ID   TXD17_PONAB             Reviewed;         123 AA.
AC   Q5REA8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Thioredoxin domain-containing protein 17;
DE   AltName: Full=Thioredoxin-like protein 5;
GN   Name=TXNDC17; Synonyms=TXNL5;
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].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Disulfide reductase. May participate in various redox
CC       reactions through the reversible oxidation of its active center dithiol
CC       to a disulfide and catalyze dithiol-disulfide exchange reactions.
CC       Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase
CC       activity and may contribute to the elimination of cellular hydrogen
CC       peroxide (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: The oxidized protein is reduced by TRXR1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; CR857624; CAH89899.1; -; mRNA.
DR   RefSeq; NP_001124889.1; NM_001131417.1.
DR   AlphaFoldDB; Q5REA8; -.
DR   SMR; Q5REA8; -.
DR   STRING; 9601.ENSPPYP00000008869; -.
DR   Ensembl; ENSPPYT00000043922; ENSPPYP00000039455; ENSPPYG00000032819.
DR   GeneID; 100171754; -.
DR   KEGG; pon:100171754; -.
DR   CTD; 84817; -.
DR   eggNOG; KOG3425; Eukaryota.
DR   GeneTree; ENSGT00390000012195; -.
DR   HOGENOM; CLU_120161_0_1_1; -.
DR   InParanoid; Q5REA8; -.
DR   OMA; IMVVTHN; -.
DR   OrthoDB; 1624076at2759; -.
DR   TreeFam; TF313854; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR045108; TXNDC17-like.
DR   InterPro; IPR010357; TXNDC17_dom.
DR   PANTHER; PTHR12452; PTHR12452; 1.
DR   Pfam; PF06110; DUF953; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Disulfide bond; Redox-active center;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   CHAIN           2..123
FT                   /note="Thioredoxin domain-containing protein 17"
FT                   /id="PRO_0000120024"
FT   DOMAIN          41..123
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   ACT_SITE        46
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   SITE            44
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   SITE            45
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT   DISULFID        43..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA2"
SQ   SEQUENCE   123 AA;  13941 MW;  887ADE1751946B86 CRC64;
     MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI
     SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLIKYG TPQKLVESEC LQANLVEMLF
     SED