR EVKKVDAQSS AGEEDVLLSK SPSSLSANII SSPKGSPSSS
RKSGTSCPSS KNSSPNSSPR TLGRSKGRLR LPQIGSKNKL SSSKENLDAS KENGAGQICE
LADALSRGHV LGGSQPELVT PQDHEVALAN GFLYEHEACG NGYSNGQLGN HSEEDSTDDQ
REDTRIKPIY NLYAISCHSG ILGGGHYVTY AKNPNCKWYC YNDSSCKELH PDEIDTDSAY
ILFYEQQGID YAQFLPKTDG KKMADTSSMD EDFESDYKKY CVLQ
