OTUB2_HUMAN
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 03-AUG-2022, entry version 164.
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 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 AlphaFoldDB; Q96DC9; -.
DR SMR; Q96DC9; -.
DR BioGRID; 122461; 104.
DR IntAct; Q96DC9; 29.
DR MINT; Q96DC9; -.
DR STRING; 9606.ENSP00000203664; -.
DR BindingDB; Q96DC9; -.
DR ChEMBL; CHEMBL4630847; -.
DR MEROPS; C65.002; -.
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; Q96DC9; -.
DR PeptideAtlas; Q96DC9; -.
DR PRIDE; Q96DC9; -.
DR ProteomicsDB; 76278; -. [Q96DC9-1]
DR ProteomicsDB; 76279; -. [Q96DC9-2]
DR Antibodypedia; 103; 420 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 CTD; 78990; -.
DR DisGeNET; 78990; -.
DR GeneCards; OTUB2; -.
DR HGNC; HGNC:20351; OTUB2.
DR HPA; ENSG00000089723; Tissue enhanced (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; EAPDLHV; -.
DR OrthoDB; 1257066at2759; -.
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 1110 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 left testis and 100 other tissues.
DR Genevisible; Q96DC9; HS.
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:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; 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 Gene3D; 1.20.1300.20; -; 1.
DR Gene3D; 3.30.200.60; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR030299; OTUB2.
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; PTHR12931; 1.
DR PANTHER; PTHR12931:SF3; PTHR12931:SF3; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
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
