TXND2_RAT
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 03-AUG-2022, entry version 124.
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.ENSRNOP00000048534; -.
DR iPTMnet; Q5XHX6; -.
DR PhosphoSitePlus; Q5XHX6; -.
DR PaxDb; Q5XHX6; -.
DR Ensembl; ENSRNOT00000032330; ENSRNOP00000034030; ENSRNOG00000027916. [Q5XHX6-1]
DR Ensembl; ENSRNOT00000065073; ENSRNOP00000062071; ENSRNOG00000027916. [Q5XHX6-2]
DR GeneID; 316777; -.
DR KEGG; rno:316777; -.
DR UCSC; RGD:1359251; rat. [Q5XHX6-1]
DR CTD; 84203; -.
DR RGD; 1359251; Txndc2.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000163147; -.
DR InParanoid; Q5XHX6; -.
DR OMA; TIQPKQG; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q5XHX6; -.
DR TreeFam; TF106377; -.
DR PRO; PR:Q5XHX6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000027916; Expressed in testis and 1 other 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 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 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 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
