UBP12_HUMAN
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 03-AUG-2022, entry version 177.
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 AlphaFoldDB; O75317; -.
DR SMR; O75317; -.
DR BioGRID; 128522; 70.
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; 279 antibodies from 27 providers.
DR DNASU; 219333; -.
DR Ensembl; ENST00000282344.11; ENSP00000282344.6; ENSG00000152484.14.
DR GeneID; 219333; -.
DR KEGG; hsa:219333; -.
DR MANE-Select; ENST00000282344.11; ENSP00000282344.6; NM_182488.4; NP_872294.2.
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; ATVVHCG; -.
DR OrthoDB; 378361at2759; -.
DR PhylomeDB; O75317; -.
DR TreeFam; TF314144; -.
DR PathwayCommons; O75317; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; O75317; -.
DR BioGRID-ORCS; 219333; 42 hits in 1119 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 endothelial cell and 194 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:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
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: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 BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5K16, ECO:0007744|PDB:5K1A,
FT ECO:0007744|PDB:5K1B, ECO:0007744|PDB:5L8W"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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
