TXND3_RAT
ID TXND3_RAT Reviewed; 587 AA.
AC Q715S9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thioredoxin domain-containing protein 3;
DE AltName: Full=NME/NM23 family member 8;
DE AltName: Full=Spermatid-specific thioredoxin-2;
DE Short=Sptrx-2;
GN Name=Nme8; Synonyms=Sptrx2, Txndc3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
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).
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. May be involved in the
CC reduction of disulfide bonds within the sperm FS components. In vitro,
CC it has neither NDP kinase nor reducing activity on disulfide bonds (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12909633}. Note=In
CC spermatozoa, it is an integral component of the FS.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q715S9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q715S9-2; Sequence=VSP_014332;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:12909633}.
CC -!- DEVELOPMENTAL STAGE: Prominently detected in the cytoplasmic lobe of
CC step 15-18 spermatids and diminishes in step 19 just before
CC spermiation. In the spermatid tail, it increases from step 15 to 19 and
CC is confined to the principal piece. First detected scattered throughout
CC the cytoplasm of the axoneme in step 14-15 spermatids, but begins to be
CC incorporated by step 16 into the FS. During steps 17-18, it increases
CC over the ribs and columns of the assembled FS. It peaks in step 19 and
CC remains in the FS of epididymal spermatozoa.
CC {ECO:0000269|PubMed:12909633}.
CC -!- DOMAIN: Contains 3 inactive NDK domains that each lack the active His
CC residue, suggesting that they have no NDP kinase activity.
CC -!- MISCELLANEOUS: In vasectomized rats, autoantibodies against Txndc3 are
CC present.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NDK family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ12344.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF548544; AAQ12344.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q715S9; -.
DR SMR; Q715S9; -.
DR STRING; 10116.ENSRNOP00000062434; -.
DR PaxDb; Q715S9; -.
DR PRIDE; Q715S9; -.
DR UCSC; RGD:735069; rat. [Q715S9-1]
DR RGD; 735069; Nme8.
DR VEuPathDB; HostDB:ENSRNOG00000058285; -.
DR eggNOG; KOG0888; Eukaryota.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_016708_0_0_1; -.
DR InParanoid; Q715S9; -.
DR PhylomeDB; Q715S9; -.
DR TreeFam; TF106374; -.
DR PRO; PR:Q715S9; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000058285; Expressed in testis and 3 other tissues.
DR ExpressionAtlas; Q715S9; baseline.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0036157; C:outer dynein arm; ISO:RGD.
DR GO; GO:0097598; C:sperm cytoplasmic droplet; ISO:RGD.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0097225; C:sperm midpiece; ISO:RGD.
DR GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; NAS:RGD.
DR Gene3D; 3.30.70.141; -; 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 Pfam; PF00334; NDK; 3.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM00562; NDK; 2.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54919; SSF54919; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Disulfide bond; Redox-active center; Reference proteome; Repeat;
KW Spermatogenesis.
FT CHAIN 1..587
FT /note="Thioredoxin domain-containing protein 3"
FT /id="PRO_0000120158"
FT DOMAIN 2..119
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 157..255
FT /note="NDK 1"
FT REGION 313..453
FT /note="NDK 2"
FT REGION 454..587
FT /note="NDK 3"
FT DISULFID 39..42
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 154..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12909633"
FT /id="VSP_014332"
SQ SEQUENCE 587 AA; 67312 MW; 7FC3D94DFCE19F4B CRC64;
MASKKREVQL QSVVNSQNLW DEMLLNKGLT VIDVYQAWCG PCKAVQALFR KLKNELNEDE
LLHFVVAEAD SIVTLQPFRD KCEPVFLFSL NGKIIAKIQG ANAPLINRKV IALIDEEKKI
AAGEMARPQY VEIPLVDSLD EEYGEVHYES NVEVYNMAVI NPDAVLMRKN LEIKEKITKE
GFIIEIQENM LLPEEVAREF YNHMIDEPDF EEFVYSMTNR LSCVLIISQG EDTEVIEEEA
LPQSDDEEEP DPLEEPHVRF APMLVKKKRD SLQEYMDRQH MSDYCHVEDD AVKVSKFIDI
LFPDFKTMKS TNVQRTLGLL YPEVCEEEKD NVLDIIQNEG FTILMQRQVV LSEEEARAVC
HVHEDEDYFD NLIGYMCSNN SYILVLMREH SVERWKELIG PKTVEEAYAS HPDSLCVRFA
SGNFPVNQFY GSSSKAAAET EIEHFFPPQS TLALIKPHVS HKERMEILKA IRDARFELTQ
MKEMHLTPEH ASKVYFKITG KDFYKNVLDV LSSGMSVVMI LTKWNAVGEW RRMMGPVDPE
EAKLLSPNSL RARYGIDVLR NAVHGASNMS EAATAISNVF TESNFEN
