ID G3TA82_LOXAF Unreviewed; 98 AA.
AC G3TA82;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Thioredoxin {ECO:0000256|ARBA:ARBA00020570};
GN Name=TXN {ECO:0000313|Ensembl:ENSLAFP00000010748.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010748.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010748.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010748.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010748.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010748.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR AlphaFoldDB; G3TA82; -.
DR STRING; 9785.ENSLAFP00000010748; -.
DR Ensembl; ENSLAFT00000012853.2; ENSLAFP00000010748.2; ENSLAFG00000012856.2.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000154259; -.
DR HOGENOM; CLU_090389_14_6_1; -.
DR InParanoid; G3TA82; -.
DR OMA; CKMIDPF; -.
DR TreeFam; TF318932; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0071731; P:response to nitric oxide; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46115:SF7; THIOREDOXIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Redox-active center {ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..98
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 20
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 27
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 28
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 26..29
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 98 AA; 10881 MW; 0A764D63BFF2D4DE CRC64;
SKEDFQAALN SAGDKLVVVD FSATWCGPCK MIKPFFHSLS EKYGNVVFLE VDVDDCQDVA
SECEVKCMPT FQFYKKGVKV GEFSGANKEK LEATINEL
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