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Database: UniProt
Entry: Q5M993_XENLA
LinkDB: Q5M993_XENLA
Original site: Q5M993_XENLA 
ID   Q5M993_XENLA            Unreviewed;       326 AA.
AC   Q5M993;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Glutaredoxin 3 S homeolog {ECO:0000313|RefSeq:NP_001088850.1};
DE   SubName: Full=LOC496161 protein {ECO:0000313|EMBL:AAH87486.1};
GN   Name=glrx3.S {ECO:0000313|RefSeq:NP_001088850.1,
GN   ECO:0000313|Xenbase:XB-GENE-866128};
GN   Synonyms=glrx3 {ECO:0000313|RefSeq:NP_001088850.1,
GN   ECO:0000313|Xenbase:XB-GENE-866128}, LOC496161
GN   {ECO:0000313|EMBL:AAH87486.1}, txnl2
GN   {ECO:0000313|RefSeq:NP_001088850.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH87486.1};
RN   [1] {ECO:0000313|RefSeq:NP_001088850.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH87486.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000313|EMBL:AAH87486.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001088850.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; BC087486; AAH87486.1; -; mRNA.
DR   RefSeq; NP_001088850.1; NM_001095381.1.
DR   DNASU; 496161; -.
DR   GeneID; 496161; -.
DR   KEGG; xla:496161; -.
DR   AGR; Xenbase:XB-GENE-866128; -.
DR   CTD; 496161; -.
DR   Xenbase; XB-GENE-866128; glrx3.S.
DR   OrthoDB; 1038at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 496161; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03028; GRX_PICOT_like; 2.
DR   CDD; cd02984; TRX_PICOT; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 2.
DR   PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR   Pfam; PF00462; Glutaredoxin; 2.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   326 AA;  36702 MW;  D59C5FC892C2F82C CRC64;
     MAAVLEAGSQ SQFEELLQKS AKSLTVVHFW APWAPQCTQM NEVMAELAKE QPQVMFVKLE
     AEAVPEVSEK YEITSVPTFL FFKNSQKIDR LDGAHAPELT KRVQRHASST SFPATPNSAP
     KEDLNGRLKK LINAAPCMLF IKGSPQEPRC GFSRQIVDIL NQHKIQFSSF DILSDEEVRQ
     GLKTFSDWPT YPQFYVNGEL LGGLDIVKEM VASGELDQMC PKAQNLEERL KVLVNKAPVM
     LFMKGNKEMA KCGFSRQILE IMNNTGVNFE TFDILEDEEV RQGLKAYSNW PTYPQLYVKG
     ELVGGLDIVK ELKENGEFVS VLKGDQ
//
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