ID TXND3_MOUSE Reviewed; 586 AA.
AC Q715T0; Q80W74;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Thioredoxin domain-containing protein 3;
DE AltName: Full=3'-5' exonuclease NME8;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8N427};
DE AltName: Full=NME/NM23 family member 8;
DE AltName: Full=Spermatid-specific thioredoxin-2 {ECO:0000303|PubMed:12909633};
DE Short=Sptrx-2 {ECO:0000303|PubMed:12909633};
GN Name=Nme8; Synonyms=Sptrx2, Txndc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=12909633; DOI=10.1074/jbc.m305475200;
RA Miranda-Vizuete A., Tsang K., Yu Y., Jimenez A., Pelto-Huikko M.,
RA Flickinger C.J., Sutovsky P., Oko R.;
RT "Cloning and developmental analysis of murid spermatid-specific
RT thioredoxin-2 (SPTRX-2), a novel sperm fibrous sheath protein and
RT autoantigen.";
RL J. Biol. Chem. 278:44874-44885(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=15781233; DOI=10.1016/j.bbrc.2005.02.128;
RA Jimenez A., Prieto-Alamo M.J., Fuentes-Almagro C.A., Jurado J.,
RA Gustafsson J.-A., Pueyo C., Miranda-Vizuete A.;
RT "Absolute mRNA levels and transcriptional regulation of the mouse testis-
RT specific thioredoxins.";
RL Biochem. Biophys. Res. Commun. 330:65-74(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=23707457; DOI=10.1016/j.freeradbiomed.2013.05.021;
RA Smith T.B., Baker M.A., Connaughton H.S., Habenicht U., Aitken R.J.;
RT "Functional deletion of Txndc2 and Txndc3 increases the susceptibility of
RT spermatozoa to age-related oxidative stress.";
RL Free Radic. Biol. Med. 65:872-881(2013).
CC -!- FUNCTION: Probably required during the final stages of sperm tail
CC maturation in the testis and/or epididymis, where extensive disulfide
CC bonding of fibrous sheath (FS) proteins occurs. In vitro, it has
CC neither nucleoside diphosphate kinase (NDPK) activity nor reducing
CC activity on disulfide bonds. Exhibits a 3'-5' exonuclease activity with
CC a preference for single-stranded DNA, suggesting roles in DNA
CC proofreading and repair. {ECO:0000250|UniProtKB:Q8N427}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8N427}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12909633}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q715T0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q715T0-2; Sequence=VSP_014330, VSP_014331;
CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed mainly in round
CC spermatids. {ECO:0000269|PubMed:12909633}.
CC -!- DEVELOPMENTAL STAGE: First expressed after puberty.
CC {ECO:0000269|PubMed:15781233}.
CC -!- DOMAIN: Contains 3 inactive NDK domains that do not possess all
CC residues considered to be crucial for the NDPK activity. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display normal reproductive system
CC phenotype. {ECO:0000269|PubMed:23707457}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NDK family.
CC {ECO:0000305}.
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DR EMBL; AF548543; AAQ12343.1; -; mRNA.
DR EMBL; BC052356; AAH52356.1; -; mRNA.
DR CCDS; CCDS26262.2; -. [Q715T0-1]
DR CCDS; CCDS49208.1; -. [Q715T0-2]
DR RefSeq; NP_001161381.1; NM_001167909.1. [Q715T0-2]
DR RefSeq; NP_853622.2; NM_181591.3. [Q715T0-1]
DR AlphaFoldDB; Q715T0; -.
DR SMR; Q715T0; -.
DR STRING; 10090.ENSMUSP00000089358; -.
DR PhosphoSitePlus; Q715T0; -.
DR PaxDb; 10090-ENSMUSP00000089358; -.
DR ProteomicsDB; 298075; -. [Q715T0-1]
DR ProteomicsDB; 298076; -. [Q715T0-2]
DR Antibodypedia; 12974; 124 antibodies from 26 providers.
DR DNASU; 73412; -.
DR Ensembl; ENSMUST00000039340.15; ENSMUSP00000047052.9; ENSMUSG00000041138.17. [Q715T0-2]
DR Ensembl; ENSMUST00000091763.3; ENSMUSP00000089358.3; ENSMUSG00000041138.17. [Q715T0-1]
DR GeneID; 73412; -.
DR KEGG; mmu:73412; -.
DR UCSC; uc007ppi.1; mouse. [Q715T0-2]
DR UCSC; uc007ppj.1; mouse. [Q715T0-1]
DR AGR; MGI:1920662; -.
DR CTD; 51314; -.
DR MGI; MGI:1920662; Nme8.
DR VEuPathDB; HostDB:ENSMUSG00000041138; -.
DR eggNOG; KOG0888; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000161182; -.
DR HOGENOM; CLU_016708_0_0_1; -.
DR InParanoid; Q715T0; -.
DR OMA; REIQYFF; -.
DR OrthoDB; 5481442at2759; -.
DR PhylomeDB; Q715T0; -.
DR TreeFam; TF106374; -.
DR BioGRID-ORCS; 73412; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Nme8; mouse.
DR PRO; PR:Q715T0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q715T0; Protein.
DR Bgee; ENSMUSG00000041138; Expressed in spermatid and 9 other cell types or tissues.
DR ExpressionAtlas; Q715T0; baseline and differential.
DR Genevisible; Q715T0; MM.
DR GO; GO:0005930; C:axoneme; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0036157; C:outer dynein arm; ISO:MGI.
DR GO; GO:0097598; C:sperm cytoplasmic droplet; IDA:MGI.
DR GO; GO:0035686; C:sperm fibrous sheath; ISO:MGI.
DR GO; GO:0097225; C:sperm midpiece; ISO:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IGI:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IGI:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd04416; NDPk_TX; 1.
DR CDD; cd02948; TRX_NDPK; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 3.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46135; NME/NM23 FAMILY MEMBER 8; 1.
DR PANTHER; PTHR46135:SF2; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00334; NDK; 3.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM00562; NDK; 2.
DR SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 3.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51374; NDPK_LIKE; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Disulfide bond; Hydrolase; Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..586
FT /note="Thioredoxin domain-containing protein 3"
FT /id="PRO_0000120157"
FT DOMAIN 10..116
FT /note="Thioredoxin"
FT REGION 157..254
FT /note="NDK 1"
FT /evidence="ECO:0000305"
FT REGION 312..452
FT /note="NDK 2"
FT /evidence="ECO:0000305"
FT REGION 453..586
FT /note="NDK 3"
FT /evidence="ECO:0000305"
FT DISULFID 39..42
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VAR_SEQ 464..470
FT /note="MEILKTI -> IHRSSRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014330"
FT VAR_SEQ 471..586
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014331"
FT CONFLICT 279
FT /note="H -> Y (in Ref. 2; AAH52356)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> F (in Ref. 2; AAH52356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 66857 MW; 5679ED17A63F1991 CRC64;
MASKKREVQL QSVVNSQNLW DEMLLNKGLT VIDVYQAWCG PCKAVQSLFR KLKNELNEDE
ILHFVVAEAD NIVTLQPFRD KCEPVFLFSL NGKIIAKIQG ANAPLINRKV ITLIDEERKI
VAGEMDRPQY VEIPLVDAID EEYGEVQYES AAEVYNMAII KPDAVLMRKN IEVREKIAKE
GFVIEIQENL ILPEEVVREF YTHIADQPDF EEFVVSMTNG LSCVLIVSQE DSEVIQEETL
PQTDTEEEPG VLEEPHVRFA PVMIKKKRDS LQEYMDRQHM SDYCDVEDDA VKVSKLIDIL
FPDFKTMKST NVQTTLALLH PDICEEEKDD VLNVIHNEGF TILMQRQIVL SEEEARTVCK
IHENEEYFDN LIGHMTSNHS YVLALRRENG VEYWKTLIGP KTIEEAYASH PQSLCVQFAS
GNFPTNQFYG SSSKAAAEKE IAHFFPPQST LALIKPHVTH KERMEILKTI KEAGFELTLM
KEMHLTPEHA NKIYFKITGK DFYKNVLEVL SLGMSLVMVL TKWNAVAEWR RMVGPVDPEE
AKLLSPESLR AKYGLDILRN AVHGASNFSE ASEIISNVFT EGNPEN
//
