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Database: UniProt
Entry: A0A2I3T0C5_PANTR
LinkDB: A0A2I3T0C5_PANTR
Original site: A0A2I3T0C5_PANTR 
ID   A0A2I3T0C5_PANTR        Unreviewed;       324 AA.
AC   A0A2I3T0C5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN   Name=NXN {ECO:0000313|Ensembl:ENSPTRP00000082642.1,
GN   ECO:0000313|VGNC:VGNC:12578};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000082642.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000082642.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000082642.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000696};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001346};
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC       {ECO:0000256|ARBA:ARBA00025782}.
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DR   EMBL; AACZ04062745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04062752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3T0C5; -.
DR   Ensembl; ENSPTRT00000095023.1; ENSPTRP00000082642.1; ENSPTRG00000008513.6.
DR   VGNC; VGNC:12578; NXN.
DR   GeneTree; ENSGT00940000161894; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000008513; Expressed in colon and 20 other cell types or tissues.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   CDD; cd03071; PDI_b'_NRX; 1.
DR   CDD; cd03009; TryX_like_TryX_NRX; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR041861; NRX_PDI_b.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR   PANTHER; PTHR46472; NUCLEOREDOXIN; 1.
DR   PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   Pfam; PF13905; Thioredoxin_8; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT   DOMAIN          56..210
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   324 AA;  36729 MW;  21624402A5665C90 CRC64;
     IFIFVIFRDL KLWNKYRISN IPSLIFLDAT TGKVVCRNGL LVIRDDPEGL EFPWGPKPFR
     EVIAGPLLRN NGQSLESSSL EGSHVGVYFS AHWCPPCRSL TRVLVESYRK IKEAGQNFEI
     IFVSADRSEE SFKQYFSEMP WLAVPYTDEA RRSRLNRLYG IQGIPTLIML DPQGEVITRQ
     GRVEVLNDED CREFPWHPKP VLELSDSNAA QLNEGPCLVL FVDSEDDGES EAAKQLIQPI
     AEKIIAKYKA KEEEAPLLFF VAGEDDMTDS LRDYTNLPEA APLLTILDMS ARAKYVMDVE
     EITPAIVEAF VNDFLAEKLK PEPI
//
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