MSRB3_PONAB
ID MSRB3_PONAB Reviewed; 190 AA.
AC Q5R930;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 88.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of free and protein-bound methionine
CC sulfoxide to methionine. {ECO:0000250|UniProtKB:Q8IXL7}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q5R930-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q5R930-2; Sequence=VSP_040884;
CC -!- MISCELLANEOUS: [Isoform 2]: Has a transit peptide. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; CR859566; CAH91730.1; -; mRNA.
DR RefSeq; NP_001127455.1; NM_001133983.1. [Q5R930-2]
DR RefSeq; XP_009246258.1; XM_009247983.1. [Q5R930-2]
DR RefSeq; XP_009246259.1; XM_009247984.1. [Q5R930-2]
DR AlphaFoldDB; Q5R930; -.
DR SMR; Q5R930; -.
DR STRING; 9601.ENSPPYP00000005393; -.
DR Ensembl; ENSPPYT00000005603; ENSPPYP00000005393; ENSPPYG00000004735. [Q5R930-2]
DR Ensembl; ENSPPYT00000046850; ENSPPYP00000034077; ENSPPYG00000004735. [Q5R930-1]
DR GeneID; 100174528; -.
DR KEGG; pon:100174528; -.
DR CTD; 253827; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000155240; -.
DR HOGENOM; CLU_031040_8_4_1; -.
DR InParanoid; Q5R930; -.
DR OMA; DEQWRAE; -.
DR OrthoDB; 1549489at2759; -.
DR TreeFam; TF329147; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Metal-binding;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome; Signal;
KW Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..190
FT /note="Methionine-R-sulfoxide reductase B3"
FT /id="PRO_0000327242"
FT DOMAIN 45..167
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 166..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..190
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU85"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU85"
FT VAR_SEQ 1..29
FT /note="MSPQRTLPRPLSLCLCLCLCLAAALGSAQ -> MSAFNLLHLVTKSQPVALR
FT ACGLP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040884"
SQ SEQUENCE 190 AA; 20489 MW; DB414F27F15FDF2F CRC64;
MSPQRTLPRP LSLCLCLCLC LAAALGSAQS GSCRDKKNCK VVFSQQELRK RLTPLQYHVT
QEKGTESAFE GEYTHHKDPG IYKCVVCGTP LFKSETKFDS GSGWPSFHDV ISSEAITFTD
DFSYGMHRVE TSCSQCGAHL GHIFDDGPRP TGKRYCINSA ALSFTPADSS GAAEGESGVA
SPAQADKAEL
