ID V3ZZ47_LOTGI Unreviewed; 170 AA.
AC V3ZZ47;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000256|ARBA:ARBA00016955};
DE EC=1.8.4.2 {ECO:0000256|ARBA:ARBA00013094};
GN ORFNames=LOTGIDRAFT_234262 {ECO:0000313|EMBL:ESO89682.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO89682.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO89682.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol +
CC glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593,
CC Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00033687};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC Evidence={ECO:0000256|ARBA:ARBA00033687};
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DR EMBL; KB202567; ESO89682.1; -; Genomic_DNA.
DR RefSeq; XP_009059733.1; XM_009061485.1.
DR AlphaFoldDB; V3ZZ47; -.
DR STRING; 225164.V3ZZ47; -.
DR EnsemblMetazoa; LotgiT234262; LotgiP234262; LotgiG234262.
DR GeneID; 20249477; -.
DR KEGG; lgi:LOTGIDRAFT_234262; -.
DR CTD; 20249477; -.
DR HOGENOM; CLU_088048_2_0_1; -.
DR OMA; SEHFVMV; -.
DR OrthoDB; 101767at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC.
DR CDD; cd02959; ERp19; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037462; ERp19.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR15337; ANTERIOR GRADIENT PROTEIN-RELATED; 1.
DR PANTHER; PTHR15337:SF11; THIOREDOXIN DOMAIN CONTAINING PROTEIN HOMOLOG; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..170
FT /note="Thioredoxin domain-containing protein 12"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004716415"
FT DOMAIN 7..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 170 AA; 19468 MW; 51471307D0C575F4 CRC64;
MADFSIISLV SLIICITLST ANELARGWND KIDWVKLEDG LKISQTEQKP LMIVIHKSWC
GACKALMPKF AESKEIEELS KQFVMVNSRD DEEPNESQYT PDGGYIPRIL FLDSSGKVRK
EFINENGNES YKYYYPAVSH IVESMEKVLK AKEKGELTTK HEEEEDKVEL
//
