ID TXND2_RAT Reviewed; 550 AA. AC Q5XHX6; Q6AY11; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 24-JAN-2024, entry version 130. DE RecName: Full=Thioredoxin domain-containing protein 2; DE AltName: Full=Spermatid-specific thioredoxin-1; DE Short=Sptrx-1; GN Name=Txndc2; Synonyms=Sptrx, Sptrx1; 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [2] 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-51; SER-158; SER-351; RP SER-379 AND SER-407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5XHX6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5XHX6-2; Sequence=VSP_014329; CC -!- TISSUE SPECIFICITY: Testis-specific. Strongly expressed in the CC testicular seminiferous tubules, mostly in the round spermatids. CC {ECO:0000269|PubMed:12390887}. CC -!- DEVELOPMENTAL STAGE: Transiently expressed in spermiogenesis, being CC mostly concentrated in the periaxonemal compartment of the tail of the CC elongating spermatid, where it transiently associates with the CC longitudinal column of the FS. In the very last steps (steps 17-19), CC when periaxonemal expression disappears, it is still weakly present in CC the shrinking cytoplasmic lobe (at protein level). CC {ECO:0000269|PubMed:12390887}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH79238.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH83924.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC079238; AAH79238.1; ALT_INIT; mRNA. DR EMBL; BC083924; AAH83924.1; ALT_INIT; mRNA. DR RefSeq; NP_001005559.2; NM_001005559.2. DR RefSeq; NP_001139476.1; NM_001146004.1. [Q5XHX6-1] DR RefSeq; XP_006245669.1; XM_006245607.3. [Q5XHX6-2] DR AlphaFoldDB; Q5XHX6; -. DR SMR; Q5XHX6; -. DR STRING; 10116.ENSRNOP00000034030; -. DR iPTMnet; Q5XHX6; -. DR PhosphoSitePlus; Q5XHX6; -. DR PaxDb; 10116-ENSRNOP00000048534; -. DR Ensembl; ENSRNOT00000032330.6; ENSRNOP00000034030.4; ENSRNOG00000027916.7. [Q5XHX6-1] DR Ensembl; ENSRNOT00000065073.4; ENSRNOP00000062071.2; ENSRNOG00000027916.7. [Q5XHX6-2] DR GeneID; 316777; -. DR KEGG; rno:316777; -. DR UCSC; RGD:1359251; rat. [Q5XHX6-1] DR AGR; RGD:1359251; -. DR CTD; 84203; -. DR RGD; 1359251; Txndc2. DR eggNOG; KOG0907; Eukaryota. DR GeneTree; ENSGT00940000163147; -. DR InParanoid; Q5XHX6; -. DR OMA; PNFPAKF; -. DR OrthoDB; 5263941at2759; -. DR PhylomeDB; Q5XHX6; -. DR TreeFam; TF106377; -. DR PRO; PR:Q5XHX6; -. DR Proteomes; UP000002494; Chromosome 9. DR Bgee; ENSRNOG00000027916; Expressed in testis and 1 other cell type or tissue. DR ExpressionAtlas; Q5XHX6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0001520; C:outer dense fiber; IDA:RGD. DR GO; GO:0036126; C:sperm flagellum; ISO:RGD. DR GO; GO:0003756; F:protein disulfide isomerase activity; ISO:RGD. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; ISO:RGD. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD. DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD. 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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation; KW Disulfide bond; Phosphoprotein; Redox-active center; Reference proteome; KW Repeat; Spermatogenesis. FT CHAIN 1..550 FT /note="Thioredoxin domain-containing protein 2" FT /id="PRO_0000120155" FT REPEAT 104..118 FT /note="1" FT REPEAT 119..133 FT /note="2" FT REPEAT 134..148 FT /note="3" FT REPEAT 149..163 FT /note="4" FT REPEAT 164..178 FT /note="5" FT REPEAT 179..193 FT /note="6" FT REPEAT 194..208 FT /note="7" FT REPEAT 209..223 FT /note="8" FT REPEAT 224..238 FT /note="9" FT REPEAT 239..252 FT /note="10" FT REPEAT 253..267 FT /note="11" FT REPEAT 268..282 FT /note="12" FT REPEAT 283..297 FT /note="13" FT REPEAT 298..312 FT /note="14" FT REPEAT 313..327 FT /note="15" FT REPEAT 328..342 FT /note="16" FT REPEAT 343..357 FT /note="17" FT REPEAT 358..384 FT /note="18" FT REPEAT 385..399 FT /note="19" FT REPEAT 400..412 FT /note="20" FT DOMAIN 401..550 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REPEAT 413..425 FT /note="21" FT REPEAT 426..440 FT /note="22" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 104..440 FT /note="22 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 64..144 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 147..205 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 252..275 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..301 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 313..347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..421 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 379 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT DISULFID 477..480 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT VAR_SEQ 1..43 FT /note="MFKKNQKLSKDKGLEVNSVQAGAPEESDVKLNNGGKANERGSN -> MQSKC FT GKQANDLKMITELFLK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014329" SQ SEQUENCE 550 AA; 61103 MW; 5F624DF65422E2A4 CRC64; MFKKNQKLSK DKGLEVNSVQ AGAPEESDVK LNNGGKANER GSNEFLDTAQ SKEKVIASVV GNMLHMSTEE SEPPQQVSST SMFSENTIYP KHEGSPKSST KNTQLKQEDI SKTSSYSKQT NSSNIPKSLA ITTYPKQGST LKPAANGTHD REAEKPKSSE DLIQSKKGDI FKPSEDSIQS KKGDMPKSSE DPIQSKKDDT AKSLEDTIQS KNGDMPKSSE DPIQSKKDDT ARSLEDSIQS KKGDMPKSSD TIQSKESETP KFLQDTIQSK GGKINKQVKD SMKSKESKIR KPLKDSIQSK ENKIPKSSQD SAQPKEGKIH KPLKDSLPSK EGDISKPSED TIQAKEEITV SPEDTIQAKE EITMSPEDTI QAKEEITVSP EDTIQAKEEI TVSPEDTMQS KEEITVSPED TVQSQEGDIK SSEDVQPSEN EIFPFEAEIE TLEEGMVRVI KDKEEFEEVL KDAGEKLVAV DFSAPWCGPC RKMRPHFHSL SLKHEDVIFL EVDTEDCEQL VQDCEVFHLP TFQFYKNEEK VGEFSGALVE KLEKSIAELK //