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Database: UniProt
Entry: A0A3B5Q8I9_XIPMA
LinkDB: A0A3B5Q8I9_XIPMA
Original site: A0A3B5Q8I9_XIPMA 
ID   A0A3B5Q8I9_XIPMA        Unreviewed;       106 AA.
AC   A0A3B5Q8I9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glutaredoxin-1 {ECO:0000256|ARBA:ARBA00013662};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000028093.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000028093.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000028093.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007787}.
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DR   RefSeq; XP_005814796.1; XM_005814739.2.
DR   AlphaFoldDB; A0A3B5Q8I9; -.
DR   STRING; 8083.ENSXMAP00000028093; -.
DR   Ensembl; ENSXMAT00000031477.1; ENSXMAP00000028093.1; ENSXMAG00000026354.1.
DR   GeneID; 102237742; -.
DR   KEGG; xma:102237742; -.
DR   CTD; 2745; -.
DR   GeneTree; ENSGT00900000141068; -.
DR   InParanoid; A0A3B5Q8I9; -.
DR   OMA; KPGHLEC; -.
DR   OrthoDB; 203654at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR047185; GLRX1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02180; GRX_euk; 1.
DR   PANTHER; PTHR46185; GLUTAREDOXIN-1; 1.
DR   PANTHER; PTHR46185:SF1; GLUTAREDOXIN-1; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          15..80
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   106 AA;  11606 MW;  55C3E46AFEA7D6C7 CRC64;
     MAQQFVKAQI KGDKVVVFLK PSCPYCVVAQ EVFSQYQFKP GHLECINISG RSDMNSLQDY
     FLETTGARSV PRVFIGEKCV GGGSDVQELD KSGKLKGMLE SIGALQ
//
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