MSRB3_HUMAN
ID MSRB3_HUMAN Reviewed; 192 AA.
AC Q8IXL7; B4DR19; B7ZAQ0; Q6UXS2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Methionine-R-sulfoxide reductase B3;
DE Short=MsrB3;
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
DE EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
DE Flags: Precursor;
GN Name=MSRB3; ORFNames=UNQ1965/PRO4487;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Esophageal carcinoma, Teratocarcinoma, and Uterus;
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 2).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=14699060; DOI=10.1091/mbc.e03-08-0629;
RA Kim H.-Y., Gladyshev V.N.;
RT "Methionine sulfoxide reduction in mammals: characterization of methionine-
RT R-sulfoxide reductases.";
RL Mol. Biol. Cell 15:1055-1064(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15914630; DOI=10.1167/iovs.05-0018;
RA Marchetti M.A., Pizarro G.O., Sagher D., Deamicis C., Brot N.,
RA Hejtmancik J.F., Weissbach H., Kantorow M.;
RT "Methionine sulfoxide reductases B1, B2, and B3 are present in the human
RT lens and confer oxidative stress resistance to lens cells.";
RL Invest. Ophthalmol. Vis. Sci. 46:2107-2112(2005).
RN [7]
RP MUTAGENESIS OF HIS-141 AND ASN-160, AND SUBUNIT.
RX PubMed=16262444; DOI=10.1371/journal.pbio.0030375;
RA Kim H.-Y., Gladyshev V.N.;
RT "Different catalytic mechanisms in mammalian selenocysteine- and cysteine-
RT containing methionine-R-sulfoxide reductases.";
RL PLoS Biol. 3:2080-2089(2005).
RN [8]
RP VARIANT DFNB74 GLY-89, FUNCTION, ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=21185009; DOI=10.1016/j.ajhg.2010.11.010;
RA Ahmed Z.M., Yousaf R., Lee B.C., Khan S.N., Lee S., Lee K., Husnain T.,
RA Rehman A.U., Bonneux S., Ansar M., Ahmad W., Leal S.M., Gladyshev V.N.,
RA Belyantseva I.A., Van Camp G., Riazuddin S., Friedman T.B., Riazuddin S.;
RT "Functional null mutations of MSRB3 encoding methionine sulfoxide reductase
RT are associated with human deafness DFNB74.";
RL Am. J. Hum. Genet. 88:19-29(2011).
CC -!- FUNCTION: Catalyzes the reduction of free and protein-bound methionine
CC sulfoxide to methionine. Isoform 2 is essential for hearing.
CC {ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:21185009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58773; EC=1.8.4.14;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14699060};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14699060};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16262444}.
CC -!- INTERACTION:
CC Q8IXL7; Q08379: GOLGA2; NbExp=3; IntAct=EBI-8634060, EBI-618309;
CC Q8IXL7; Q9UKN5: PRDM4; NbExp=3; IntAct=EBI-8634060, EBI-2803427;
CC Q8IXL7; P15884: TCF4; NbExp=3; IntAct=EBI-8634060, EBI-533224;
CC Q8IXL7; Q15654: TRIP6; NbExp=3; IntAct=EBI-8634060, EBI-742327;
CC Q8IXL7-2; Q8WXK3-2: ASB13; NbExp=3; IntAct=EBI-10699187, EBI-12015080;
CC Q8IXL7-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-10699187, EBI-11524452;
CC Q8IXL7-2; P56545-3: CTBP2; NbExp=5; IntAct=EBI-10699187, EBI-10171902;
CC Q8IXL7-2; Q96AZ1: EEF1AKMT3; NbExp=3; IntAct=EBI-10699187, EBI-12108304;
CC Q8IXL7-2; Q12805: EFEMP1; NbExp=3; IntAct=EBI-10699187, EBI-536772;
CC Q8IXL7-2; P56537: EIF6; NbExp=3; IntAct=EBI-10699187, EBI-372243;
CC Q8IXL7-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-10699187, EBI-12193763;
CC Q8IXL7-2; Q13643: FHL3; NbExp=3; IntAct=EBI-10699187, EBI-741101;
CC Q8IXL7-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10699187, EBI-618309;
CC Q8IXL7-2; O15354: GPR37; NbExp=3; IntAct=EBI-10699187, EBI-15639515;
CC Q8IXL7-2; P28799: GRN; NbExp=3; IntAct=EBI-10699187, EBI-747754;
CC Q8IXL7-2; P28799-2: GRN; NbExp=3; IntAct=EBI-10699187, EBI-25860013;
CC Q8IXL7-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10699187, EBI-10975473;
CC Q8IXL7-2; Q15323: KRT31; NbExp=3; IntAct=EBI-10699187, EBI-948001;
CC Q8IXL7-2; O76011: KRT34; NbExp=3; IntAct=EBI-10699187, EBI-1047093;
CC Q8IXL7-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-10699187, EBI-10171697;
CC Q8IXL7-2; P80188: LCN2; NbExp=3; IntAct=EBI-10699187, EBI-11911016;
CC Q8IXL7-2; Q86YW9: MED12L; NbExp=3; IntAct=EBI-10699187, EBI-3957138;
CC Q8IXL7-2; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-10699187, EBI-10174029;
CC Q8IXL7-2; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-10699187, EBI-8652459;
CC Q8IXL7-2; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-10699187, EBI-12866138;
CC Q8IXL7-2; P07196: NEFL; NbExp=3; IntAct=EBI-10699187, EBI-475646;
CC Q8IXL7-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10699187, EBI-79165;
CC Q8IXL7-2; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-10699187, EBI-949255;
CC Q8IXL7-2; P78424: POU6F2; NbExp=3; IntAct=EBI-10699187, EBI-12029004;
CC Q8IXL7-2; Q04864-2: REL; NbExp=3; IntAct=EBI-10699187, EBI-10829018;
CC Q8IXL7-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10699187, EBI-396669;
CC Q8IXL7-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10699187, EBI-5235340;
CC Q8IXL7-2; P36406: TRIM23; NbExp=3; IntAct=EBI-10699187, EBI-740098;
CC Q8IXL7-2; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-10699187, EBI-12068150;
CC Q8IXL7-2; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-10699187, EBI-358545;
CC Q8IXL7-2; O76024: WFS1; NbExp=3; IntAct=EBI-10699187, EBI-720609;
CC Q8IXL7-2; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-10699187, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q8IXL7-1; Sequence=Displayed;
CC Name=2; Synonyms=B, C, D;
CC IsoId=Q8IXL7-2; Sequence=VSP_040883;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15914630,
CC ECO:0000269|PubMed:21185009}.
CC -!- DISEASE: Deafness, autosomal recessive, 74 (DFNB74) [MIM:613718]: A
CC form of non-syndromic sensorineural deafness characterized by
CC prelingual, bilateral, profound hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:21185009}. Note=The disease is caused
CC by variants affecting the gene represented in this entry. A nonsense
CC mutation affecting exclusively mitochondrial isoform 2 is sufficient to
CC produce hearing loss.
CC -!- MISCELLANEOUS: [Isoform 2]: Has a transit peptide. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY358229; AAQ88596.1; -; mRNA.
DR EMBL; AK293084; BAF85773.1; -; mRNA.
DR EMBL; AK299065; BAG61131.1; -; mRNA.
DR EMBL; AK316365; BAH14736.1; -; mRNA.
DR EMBL; BX648776; CAI46018.1; -; mRNA.
DR EMBL; BC040053; AAH40053.1; -; mRNA.
DR CCDS; CCDS31853.1; -. [Q8IXL7-2]
DR CCDS; CCDS8973.1; -. [Q8IXL7-1]
DR RefSeq; NP_001026849.1; NM_001031679.2. [Q8IXL7-2]
DR RefSeq; NP_001180389.1; NM_001193460.1. [Q8IXL7-2]
DR RefSeq; NP_001180390.1; NM_001193461.1. [Q8IXL7-2]
DR RefSeq; NP_932346.1; NM_198080.3. [Q8IXL7-1]
DR PDB; 6QA0; X-ray; 1.71 A; A/B=31-169.
DR PDBsum; 6QA0; -.
DR AlphaFoldDB; Q8IXL7; -.
DR SMR; Q8IXL7; -.
DR BioGRID; 128990; 77.
DR IntAct; Q8IXL7; 46.
DR MINT; Q8IXL7; -.
DR STRING; 9606.ENSP00000347324; -.
DR ChEMBL; CHEMBL3509604; -.
DR iPTMnet; Q8IXL7; -.
DR PhosphoSitePlus; Q8IXL7; -.
DR BioMuta; MSRB3; -.
DR DMDM; 327478523; -.
DR EPD; Q8IXL7; -.
DR jPOST; Q8IXL7; -.
DR MassIVE; Q8IXL7; -.
DR MaxQB; Q8IXL7; -.
DR PaxDb; Q8IXL7; -.
DR PeptideAtlas; Q8IXL7; -.
DR PRIDE; Q8IXL7; -.
DR ProteomicsDB; 71024; -. [Q8IXL7-1]
DR ProteomicsDB; 71025; -. [Q8IXL7-2]
DR Antibodypedia; 2870; 127 antibodies from 22 providers.
DR DNASU; 253827; -.
DR Ensembl; ENST00000308259.10; ENSP00000312274.6; ENSG00000174099.12. [Q8IXL7-2]
DR Ensembl; ENST00000355192.8; ENSP00000347324.3; ENSG00000174099.12. [Q8IXL7-1]
DR Ensembl; ENST00000535664.5; ENSP00000441650.1; ENSG00000174099.12. [Q8IXL7-2]
DR Ensembl; ENST00000614640.4; ENSP00000481483.1; ENSG00000174099.12. [Q8IXL7-2]
DR Ensembl; ENST00000642404.1; ENSP00000496008.1; ENSG00000174099.12. [Q8IXL7-2]
DR Ensembl; ENST00000642411.1; ENSP00000494265.1; ENSG00000174099.12. [Q8IXL7-2]
DR Ensembl; ENST00000646299.1; ENSP00000494941.1; ENSG00000174099.12. [Q8IXL7-2]
DR GeneID; 253827; -.
DR KEGG; hsa:253827; -.
DR MANE-Select; ENST00000308259.10; ENSP00000312274.6; NM_001031679.3; NP_001026849.1. [Q8IXL7-2]
DR UCSC; uc001ssm.3; human. [Q8IXL7-1]
DR CTD; 253827; -.
DR DisGeNET; 253827; -.
DR GeneCards; MSRB3; -.
DR HGNC; HGNC:27375; MSRB3.
DR HPA; ENSG00000174099; Low tissue specificity.
DR MalaCards; MSRB3; -.
DR MIM; 613718; phenotype.
DR MIM; 613719; gene.
DR neXtProt; NX_Q8IXL7; -.
DR OpenTargets; ENSG00000174099; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA134991350; -.
DR VEuPathDB; HostDB:ENSG00000174099; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000155240; -.
DR InParanoid; Q8IXL7; -.
DR OMA; DEQWRAE; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q8IXL7; -.
DR TreeFam; TF329147; -.
DR BRENDA; 1.8.4.12; 2681.
DR BRENDA; 1.8.4.B3; 2681.
DR PathwayCommons; Q8IXL7; -.
DR Reactome; R-HSA-5676934; Protein repair.
DR SignaLink; Q8IXL7; -.
DR BioGRID-ORCS; 253827; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; MSRB3; human.
DR GenomeRNAi; 253827; -.
DR Pharos; Q8IXL7; Tbio.
DR PRO; PR:Q8IXL7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IXL7; protein.
DR Bgee; ENSG00000174099; Expressed in saphenous vein and 183 other tissues.
DR ExpressionAtlas; Q8IXL7; baseline and differential.
DR Genevisible; Q8IXL7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC-UCL.
DR GO; GO:0030091; P:protein repair; IDA:HGNC-UCL.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01400; MsrB; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Deafness; Disease variant;
KW Endoplasmic reticulum; Metal-binding; Mitochondrion;
KW Non-syndromic deafness; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..192
FT /note="Methionine-R-sulfoxide reductase B3"
FT /id="PRO_0000327240"
FT DOMAIN 47..169
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 189..192
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU85"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU85"
FT VAR_SEQ 1..31
FT /note="MSPRRTLPRPLSLCLSLCLCLCLAAALGSAQ -> MSAFNLLHLVTKSQPVA
FT LRACGLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_040883"
FT VARIANT 89
FT /note="C -> G (in DFNB74; abolishes zinc-binding and
FT enzymatic activity; dbSNP:rs387907088)"
FT /evidence="ECO:0000269|PubMed:21185009"
FT /id="VAR_064904"
FT MUTAGEN 141
FT /note="H->G: 30-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16262444"
FT MUTAGEN 160
FT /note="N->F: 7000-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16262444"
FT MUTAGEN 160
FT /note="N->Y: 500-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16262444"
FT CONFLICT 49
FT /note="E -> G (in Ref. 2; BAH14736)"
FT /evidence="ECO:0000305"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:6QA0"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:6QA0"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:6QA0"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6QA0"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6QA0"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6QA0"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6QA0"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6QA0"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6QA0"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6QA0"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:6QA0"
SQ SEQUENCE 192 AA; 20702 MW; C3326F6103369083 CRC64;
MSPRRTLPRP LSLCLSLCLC LCLAAALGSA QSGSCRDKKN CKVVFSQQEL RKRLTPLQYH
VTQEKGTESA FEGEYTHHKD PGIYKCVVCG TPLFKSETKF DSGSGWPSFH DVINSEAITF
TDDFSYGMHR VETSCSQCGA HLGHIFDDGP RPTGKRYCIN SAALSFTPAD SSGTAEGGSG
VASPAQADKA EL
