TXND2_HUMAN
ID TXND2_HUMAN Reviewed; 553 AA.
AC Q86VQ3; A5YM73; Q8N7U4; Q96RX3; Q9H0L8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 171.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ENZYME ACTIVITY IN VITRO.
RX PubMed=11399755; DOI=10.1074/jbc.m101760200;
RA Miranda-Vizuete A., Ljung J., Damdimopoulos A.E., Gustafsson J.-A., Oko R.,
RA Pelto-Huikko M., Spyrou G.;
RT "Characterization of Sptrx, a novel member of the thioredoxin family
RT specifically expressed in human spermatozoa.";
RL J. Biol. Chem. 276:31567-31574(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT LYS-341.
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LYS-341;
RP ASP-357 AND THR-487.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS LYS-341
RP AND ASP-357.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-553, AND VARIANT THR-461.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP ENZYME ACTIVITY IN VITRO.
RX PubMed=12387870; DOI=10.1016/s0014-5793(02)03417-8;
RA Jimenez A., Johansson C., Ljung J., Sagemark J., Berndt K.D., Ren B.,
RA Tibbelin G., Ladenstein R., Kieselbach T., Holmgren A., Gustafsson J.-A.,
RA Miranda-Vizuete A.;
RT "Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein
RT with oxidizing activity.";
RL FEBS Lett. 530:79-84(2002).
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 -!- INTERACTION:
CC Q86VQ3; P35638: DDIT3; NbExp=3; IntAct=EBI-1220595, EBI-742651;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11399755}. Note=In
CC ejaculated spermatozoa, it localizes in the caudal region of the head
CC to the end of the principal piece.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VQ3-2; Sequence=VSP_014328;
CC Name=3;
CC IsoId=Q86VQ3-3; Sequence=VSP_053684;
CC -!- TISSUE SPECIFICITY: Testis-specific. Only expressed during
CC spermiogenesis, prominently in round and elongating spermatids.
CC {ECO:0000269|PubMed:11399755}.
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DR EMBL; AF080095; AAK94950.1; -; mRNA.
DR EMBL; EF560747; ABQ59057.1; -; mRNA.
DR EMBL; AK097656; BAC05133.1; -; mRNA.
DR EMBL; AC006238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050132; AAH50132.1; -; mRNA.
DR EMBL; AL136742; CAB66676.2; -; mRNA.
DR CCDS; CCDS11846.1; -. [Q86VQ3-2]
DR CCDS; CCDS42414.1; -. [Q86VQ3-1]
DR RefSeq; NP_001091999.1; NM_001098529.1. [Q86VQ3-1]
DR RefSeq; NP_115619.4; NM_032243.5. [Q86VQ3-2]
DR RefSeq; XP_016881530.1; XM_017026041.1.
DR AlphaFoldDB; Q86VQ3; -.
DR SMR; Q86VQ3; -.
DR BioGRID; 123944; 16.
DR IntAct; Q86VQ3; 2.
DR STRING; 9606.ENSP00000304908; -.
DR iPTMnet; Q86VQ3; -.
DR PhosphoSitePlus; Q86VQ3; -.
DR BioMuta; TXNDC2; -.
DR DMDM; 313104290; -.
DR jPOST; Q86VQ3; -.
DR MassIVE; Q86VQ3; -.
DR MaxQB; Q86VQ3; -.
DR PaxDb; Q86VQ3; -.
DR PeptideAtlas; Q86VQ3; -.
DR PRIDE; Q86VQ3; -.
DR ProteomicsDB; 70057; -. [Q86VQ3-1]
DR ProteomicsDB; 70058; -. [Q86VQ3-2]
DR Antibodypedia; 6577; 28 antibodies from 16 providers.
DR DNASU; 84203; -.
DR Ensembl; ENST00000306084.6; ENSP00000304908.6; ENSG00000168454.13. [Q86VQ3-1]
DR Ensembl; ENST00000357775.6; ENSP00000350419.4; ENSG00000168454.13. [Q86VQ3-2]
DR GeneID; 84203; -.
DR KEGG; hsa:84203; -.
DR MANE-Select; ENST00000357775.6; ENSP00000350419.4; NM_032243.6; NP_115619.4. [Q86VQ3-2]
DR UCSC; uc002koh.5; human. [Q86VQ3-1]
DR CTD; 84203; -.
DR DisGeNET; 84203; -.
DR GeneCards; TXNDC2; -.
DR HGNC; HGNC:16470; TXNDC2.
DR HPA; ENSG00000168454; Tissue enriched (testis).
DR MIM; 617790; gene.
DR neXtProt; NX_Q86VQ3; -.
DR OpenTargets; ENSG00000168454; -.
DR PharmGKB; PA38147; -.
DR VEuPathDB; HostDB:ENSG00000168454; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000163147; -.
DR HOGENOM; CLU_045129_0_0_1; -.
DR InParanoid; Q86VQ3; -.
DR PhylomeDB; Q86VQ3; -.
DR TreeFam; TF106377; -.
DR PathwayCommons; Q86VQ3; -.
DR SignaLink; Q86VQ3; -.
DR BioGRID-ORCS; 84203; 8 hits in 1071 CRISPR screens.
DR GeneWiki; TXNDC2; -.
DR GenomeRNAi; 84203; -.
DR Pharos; Q86VQ3; Tbio.
DR PRO; PR:Q86VQ3; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q86VQ3; protein.
DR Bgee; ENSG00000168454; Expressed in left testis and 87 other tissues.
DR ExpressionAtlas; Q86VQ3; baseline and differential.
DR Genevisible; Q86VQ3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
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..553
FT /note="Thioredoxin domain-containing protein 2"
FT /id="PRO_0000120153"
FT REPEAT 113..127
FT /note="1"
FT REPEAT 128..142
FT /note="2"
FT REPEAT 143..157
FT /note="3"
FT REPEAT 158..172
FT /note="4"
FT REPEAT 173..187
FT /note="5"
FT REPEAT 188..202
FT /note="6"
FT REPEAT 203..217
FT /note="7"
FT REPEAT 218..232
FT /note="8"
FT REPEAT 233..247
FT /note="9"
FT REPEAT 248..262
FT /note="10"
FT REPEAT 263..277
FT /note="11"
FT REPEAT 278..292
FT /note="12"
FT REPEAT 293..307
FT /note="13"
FT REPEAT 308..322
FT /note="14"
FT REPEAT 323..337
FT /note="15"
FT REPEAT 338..352
FT /note="16"
FT REPEAT 353..367
FT /note="17"
FT REPEAT 368..382
FT /note="18"
FT REPEAT 383..397
FT /note="19"
FT REPEAT 398..412
FT /note="20"
FT REPEAT 413..427
FT /note="21"
FT REPEAT 428..442
FT /note="22"
FT DOMAIN 429..553
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..442
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 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHX6"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XHX6"
FT DISULFID 480..483
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11399755,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014328"
FT VAR_SEQ 304..318
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053684"
FT VARIANT 225
FT /note="A -> P (in dbSNP:rs11662946)"
FT /id="VAR_057351"
FT VARIANT 314
FT /note="I -> L (in dbSNP:rs2240909)"
FT /id="VAR_057352"
FT VARIANT 341
FT /note="E -> K (in dbSNP:rs11081510)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_022762"
FT VARIANT 357
FT /note="G -> D (in dbSNP:rs2240906)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_022763"
FT VARIANT 461
FT /note="A -> T (in dbSNP:rs17732496)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_022764"
FT VARIANT 487
FT /note="R -> T (in dbSNP:rs17805544)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_022765"
SQ SEQUENCE 553 AA; 60404 MW; 74EE3210BA5EBCF1 CRC64;
MDVDKELGME SVKAGASGKP EMRLGTQEET SEGDANESSL LVLSSNVPLL ALEFLEIAQA
KEKAFLPMVS HTFHMRTEES DASQEGDDLP KSSANTSHPK QDDSPKSSEE TIQPKEGDIP
KAPEETIQSK KEDLPKSSEK AIQPKESNIP KSSAKPIQPK LGNIPKASVK PSQPKEGDIP
KAPEETIQSK KEDLPKSSEE AIQPKEGDIP KSSAKPIQPK LGNIAKTSVK PSQPKESDIP
KSPEETIQPK EGDIPKSSAK PIQPKLGNIP KASVKPSQPK EGDISKSPEE AIQPKEGDLP
KSLEEAIQPK EGDIPKSPEE AIQPKEGDIP KSLEEAIQPK EGDIPKSPEE TIQPKKGDIP
KSPEEAIQPK EGDIPKSPKQ AIQPKEGDIP KSLEEAIPPK EIDIPKSPEE TIQPKEDDSP
KSLEEATPSK EGDILKPEEE TMEFPEGDKV KVILSKEDFE ASLKEAGERL VAVDFSATWC
GPCRTIRPFF HALSVKHEDV VFLEVDADNC EEVVRECAIM CVPTFQFYKK EEKVDELCGA
LKEKLEAVIA ELK
