ID   TXND2_MOUSE             Reviewed;         515 AA.
AC   Q6P902; Q8CJD1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 142.
DE   RecName: Full=Thioredoxin domain-containing protein 2;
DE   AltName: Full=Spermatid-specific thioredoxin-1;
DE            Short=Sptrx-1;
DE   AltName: Full=Thioredoxin-4;
GN   Name=Txndc2; Synonyms=Sptrx, Sptrx1, Trx4;
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], TISSUE SPECIFICITY, AND ENZYME ACTIVITY IN
RP   VITRO.
RX   PubMed=12149401; DOI=10.1093/molehr/8.8.710;
RA   Jimenez A., Oko R., Gustafsson J.-A., Spyrou G., Pelto-Huikko M.,
RA   Miranda-Vizuete A.;
RT   "Cloning, expression and characterization of mouse spermatid specific
RT   thioredoxin-1 gene and protein.";
RL   Mol. Hum. Reprod. 8:710-718(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12390887; DOI=10.1095/biolreprod.102.004838;
RA   Yu Y., Oko R., Miranda-Vizuete A.;
RT   "Developmental expression of spermatid-specific thioredoxin-1 protein:
RT   transient association to the longitudinal columns of the fibrous sheath
RT   during sperm tail formation.";
RL   Biol. Reprod. 67:1546-1554(2002).
RN   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Probably plays a regulatory role in sperm development. May
CC       participate in regulation of fibrous sheath (FS) assembly by supporting
CC       the formation of disulfide bonds during sperm tail morphogenesis. May
CC       also be required to rectify incorrect disulfide pairing and generate
CC       suitable pairs between the FS constituents. Can reduce disulfide bonds
CC       in vitro in the presence of NADP and thioredoxin reductase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Testis-specific. Strongly expressed in the
CC       testicular seminiferous tubules, mostly in the round spermatids.
CC       {ECO:0000269|PubMed:12149401, ECO:0000269|PubMed:12390887}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during spermiogenesis, restricted to the
CC       postmeiotic phase of spermatogenesis. First detected in elongating
CC       spermatids tails during steps 9 and 10 and is prominent in this region
CC       during steps 11-16. Also weakly present in the cytoplasmic lobe of
CC       these spermatids. During the last steps of spermiogenesis (steps 17-
CC       19), it strongly diminishes in the tail but appears to increase or
CC       become concentrated in the shrinking cytoplasmic lobe. By the last step
CC       of spermiogenesis (late step 19), cytoplasmic localization is barely
CC       detectable in the resulting residual body but still detectable in the
CC       cytoplasmic droplet (at protein level). Detected in testis of pre-
CC       pubertal animals at very low level. {ECO:0000269|PubMed:12390887,
CC       ECO:0000269|PubMed:15781233}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM94687.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF196282; AAM94687.2; ALT_INIT; mRNA.
DR   EMBL; BC060981; AAH60981.1; -; mRNA.
DR   RefSeq; NP_001139474.1; NM_001146002.1.
DR   RefSeq; NP_705739.2; NM_153519.2.
DR   AlphaFoldDB; Q6P902; -.
DR   SMR; Q6P902; -.
DR   STRING; 10090.ENSMUSP00000054909; -.
DR   iPTMnet; Q6P902; -.
DR   PhosphoSitePlus; Q6P902; -.
DR   PaxDb; 10090-ENSMUSP00000054909; -.
DR   ProteomicsDB; 298397; -.
DR   DNASU; 213272; -.
DR   GeneID; 213272; -.
DR   KEGG; mmu:213272; -.
DR   AGR; MGI:2389312; -.
DR   CTD; 84203; -.
DR   MGI; MGI:2389312; Txndc2.
DR   eggNOG; KOG0907; Eukaryota.
DR   InParanoid; Q6P902; -.
DR   OrthoDB; 5263941at2759; -.
DR   PhylomeDB; Q6P902; -.
DR   BioGRID-ORCS; 213272; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Txndc2; mouse.
DR   PRO; PR:Q6P902; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6P902; Protein.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0001520; C:outer dense fiber; ISO:MGI.
DR   GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:MGI.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; 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:0030317; P:flagellated sperm motility; IGI:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; THIOREDOXIN; 1.
DR   PANTHER; PTHR10438:SF107; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Disulfide bond;
KW   Phosphoprotein; Redox-active center; Reference proteome; Repeat;
KW   Spermatogenesis.
FT   CHAIN           1..515
FT                   /note="Thioredoxin domain-containing protein 2"
FT                   /id="PRO_0000120154"
FT   REPEAT          92..106
FT                   /note="1"
FT   REPEAT          107..121
FT                   /note="2"
FT   REPEAT          122..136
FT                   /note="3"
FT   REPEAT          137..151
FT                   /note="4"
FT   REPEAT          152..166
FT                   /note="5"
FT   REPEAT          167..181
FT                   /note="6"
FT   REPEAT          182..196
FT                   /note="7"
FT   REPEAT          197..211
FT                   /note="8"
FT   REPEAT          212..226
FT                   /note="9"
FT   REPEAT          227..241
FT                   /note="10"
FT   REPEAT          242..256
FT                   /note="11"
FT   REPEAT          257..271
FT                   /note="12"
FT   REPEAT          272..286
FT                   /note="13"
FT   REPEAT          287..301
FT                   /note="14"
FT   REPEAT          302..316
FT                   /note="15"
FT   REPEAT          317..331
FT                   /note="16"
FT   REPEAT          332..346
FT                   /note="17"
FT   REPEAT          347..362
FT                   /note="18"
FT   REPEAT          363..375
FT                   /note="19"
FT   REPEAT          376..390
FT                   /note="20"
FT   REPEAT          391..405
FT                   /note="21"
FT   DOMAIN          398..515
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..405
FT                   /note="21 X 15 AA approximate tandem repeat of Q-P-K-X-G-D-
FT                   I-P-K-S-[PS]-E-[KE]-X-I"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XHX6"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XHX6"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XHX6"
FT   DISULFID        442..445
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   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
//