ID M3VX30_FELCA Unreviewed; 439 AA.
AC M3VX30;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN Name=NXN {ECO:0000313|Ensembl:ENSFCAP00000001553.4,
GN ECO:0000313|VGNC:VGNC:63935};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001553.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001553.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001553.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001553.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001553.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001553.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001553.4};
RG Ensembl;
RL Submitted (SEP-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; AANG04004035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC235687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VX30; -.
DR STRING; 9685.ENSFCAP00000001553; -.
DR PaxDb; 9685-ENSFCAP00000001553; -.
DR Ensembl; ENSFCAT00000001674.4; ENSFCAP00000001553.4; ENSFCAG00000001674.4.
DR VGNC; VGNC:63935; NXN.
DR eggNOG; KOG2501; Eukaryota.
DR GeneTree; ENSGT00940000161894; -.
DR HOGENOM; CLU_019626_2_0_1; -.
DR InParanoid; M3VX30; -.
DR OMA; NAPCRQF; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000011712; Chromosome E1.
DR Bgee; ENSFCAG00000001674; Expressed in tip of external ear and 10 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0072359; P:circulatory system development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 171..318
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 439 AA; 48629 MW; E0A567DC2CAC2574 CRC64;
MSGFLEELLG EKLVTGGGEE VDVHSLGSRG ISLLGLYFGC SLSAPCAQLS GSLAAFYGRL
RGDAAAGPGA GAGPGPGAGA AAEPEPLRRL EIVFVSSDQD QRQWQDFVRD MPWLALPYKE
KHRKLKLWNK YRISNIPSLI FLDATTGKVV CRNGLLVIRD DPEGLEFPWG PKPFREVIAG
PLLRNNGQSL ESSSLEGSHV GVYFSAHWCP PCRSLTRVLV ESYRKIKEAG QKFEIIFVSA
DRSEDSFKQY FSEMPWLAVP YTDEARRSRL NRLYGIQGIP TLIVLDPQGE VITRQGRVEV
LNDEDCREFP WHPKPVLELS DSNAVQLNEG PCLVLFVDSE DDGESEAAKQ LIQPIAEKII
AKYKAKEEEA PLLFFVAGED DMTDSLRDYT NLPEAAPLLT ILDMSARAKY VMDVEEITPA
IVEAFVNDFL AEKLKPEPI
//
