UBP42_HUMAN
ID UBP42_HUMAN Reviewed; 1324 AA.
AC Q9H9J4; A2RUE3; B5MDA5; Q0VIN8; Q3C166; Q6P9B4;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 42;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 42;
DE AltName: Full=Ubiquitin thioesterase 42;
DE AltName: Full=Ubiquitin-specific-processing protease 42;
GN Name=USP42;
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), TISSUE SPECIFICITY, AND ENZYME
RP ACTIVITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Baek K.-H., Yoo K.-J.;
RT "A discovery of a novel deubiquitinating enzyme human USP42.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1202 (ISOFORM 1).
RC TISSUE=Placenta;
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 [LARGE SCALE MRNA] OF 1-1198.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1226, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, 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-75; SER-483; SER-754;
RP SER-856; SER-1181 AND SER-1247, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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-856, 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 -!- FUNCTION: Deubiquitinating enzyme which may play an important role
CC during spermatogenesis. {ECO:0000250}.
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:14715245};
CC -!- INTERACTION:
CC Q9H9J4; P04637: TP53; NbExp=2; IntAct=EBI-2513638, EBI-366083;
CC Q9H9J4-2; P04637: TP53; NbExp=2; IntAct=EBI-9118105, EBI-366083;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H9J4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9J4-2; Sequence=VSP_040529;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AJ601395; CAE53097.1; -; mRNA.
DR EMBL; AY618868; AAT67238.1; -; mRNA.
DR EMBL; AC004895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060846; AAH60846.2; -; mRNA.
DR EMBL; BC132862; AAI32863.1; -; mRNA.
DR EMBL; AK022759; BAB14232.1; -; mRNA.
DR CCDS; CCDS47535.1; -. [Q9H9J4-2]
DR RefSeq; NP_115548.1; NM_032172.2. [Q9H9J4-2]
DR AlphaFoldDB; Q9H9J4; -.
DR SMR; Q9H9J4; -.
DR BioGRID; 123904; 60.
DR IntAct; Q9H9J4; 34.
DR MINT; Q9H9J4; -.
DR STRING; 9606.ENSP00000301962; -.
DR MEROPS; C19.048; -.
DR iPTMnet; Q9H9J4; -.
DR PhosphoSitePlus; Q9H9J4; -.
DR BioMuta; USP42; -.
DR DMDM; 322510098; -.
DR EPD; Q9H9J4; -.
DR jPOST; Q9H9J4; -.
DR MassIVE; Q9H9J4; -.
DR MaxQB; Q9H9J4; -.
DR PaxDb; Q9H9J4; -.
DR PeptideAtlas; Q9H9J4; -.
DR PRIDE; Q9H9J4; -.
DR ProteomicsDB; 81325; -. [Q9H9J4-1]
DR ProteomicsDB; 81326; -. [Q9H9J4-2]
DR Antibodypedia; 1719; 107 antibodies from 27 providers.
DR DNASU; 84132; -.
DR Ensembl; ENST00000306177.10; ENSP00000301962.5; ENSG00000106346.12. [Q9H9J4-2]
DR GeneID; 84132; -.
DR KEGG; hsa:84132; -.
DR MANE-Select; ENST00000306177.10; ENSP00000301962.5; NM_032172.3; NP_115548.1. [Q9H9J4-2]
DR UCSC; uc011jwp.3; human. [Q9H9J4-1]
DR CTD; 84132; -.
DR DisGeNET; 84132; -.
DR GeneCards; USP42; -.
DR HGNC; HGNC:20068; USP42.
DR HPA; ENSG00000106346; Low tissue specificity.
DR neXtProt; NX_Q9H9J4; -.
DR OpenTargets; ENSG00000106346; -.
DR PharmGKB; PA134902515; -.
DR VEuPathDB; HostDB:ENSG00000106346; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000154596; -.
DR HOGENOM; CLU_005541_1_0_1; -.
DR InParanoid; Q9H9J4; -.
DR OMA; HVEKKAW; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; Q9H9J4; -.
DR TreeFam; TF315281; -.
DR PathwayCommons; Q9H9J4; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9H9J4; -.
DR BioGRID-ORCS; 84132; 18 hits in 1119 CRISPR screens.
DR ChiTaRS; USP42; human.
DR GeneWiki; USP42; -.
DR GenomeRNAi; 84132; -.
DR Pharos; Q9H9J4; Tbio.
DR PRO; PR:Q9H9J4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H9J4; protein.
DR Bgee; ENSG00000106346; Expressed in sperm and 189 other tissues.
DR ExpressionAtlas; Q9H9J4; baseline and differential.
DR Genevisible; Q9H9J4; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
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; Differentiation; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Spermatogenesis; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1324
FT /note="Ubiquitin carboxyl-terminal hydrolase 42"
FT /id="PRO_0000080672"
FT DOMAIN 111..412
FT /note="USP"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1209
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1245
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQC2"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RQC2"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1316..1324
FT /note="KRRYLELGR -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040529"
FT VARIANT 1030
FT /note="L -> P (in dbSNP:rs6463529)"
FT /id="VAR_059754"
FT CONFLICT 655
FT /note="M -> T (in Ref. 1; CAE53097 and 5; BAB14232)"
FT /evidence="ECO:0000305"
FT CONFLICT 1214
FT /note="R -> RR (in Ref. 1; CAE53097)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217
FT /note="Q -> R (in Ref. 4; AAT67238)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="K -> E (in Ref. 4; AAT67238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1324 AA; 145392 MW; 6EB4975521ABF516 CRC64;
MTIVDKASES SDPSAYQNQP GSSEAVSPGD MDAGSASWGA VSSLNDVSNH TLSLGPVPGA
VVYSSSSVPD KSKPSPQKDQ ALGDGIAPPQ KVLFPSEKIC LKWQQTHRVG AGLQNLGNTC
FANAALQCLT YTPPLANYML SHEHSKTCHA EGFCMMCTMQ AHITQALSNP GDVIKPMFVI
NEMRRIARHF RFGNQEDAHE FLQYTVDAMQ KACLNGSNKL DRHTQATTLV CQIFGGYLRS
RVKCLNCKGV SDTFDPYLDI TLEIKAAQSV NKALEQFVKP EQLDGENSYK CSKCKKMVPA
SKRFTIHRSS NVLTLSLKRF ANFTGGKIAK DVKYPEYLDI RPYMSQPNGE PIVYVLYAVL
VHTGFNCHAG HYFCYIKASN GLWYQMNDSI VSTSDIRSVL SQQAYVLFYI RSHDVKNGGE
LTHPTHSPGQ SSPRPVISQR VVTNKQAAPG FIGPQLPSHM IKNPPHLNGT GPLKDTPSSS
MSSPNGNSSV NRASPVNASA SVQNWSVNRS SVIPEHPKKQ KITISIHNKL PVRQCQSQPN
LHSNSLENPT KPVPSSTITN SAVQSTSNAS TMSVSSKVTK PIPRSESCSQ PVMNGKSKLN
SSVLVPYGAE SSEDSDEESK GLGKENGIGT IVSSHSPGQD AEDEEATPHE LQEPMTLNGA
NSADSDSDPK ENGLAPDGAS CQGQPALHSE NPFAKANGLP GKLMPAPLLS LPEDKILETF
RLSNKLKGST DEMSAPGAER GPPEDRDAEP QPGSPAAESL EEPDAAAGLS STKKAPPPRD
PGTPATKEGA WEAMAVAPEE PPPSAGEDIV GDTAPPDLCD PGSLTGDASP LSQDAKGMIA
EGPRDSALAE APEGLSPAPP ARSEEPCEQP LLVHPSGDHA RDAQDPSQSL GAPEAAERPP
APVLDMAPAG HPEGDAEPSP GERVEDAAAP KAPGPSPAKE KIGSLRKVDR GHYRSRRERS
SSGEPARESR SKTEGHRHRR RRTCPRERDR QDRHAPEHHP GHGDRLSPGE RRSLGRCSHH
HSRHRSGVEL DWVRHHYTEG ERGWGREKFY PDRPRWDRCR YYHDRYALYA ARDWKPFHGG
REHERAGLHE RPHKDHNRGR RGCEPARERE RHRPSSPRAG APHALAPHPD RFSHDRTALV
AGDNCNLSDR FHEHENGKSR KRRHDSVENS DSHVEKKARR SEQKDPLEEP KAKKHKKSKK
KKKSKDKHRD RDSRHQQDSD LSAACSDADL HRHKKKKKKK KRHSRKSEDF VKDSELHLPR
VTSLETVAQF RRAQGGFPLS GGPPLEGVGP FREKTKHLRM ESRDDRCRLF EYGQGKRRYL
ELGR
