NXN_BOVIN
ID NXN_BOVIN Reviewed; 435 AA.
AC A6QLU8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nucleoredoxin;
DE EC=1.8.1.8;
GN Name=NXN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a redox-dependent negative regulator of the Wnt
CC signaling pathway, possibly by preventing ubiquitination of DVL3 by the
CC BCR(KLHL12) complex. May also function as a transcriptional regulator
CC act as a regulator of protein phosphatase 2A (PP2A) (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Associates with the phosphatase 2A holoenzyme. Interacts with
CC PPP2CA; the interaction is direct. Interacts with DVL1 (via PDZ
CC domain); the interaction is direct and regulated by oxidative stress
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P97346}. Nucleus {ECO:0000250|UniProtKB:P97346}.
CC -!- SIMILARITY: Belongs to the nucleoredoxin family. {ECO:0000305}.
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DR EMBL; BC148092; AAI48093.1; -; mRNA.
DR RefSeq; NP_001095606.1; NM_001102136.1.
DR AlphaFoldDB; A6QLU8; -.
DR STRING; 9913.ENSBTAP00000001140; -.
DR PaxDb; A6QLU8; -.
DR PRIDE; A6QLU8; -.
DR Ensembl; ENSBTAT00000001140; ENSBTAP00000001140; ENSBTAG00000000855.
DR GeneID; 531367; -.
DR KEGG; bta:531367; -.
DR CTD; 64359; -.
DR VEuPathDB; HostDB:ENSBTAG00000000855; -.
DR VGNC; VGNC:32376; NXN.
DR eggNOG; KOG2501; Eukaryota.
DR GeneTree; ENSGT00940000161894; -.
DR HOGENOM; CLU_019626_2_1_1; -.
DR InParanoid; A6QLU8; -.
DR OMA; EMITRQG; -.
DR OrthoDB; 1350271at2759; -.
DR TreeFam; TF331873; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000855; Expressed in vas deferens and 103 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0072359; P:circulatory system development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd03071; PDI_b'_NRX; 1.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
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 Pfam; PF13905; Thioredoxin_8; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Developmental protein; Differentiation; NAD;
KW Nucleus; Oxidoreductase; Reference proteome; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6DKJ4"
FT CHAIN 2..435
FT /note="Nucleoredoxin"
FT /id="PRO_0000332932"
FT DOMAIN 167..321
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DKJ4"
SQ SEQUENCE 435 AA; 48331 MW; 1A8582D78FBA2774 CRC64;
MSGFLEELLG EKLVTGGGEE VDVHSLAARG ISLLGLYFGC SLSAPCAQLS ASLAAFYGRL
RGDAAAGPGP GPGAGASAEP EPRRRLEIVF VSSDQDQRQW QDFVRDMPWL ALPYKEKHRK
LKLWNKYRIS NIPSLIFLDA TSGKVVCRNG LLVIRDDPEG LEFPWGPKPF REVIAGPLLR
SNGQSLESSS LEGSHVGVYF SAHWCPPCRS LTRVLVESYR KIKEAGQKFE IIFVSADRSE
DSFKQYFSEM PWLAVPYTDE ARRSRLNRLY GIQGIPTLIV LDPQGEVITR QGRVEVLNDE
DCRGFPWHPK PVLELSDSNA VQLNEGPCLV LFVDSEDDGE SEAAKQLIQP IAEKIIAKYK
AKEEEAPLLF FVAGEDDMTD SLRDYTNLPE AAPLLTILDM SARAKYVMDV EEITPAIVEA
FVNDFLAEKL KPEPI