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Database: UniProt
Entry: O75317
LinkDB: O75317
Original site: O75317 
ID   UBP12_HUMAN             Reviewed;         370 AA.
AC   O75317; A8K0X0; Q5VZV3; Q8TC49;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   29-SEP-2021, entry version 174.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 12;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 12;
DE   AltName: Full=Ubiquitin thioesterase 12;
DE   AltName: Full=Ubiquitin-hydrolyzing enzyme 1;
DE   AltName: Full=Ubiquitin-specific-processing protease 12;
GN   Name=USP12; Synonyms=UBH1, USP12L1;
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=9615226; DOI=10.1006/geno.1998.5275;
RA   Hansen-Hagge T.E., Janssen J.W.G., Hameister H., Papa F.R., Zechner U.,
RA   Seriu T., Jauch A., Becke D., Hochstrasser M., Bartram C.R.;
RT   "An evolutionarily conserved gene on human chromosome 5q33-q34, UBH1,
RT   encodes a novel deubiquitinating enzyme.";
RL   Genomics 49:411-418(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Amygdala;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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 BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION,
RP   INTERACTION WITH WDR48, AND MUTAGENESIS OF CYS-48.
RX   PubMed=19075014; DOI=10.1074/jbc.m808430200;
RA   Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.;
RT   "UAF1 is a subunit of multiple deubiquitinating enzyme complexes.";
RL   J. Biol. Chem. 284:5343-5351(2009).
RN   [7]
RP   SUBUNIT, ACTIVITY REGULATION, AND INTERACTION WITH WDR20.
RX   PubMed=20147737; DOI=10.1074/jbc.m109.095141;
RA   Kee Y., Yang K., Cohn M.A., Haas W., Gygi S.P., D'Andrea A.D.;
RT   "WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme
RT   complex.";
RL   J. Biol. Chem. 285:11252-11257(2010).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH PHLPP1.
RX   PubMed=24145035; DOI=10.1074/jbc.m113.503383;
RA   Gangula N.R., Maddika S.;
RT   "WD repeat protein WDR48 in complex with deubiquitinase USP12 suppresses
RT   Akt-dependent cell survival signaling by stabilizing PH domain leucine-rich
RT   repeat protein phosphatase 1 (PHLPP1).";
RL   J. Biol. Chem. 288:34545-34554(2013).
RN   [9] {ECO:0007744|PDB:5L8W}
RP   X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH WDR48 AND UBIQUITIN,
RP   ZINC-BINDING, INTERACTION WITH WDR48, AND MUTAGENESIS OF GLU-190.
RX   PubMed=27650958; DOI=10.1016/j.jsb.2016.09.011;
RA   Dharadhar S., Clerici M., van Dijk W.J., Fish A., Sixma T.K.;
RT   "A conserved two-step binding for the UAF1 regulator to the USP12
RT   deubiquitinating enzyme.";
RL   J. Struct. Biol. 196:437-447(2016).
RN   [10] {ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A, ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 40-370 IN COMPLEX WITH WDR20 AND
RP   WDR48, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH WRD20 AND WRD48,
RP   ZINC-BINDING, ACTIVE SITE, AND MUTAGENESIS OF CYS-48; 208-GLN--THR-210;
RP   PHE-219; GLN-240; GLU-241; TYR-264; VAL-279 AND PHE-287.
RX   PubMed=27373336; DOI=10.1016/j.molcel.2016.05.031;
RA   Li H., Lim K.S., Kim H., Hinds T.R., Jo U., Mao H., Weller C.E., Sun J.,
RA   Chatterjee C., D'Andrea A.D., Zheng N.;
RT   "Allosteric activation of ubiquitin-specific proteases by beta-propeller
RT   proteins UAF1 and WDR20.";
RL   Mol. Cell 63:249-260(2016).
CC   -!- FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating
CC       activity by itself and requires the interaction with WDR20 and WDR48 to
CC       have a high activity (PubMed:19075014, PubMed:27373336). Not involved
CC       in deubiquitination of monoubiquitinated FANCD2 (PubMed:19075014). In
CC       complex with WDR48, acts as a potential tumor suppressor by positively
CC       regulating PHLPP1 stability (PubMed:24145035).
CC       {ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:24145035,
CC       ECO:0000269|PubMed:27373336}.
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:19075014};
CC   -!- ACTIVITY REGULATION: Activated by interaction with WDR20 and WDR48
CC       through different allosteric mechanisms. {ECO:0000269|PubMed:20147737,
CC       ECO:0000269|PubMed:27373336}.
CC   -!- SUBUNIT: Interacts with WDR48 (PubMed:19075014, PubMed:27650958,
CC       PubMed:27373336). Interacts with WDR20 (PubMed:20147737,
CC       PubMed:27373336). Component of the USP12/WDR20/WDR48 deubiquitinating
CC       complex (PubMed:20147737, PubMed:27373336). Interacts with PHLPP1
CC       (PubMed:24145035). {ECO:0000269|PubMed:19075014,
CC       ECO:0000269|PubMed:20147737, ECO:0000269|PubMed:24145035,
CC       ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:27650958}.
CC   -!- INTERACTION:
CC       O75317; P27797: CALR; NbExp=3; IntAct=EBI-2511507, EBI-1049597;
CC       O75317; P36957: DLST; NbExp=3; IntAct=EBI-2511507, EBI-351007;
CC       O75317; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-2511507, EBI-1055945;
CC       O75317; Q8TBZ3: WDR20; NbExp=5; IntAct=EBI-2511507, EBI-2511486;
CC   -!- MISCELLANEOUS: Knockdown of USP12 increases Akt activation.
CC       {ECO:0000269|PubMed:24145035}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF022789; AAC23551.1; ALT_INIT; mRNA.
DR   EMBL; AK289685; BAF82374.1; -; mRNA.
DR   EMBL; AL158062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL355473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08392.1; -; Genomic_DNA.
DR   EMBL; BC026072; AAH26072.1; -; mRNA.
DR   CCDS; CCDS31952.1; -.
DR   RefSeq; NP_872294.2; NM_182488.3.
DR   PDB; 5K16; X-ray; 2.60 A; A/B=16-370.
DR   PDB; 5K1A; X-ray; 2.30 A; A/C/E/G=40-370.
DR   PDB; 5K1B; X-ray; 3.30 A; A=4-370.
DR   PDB; 5K1C; X-ray; 3.00 A; A=16-370.
DR   PDB; 5L8W; X-ray; 2.79 A; A=1-370.
DR   PDBsum; 5K16; -.
DR   PDBsum; 5K1A; -.
DR   PDBsum; 5K1B; -.
DR   PDBsum; 5K1C; -.
DR   PDBsum; 5L8W; -.
DR   SMR; O75317; -.
DR   BioGRID; 128522; 43.
DR   CORUM; O75317; -.
DR   IntAct; O75317; 30.
DR   MINT; O75317; -.
DR   STRING; 9606.ENSP00000282344; -.
DR   MEROPS; C19.020; -.
DR   iPTMnet; O75317; -.
DR   PhosphoSitePlus; O75317; -.
DR   BioMuta; USP12; -.
DR   EPD; O75317; -.
DR   jPOST; O75317; -.
DR   MassIVE; O75317; -.
DR   MaxQB; O75317; -.
DR   PaxDb; O75317; -.
DR   PeptideAtlas; O75317; -.
DR   PRIDE; O75317; -.
DR   ProteomicsDB; 49890; -.
DR   Antibodypedia; 22631; 274 antibodies.
DR   DNASU; 219333; -.
DR   Ensembl; ENST00000282344; ENSP00000282344; ENSG00000152484.
DR   GeneID; 219333; -.
DR   KEGG; hsa:219333; -.
DR   UCSC; uc001uqy.4; human.
DR   CTD; 219333; -.
DR   DisGeNET; 219333; -.
DR   GeneCards; USP12; -.
DR   HGNC; HGNC:20485; USP12.
DR   HPA; ENSG00000152484; Low tissue specificity.
DR   MIM; 603091; gene.
DR   neXtProt; NX_O75317; -.
DR   OpenTargets; ENSG00000152484; -.
DR   PharmGKB; PA37236; -.
DR   VEuPathDB; HostDB:ENSG00000152484; -.
DR   eggNOG; KOG1864; Eukaryota.
DR   GeneTree; ENSGT00940000153284; -.
DR   HOGENOM; CLU_008279_2_0_1; -.
DR   InParanoid; O75317; -.
DR   OMA; RIKKPPQ; -.
DR   OrthoDB; 378361at2759; -.
DR   PhylomeDB; O75317; -.
DR   TreeFam; TF314144; -.
DR   PathwayCommons; O75317; -.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 219333; 35 hits in 1054 CRISPR screens.
DR   ChiTaRS; USP12; human.
DR   GenomeRNAi; 219333; -.
DR   Pharos; O75317; Tbio.
DR   PRO; PR:O75317; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; O75317; protein.
DR   Bgee; ENSG00000152484; Expressed in esophagogastric junction muscularis propria and 244 other tissues.
DR   ExpressionAtlas; O75317; baseline and differential.
DR   Genevisible; O75317; 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:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:thiol-dependent deubiquitinase; IDA:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
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   3D-structure; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway; Zinc.
FT   CHAIN           1..370
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 12"
FT                   /id="PRO_0000080634"
FT   DOMAIN          39..369
FT                   /note="USP"
FT   REGION          145..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   METAL           186
FT                   /note="Zinc"
FT                   /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A,
FT                   ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5L8W"
FT   METAL           189
FT                   /note="Zinc"
FT                   /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A,
FT                   ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C,
FT                   ECO:0007744|PDB:5L8W"
FT   METAL           233
FT                   /note="Zinc"
FT                   /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A,
FT                   ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C,
FT                   ECO:0007744|PDB:5L8W"
FT   METAL           236
FT                   /note="Zinc"
FT                   /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A,
FT                   ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5K1C,
FT                   ECO:0007744|PDB:5L8W"
FT   MUTAGEN         48
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         48
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19075014"
FT   MUTAGEN         190
FT                   /note="E->K: Impaired binding to WDR48."
FT                   /evidence="ECO:0000269|PubMed:27650958"
FT   MUTAGEN         208..210
FT                   /note="QNT->GGG: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         219
FT                   /note="F->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         240
FT                   /note="Q->A: Impaired binding to WDR48; when associated
FT                   with Ala-241."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         241
FT                   /note="E->A: Impaired binding to WDR48; when associated
FT                   with Ala-240."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         264
FT                   /note="Y->A: Strong reduction of activity."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         279
FT                   /note="V->D: Impaired binding to WDR20; when associated
FT                   with Ala-287."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         287
FT                   /note="F->A: Impaired binding to WDR20; when associated
FT                   with Asp-279."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   CONFLICT        173
FT                   /note="H -> D (in Ref. 5; AAH26072)"
FT                   /evidence="ECO:0000305"
FT   HELIX           22..27
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           47..58
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           61..68
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   HELIX           128..146
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           171..176
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          178..186
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          192..204
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          208..211
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   HELIX           212..217
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   TURN            234..237
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          242..250
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   TURN            266..269
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   STRAND          270..273
FT                   /evidence="ECO:0007829|PDB:5K16"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          299..308
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          317..324
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          327..332
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          335..339
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   TURN            341..343
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   HELIX           344..347
FT                   /evidence="ECO:0007829|PDB:5K1A"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:5L8W"
FT   STRAND          362..368
FT                   /evidence="ECO:0007829|PDB:5K1A"
SQ   SEQUENCE   370 AA;  42858 MW;  267EE6A3674F6440 CRC64;
     MEILMTVSKF ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
     RPFREKVLAY KSQPRKKESL LTCLADLFHS IATQKKKVGV IPPKKFITRL RKENELFDNY
     MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLPNGNIDN ENNNSTPDPT WVHEIFQGTL
     TNETRCLTCE TISSKDEDFL DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ
     EAHKRMKVKK LPMILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY
     DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL TSDISKNSES
     GYILFYQSRD
//
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