ID   OTUB2_HUMAN             Reviewed;         234 AA.
AC   Q96DC9; Q6IA10; Q9H6T1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Ubiquitin thioesterase OTUB2;
DE            EC=3.4.19.12 {ECO:0000269|PubMed:23827681};
DE   AltName: Full=Deubiquitinating enzyme OTUB2;
DE   AltName: Full=OTU domain-containing ubiquitin aldehyde-binding protein 2;
DE   AltName: Full=Otubain-2;
DE   AltName: Full=Ubiquitin-specific-processing protease OTUB2;
GN   Name=OTUB2; Synonyms=C14orf137, OTB2, OTU2;
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), IDENTIFICATION BY MASS
RP   SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-51.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12704427; DOI=10.1038/sj.embor.embor824;
RA   Balakirev M.Y., Tcherniuk S.O., Jaquinod M., Chroboczek J.;
RT   "Otubains: a new family of cysteine proteases in the ubiquitin pathway.";
RL   EMBO Rep. 4:517-522(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, and Lung;
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   FUNCTION, AND MUTAGENESIS OF GLY-47.
RX   PubMed=18954305; DOI=10.1042/bj20081318;
RA   Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B.,
RA   Fiebiger E., Dhe-Paganon S., Kessler B.M.;
RT   "Structural basis and specificity of human otubain 1-mediated
RT   deubiquitination.";
RL   Biochem. J. 418:379-390(2009).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA   Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA   Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA   Ovaa H., Komander D.;
RT   "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT   ubiquitin chain restriction analysis.";
RL   Cell 154:169-184(2013).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND MUTAGENESIS OF ASN-226.
RX   PubMed=15258613; DOI=10.1038/sj.embor.7400201;
RA   Nanao M.H., Tcherniuk S.O., Chroboczek J., Dideberg O., Dessen A.,
RA   Balakirev M.Y.;
RT   "Crystal structure of human otubain 2.";
RL   EMBO Rep. 5:783-788(2004).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       in vitro and may therefore play an important regulatory role at the
CC       level of protein turnover by preventing degradation. Mediates
CC       deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitin chains, with a preference for 'Lys-63'-linked
CC       polyubiquitin chains. {ECO:0000269|PubMed:12704427,
CC       ECO:0000269|PubMed:18954305, ECO:0000269|PubMed:23827681}.
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:23827681};
CC   -!- INTERACTION:
CC       Q96DC9; Q96B67: ARRDC3; NbExp=8; IntAct=EBI-746259, EBI-2875665;
CC       Q96DC9; P54252: ATXN3; NbExp=9; IntAct=EBI-746259, EBI-946046;
CC       Q96DC9; Q9H305: CDIP1; NbExp=3; IntAct=EBI-746259, EBI-2876678;
CC       Q96DC9; Q16630: CPSF6; NbExp=3; IntAct=EBI-746259, EBI-358410;
CC       Q96DC9; Q15038: DAZAP2; NbExp=5; IntAct=EBI-746259, EBI-724310;
CC       Q96DC9; Q92567: FAM168A; NbExp=5; IntAct=EBI-746259, EBI-7957930;
CC       Q96DC9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-746259, EBI-11978259;
CC       Q96DC9; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-746259, EBI-741037;
CC       Q96DC9; O15344: MID1; NbExp=3; IntAct=EBI-746259, EBI-2340316;
CC       Q96DC9; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746259, EBI-10172526;
CC       Q96DC9; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-746259, EBI-373524;
CC       Q96DC9; Q53GA4: PHLDA2; NbExp=3; IntAct=EBI-746259, EBI-4402464;
CC       Q96DC9; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-746259, EBI-373552;
CC       Q96DC9; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-746259, EBI-13318883;
CC       Q96DC9; Q04864: REL; NbExp=3; IntAct=EBI-746259, EBI-307352;
CC       Q96DC9; Q04864-2: REL; NbExp=3; IntAct=EBI-746259, EBI-10829018;
CC       Q96DC9; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-746259, EBI-747107;
CC       Q96DC9; Q8N0X7: SPART; NbExp=3; IntAct=EBI-746259, EBI-2643803;
CC       Q96DC9; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-746259, EBI-11952721;
CC       Q96DC9; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-746259, EBI-10175039;
CC       Q96DC9; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-746259, EBI-359276;
CC       Q96DC9; Q9BYV2: TRIM54; NbExp=4; IntAct=EBI-746259, EBI-2130429;
CC       Q96DC9; Q9BZR9: TRIM8; NbExp=7; IntAct=EBI-746259, EBI-2340370;
CC       Q96DC9-2; P54252: ATXN3; NbExp=9; IntAct=EBI-25973449, EBI-946046;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96DC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96DC9-2; Sequence=VSP_009465;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain. {ECO:0000269|PubMed:12704427}.
CC   -!- MISCELLANEOUS: In the structure described by PubMed:15258613, the Asp-
CC       48 active site of the catalytic triad is located too far to interact
CC       directly with the active site His-224. A possible explanation is that
CC       OTUB2 is in inactive conformation in absence of ubiquitin and a
CC       conformation change may move Asp-48 in the proximity of His-224 in
CC       presence of ubiquitin substrate. {ECO:0000305|PubMed:15258613}.
CC   -!- SIMILARITY: Belongs to the peptidase C65 family. {ECO:0000305}.
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DR   EMBL; AY177201; AAO27703.1; -; mRNA.
DR   EMBL; AK025569; BAB15172.1; -; mRNA.
DR   EMBL; CR457345; CAG33626.1; -; mRNA.
DR   EMBL; AL079302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009615; AAH09615.1; -; mRNA.
DR   EMBL; BC068058; AAH68058.1; -; mRNA.
DR   CCDS; CCDS9917.1; -. [Q96DC9-1]
DR   RefSeq; NP_075601.1; NM_023112.3. [Q96DC9-1]
DR   PDB; 1TFF; X-ray; 2.10 A; A=1-234.
DR   PDB; 4FJV; X-ray; 2.05 A; A/C=1-234.
DR   PDB; 5QIO; X-ray; 1.46 A; A=6-230.
DR   PDB; 5QIP; X-ray; 1.63 A; A=6-230.
DR   PDB; 5QIQ; X-ray; 1.44 A; A=6-230.
DR   PDB; 5QIR; X-ray; 1.43 A; A=6-230.
DR   PDB; 5QIS; X-ray; 1.53 A; A=6-230.
DR   PDB; 5QIT; X-ray; 1.46 A; A=6-230.
DR   PDB; 5QIU; X-ray; 1.56 A; A=6-230.
DR   PDB; 5QIV; X-ray; 1.39 A; A=6-230.
DR   PDB; 5QIW; X-ray; 1.71 A; A=6-230.
DR   PDB; 5QIX; X-ray; 1.39 A; A=6-230.
DR   PDB; 5QIY; X-ray; 1.58 A; A=6-230.
DR   PDB; 5QIZ; X-ray; 1.63 A; A=6-230.
DR   PDB; 8CMS; X-ray; 1.77 A; AAA=1-234.
DR   PDBsum; 1TFF; -.
DR   PDBsum; 4FJV; -.
DR   PDBsum; 5QIO; -.
DR   PDBsum; 5QIP; -.
DR   PDBsum; 5QIQ; -.
DR   PDBsum; 5QIR; -.
DR   PDBsum; 5QIS; -.
DR   PDBsum; 5QIT; -.
DR   PDBsum; 5QIU; -.
DR   PDBsum; 5QIV; -.
DR   PDBsum; 5QIW; -.
DR   PDBsum; 5QIX; -.
DR   PDBsum; 5QIY; -.
DR   PDBsum; 5QIZ; -.
DR   PDBsum; 8CMS; -.
DR   AlphaFoldDB; Q96DC9; -.
DR   SMR; Q96DC9; -.
DR   BioGRID; 122461; 107.
DR   IntAct; Q96DC9; 29.
DR   MINT; Q96DC9; -.
DR   STRING; 9606.ENSP00000203664; -.
DR   BindingDB; Q96DC9; -.
DR   ChEMBL; CHEMBL4630847; -.
DR   MEROPS; C65.002; -.
DR   GlyGen; Q96DC9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96DC9; -.
DR   PhosphoSitePlus; Q96DC9; -.
DR   BioMuta; OTUB2; -.
DR   DMDM; 44888285; -.
DR   EPD; Q96DC9; -.
DR   jPOST; Q96DC9; -.
DR   MassIVE; Q96DC9; -.
DR   MaxQB; Q96DC9; -.
DR   PaxDb; 9606-ENSP00000203664; -.
DR   PeptideAtlas; Q96DC9; -.
DR   ProteomicsDB; 76278; -. [Q96DC9-1]
DR   ProteomicsDB; 76279; -. [Q96DC9-2]
DR   Pumba; Q96DC9; -.
DR   Antibodypedia; 103; 472 antibodies from 33 providers.
DR   CPTC; Q96DC9; 2 antibodies.
DR   DNASU; 78990; -.
DR   Ensembl; ENST00000203664.10; ENSP00000203664.5; ENSG00000089723.10. [Q96DC9-1]
DR   Ensembl; ENST00000553723.1; ENSP00000451283.1; ENSG00000089723.10. [Q96DC9-2]
DR   Ensembl; ENST00000617748.3; ENSP00000478628.1; ENSG00000277276.3. [Q96DC9-1]
DR   Ensembl; ENST00000628711.1; ENSP00000487491.1; ENSG00000277276.3. [Q96DC9-2]
DR   GeneID; 78990; -.
DR   KEGG; hsa:78990; -.
DR   MANE-Select; ENST00000203664.10; ENSP00000203664.5; NM_023112.4; NP_075601.1.
DR   UCSC; uc001ych.5; human. [Q96DC9-1]
DR   AGR; HGNC:20351; -.
DR   CTD; 78990; -.
DR   DisGeNET; 78990; -.
DR   GeneCards; OTUB2; -.
DR   HGNC; HGNC:20351; OTUB2.
DR   HPA; ENSG00000089723; Group enriched (esophagus, skin, testis).
DR   MIM; 608338; gene.
DR   neXtProt; NX_Q96DC9; -.
DR   OpenTargets; ENSG00000089723; -.
DR   PharmGKB; PA134861658; -.
DR   VEuPathDB; HostDB:ENSG00000089723; -.
DR   eggNOG; KOG3991; Eukaryota.
DR   GeneTree; ENSGT00390000006979; -.
DR   HOGENOM; CLU_014832_3_2_1; -.
DR   InParanoid; Q96DC9; -.
DR   OMA; KVYCRQE; -.
DR   OrthoDB; 148019at2759; -.
DR   PhylomeDB; Q96DC9; -.
DR   TreeFam; TF314145; -.
DR   PathwayCommons; Q96DC9; -.
DR   Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR   SignaLink; Q96DC9; -.
DR   BioGRID-ORCS; 78990; 7 hits in 1186 CRISPR screens.
DR   ChiTaRS; OTUB2; human.
DR   EvolutionaryTrace; Q96DC9; -.
DR   GeneWiki; OTUB2; -.
DR   GenomeRNAi; 78990; -.
DR   Pharos; Q96DC9; Tbio.
DR   PRO; PR:Q96DC9; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q96DC9; Protein.
DR   Bgee; ENSG00000089723; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 102 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:2000780; P:negative regulation of double-strand break repair; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IMP:UniProtKB.
DR   GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22764; OTUB2; 1.
DR   Gene3D; 3.30.200.60; Peptidase C65 Otubain, subdomain 1; 1.
DR   Gene3D; 1.20.1300.20; Peptidase C65 Otubain, subdomain 2; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR016615; Otubain.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR019400; Peptidase_C65_otubain.
DR   InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR   InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR   PANTHER; PTHR12931:SF3; UBIQUITIN THIOESTERASE OTUB2; 1.
DR   PANTHER; PTHR12931; UBIQUITIN THIOLESTERASE PROTEIN OTUB; 1.
DR   Pfam; PF10275; Peptidase_C65; 1.
DR   PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   Genevisible; Q96DC9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..234
FT                   /note="Ubiquitin thioesterase OTUB2"
FT                   /id="PRO_0000221010"
FT   DOMAIN          40..231
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000305|PubMed:15258613"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:12704427,
FT                   ECO:0000305|PubMed:15258613"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000305|PubMed:15258613"
FT   SITE            226
FT                   /note="Required to orient and stabilize the active site H-
FT                   224"
FT                   /evidence="ECO:0000305|PubMed:15258613"
FT   VAR_SEQ         74..234
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009465"
FT   MUTAGEN         47
FT                   /note="G->P: Affects its ability to cleave 'K63'-linked
FT                   ubiquitin."
FT                   /evidence="ECO:0000269|PubMed:18954305"
FT   MUTAGEN         51
FT                   /note="C->S: Loss of function in vitro."
FT                   /evidence="ECO:0000269|PubMed:12704427"
FT   MUTAGEN         226
FT                   /note="N->A: Abolishes deubiquitinase activity."
FT                   /evidence="ECO:0000269|PubMed:15258613"
FT   STRAND          8..14
FT                   /evidence="ECO:0007829|PDB:5QIQ"
FT   HELIX           15..21
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           26..35
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:4FJV"
FT   HELIX           51..64
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           68..87
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           92..111
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           115..123
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           125..145
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           147..153
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   TURN            154..157
FT                   /evidence="ECO:0007829|PDB:5QIQ"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   HELIX           177..187
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:5QIV"
FT   STRAND          225..229
FT                   /evidence="ECO:0007829|PDB:5QIV"
SQ   SEQUENCE   234 AA;  27213 MW;  DF2DBD32A78F9929 CRC64;
     MSETSFNLIS EKCDILSILR DHPENRIYRR KIEELSKRFT AIRKTKGDGN CFYRALGYSY
     LESLLGKSRE IFKFKERVLQ TPNDLLAAGF EEHKFRNFFN AFYSVVELVE KDGSVSSLLK
     VFNDQSASDH IVQFLRLLTS AFIRNRADFF RHFIDEEMDI KDFCTHEVEP MATECDHIQI
     TALSQALSIA LQVEYVDEMD TALNHHVFPE AATPSVYLLY KTSHYNILYA ADKH
//