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Thioredoxin domain-containing protein 2 (Spermatid-specific thioredoxin-1) (Sptrx-1) (Thioredoxin-4)

 TXND2_MOUSE             Reviewed;         515 AA.
Q6P902; Q8CJD1;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
18-JUL-2018, entry version 121.
RecName: Full=Thioredoxin domain-containing protein 2;
AltName: Full=Spermatid-specific thioredoxin-1;
Short=Sptrx-1;
AltName: Full=Thioredoxin-4;
Name=Txndc2; Synonyms=Sptrx, Sptrx1, Trx4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ENZYME ACTIVITY IN
VITRO.
PubMed=12149401; DOI=10.1093/molehr/8.8.710;
Jimenez A., Oko R., Gustafsson J.-A., Spyrou G., Pelto-Huikko M.,
Miranda-Vizuete A.;
"Cloning, expression and characterization of mouse spermatid specific
thioredoxin-1 gene and protein.";
Mol. Hum. Reprod. 8:710-718(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12390887; DOI=10.1095/biolreprod.102.004838;
Yu Y., Oko R., Miranda-Vizuete A.;
"Developmental expression of spermatid-specific thioredoxin-1 protein:
transient association to the longitudinal columns of the fibrous
sheath during sperm tail formation.";
Biol. Reprod. 67:1546-1554(2002).
[4]
DEVELOPMENTAL STAGE.
PubMed=15781233; DOI=10.1016/j.bbrc.2005.02.128;
Jimenez A., Prieto-Alamo M.J., Fuentes-Almagro C.A., Jurado J.,
Gustafsson J.-A., Pueyo C., Miranda-Vizuete A.;
"Absolute mRNA levels and transcriptional regulation of the mouse
testis-specific thioredoxins.";
Biochem. Biophys. Res. Commun. 330:65-74(2005).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Probably plays a regulatory role in sperm development.
May participate in regulation of fibrous sheath (FS) assembly by
supporting the formation of disulfide bonds during sperm tail
morphogenesis. May also be required to rectify incorrect disulfide
pairing and generate suitable pairs between the FS constituents.
Can reduce disulfide bonds in vitro in the presence of NADP and
thioredoxin reductase.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Testis-specific. Strongly expressed in the
testicular seminiferous tubules, mostly in the round spermatids.
{ECO:0000269|PubMed:12149401, ECO:0000269|PubMed:12390887}.
-!- DEVELOPMENTAL STAGE: Expressed during spermiogenesis, restricted
to the postmeiotic phase of spermatogenesis. First detected in
elongating spermatids tails during steps 9 and 10 and is prominent
in this region during steps 11-16. Also weakly present in the
cytoplasmic lobe of these spermatids. During the last steps of
spermiogenesis (steps 17-19), it strongly diminishes in the tail
but appears to increase or become concentrated in the shrinking
cytoplasmic lobe. By the last step of spermiogenesis (late step
19), cytoplasmic localization is barely detectable in the
resulting residual body but still detectable in the cytoplasmic
droplet (at protein level). Detected in testis of pre-pubertal
animals at very low level. {ECO:0000269|PubMed:12390887,
ECO:0000269|PubMed:15781233}.
-!- SEQUENCE CAUTION:
Sequence=AAM94687.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF196282; AAM94687.2; ALT_INIT; mRNA.
EMBL; BC060981; AAH60981.1; -; mRNA.
RefSeq; NP_001139474.1; NM_001146002.1.
RefSeq; NP_705739.2; NM_153519.2.
UniGene; Mm.255732; -.
ProteinModelPortal; Q6P902; -.
SMR; Q6P902; -.
STRING; 10090.ENSMUSP00000054909; -.
iPTMnet; Q6P902; -.
PhosphoSitePlus; Q6P902; -.
PaxDb; Q6P902; -.
PRIDE; Q6P902; -.
GeneID; 213272; -.
KEGG; mmu:213272; -.
CTD; 84203; -.
MGI; MGI:2389312; Txndc2.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000154719; -.
HOVERGEN; HBG087115; -.
InParanoid; Q6P902; -.
PhylomeDB; Q6P902; -.
PRO; PR:Q6P902; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_TXNDC2; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0001520; C:outer dense fiber; ISO:MGI.
GO; GO:0036126; C:sperm flagellum; IDA:MGI.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:MGI.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
GO; GO:0047134; F:protein-disulfide reductase activity; IBA:GO_Central.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; IGI:MGI.
GO; GO:0030317; P:flagellated sperm motility; IGI:MGI.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10438; PTHR10438; 5.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Disulfide bond; Phosphoprotein; Redox-active center;
Reference proteome; Repeat; Spermatogenesis.
CHAIN 1 515 Thioredoxin domain-containing protein 2.
/FTId=PRO_0000120154.
REPEAT 92 106 1.
REPEAT 107 121 2.
REPEAT 122 136 3.
REPEAT 137 151 4.
REPEAT 152 166 5.
REPEAT 167 181 6.
REPEAT 182 196 7.
REPEAT 197 211 8.
REPEAT 212 226 9.
REPEAT 227 241 10.
REPEAT 242 256 11.
REPEAT 257 271 12.
REPEAT 272 286 13.
REPEAT 287 301 14.
REPEAT 302 316 15.
REPEAT 317 331 16.
REPEAT 332 346 17.
REPEAT 347 362 18.
REPEAT 363 375 19.
REPEAT 376 390 20.
REPEAT 391 405 21.
DOMAIN 398 515 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 92 405 21 X 15 AA approximate tandem repeat of
Q-P-K-X-G-D-I-P-K-S-[PS]-E-[KE]-X-I.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XHX6}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XHX6}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XHX6}.
DISULFID 442 445 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
SEQUENCE 515 AA; 57767 MW; 46F178558C27A71A CRC64;
MTLNNGGKAN ERGSNENPLQ ALSKNEAFLV PEFLDTAQSK EKAIASKVSN TLHMSTEESE
FPQQVSSTPM FSENTVHPRH EVSPKPSSKN TQLKQENISK SSGYSKQTNY SNTPKSLAKT
THPKQGSTLK PATNSTHYRE DDIPKSSEDI IQPKKGDRPK SSEDIIQSKK EDRPKSSEDI
IQSKKEDRPK SSEDIIQSKK EDRPKSSEDI IQSKKEDRPK SSEDIIQPKK EDRPKSSEDS
VPSKKGDRPK SSEDSVQPKK EDRPKSSEDS VQSKEGEVHK PLKDSIQSKE TKVPKSPQDS
IQSKEDKTHR PLKDSVQSKE SEEPKSSHES IQSKEDKIHK PLKDSIPSKE GDIPKSPEDT
IQSQEEITAS EEDTIQSQEG NTIKSSEEDV QLSESKLLGL GAEIETLEEG LVRVIKDKEE
FEEVLKDAGE KLVAVDFSAA WCGPCRMMKP LFHSLSLKHE DVIFLEVDTE DCEQLVQDCE
IFHLPTFQFY KNEEKVGEFS GALVGKLERS ISELK


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