TXND2_MOUSE
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 25-MAY-2022, entry version 138.
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; Q6P902; -.
DR PRIDE; Q6P902; -.
DR ProteomicsDB; 298397; -.
DR DNASU; 213272; -.
DR GeneID; 213272; -.
DR KEGG; mmu:213272; -.
DR CTD; 84203; -.
DR MGI; MGI:2389312; Txndc2.
DR eggNOG; KOG0907; Eukaryota.
DR InParanoid; Q6P902; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q6P902; -.
DR BioGRID-ORCS; 213272; 0 hits in 72 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 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 InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 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
