ID   H7BX21_MOUSE            Unreviewed;       550 AA.
AC   H7BX21;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Thioredoxin domain containing 2 (spermatozoa) {ECO:0000313|Ensembl:ENSMUSP00000054909.6};
GN   Name=Txndc2 {ECO:0000313|Ensembl:ENSMUSP00000054909.6,
GN   ECO:0000313|MGI:MGI:2389312};
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 {ECO:0000313|Ensembl:ENSMUSP00000054909.6, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000054909.6, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000054909.6,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000054909.6}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000054909.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001139474.1; NM_001146002.1.
DR   AlphaFoldDB; H7BX21; -.
DR   SMR; H7BX21; -.
DR   SwissPalm; H7BX21; -.
DR   PeptideAtlas; H7BX21; -.
DR   ProteomicsDB; 314233; -.
DR   Antibodypedia; 6577; 28 antibodies from 16 providers.
DR   DNASU; 213272; -.
DR   Ensembl; ENSMUST00000050236.7; ENSMUSP00000054909.6; ENSMUSG00000050612.7.
DR   GeneID; 213272; -.
DR   UCSC; uc008dge.2; mouse.
DR   AGR; MGI:2389312; -.
DR   CTD; 84203; -.
DR   MGI; MGI:2389312; Txndc2.
DR   VEuPathDB; HostDB:ENSMUSG00000050612; -.
DR   GeneTree; ENSGT00940000163147; -.
DR   HOGENOM; CLU_045129_0_0_1; -.
DR   OMA; PNFPAKF; -.
DR   OrthoDB; 5263941at2759; -.
DR   TreeFam; TF106377; -.
DR   BioGRID-ORCS; 213272; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Txndc2; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000050612; Expressed in seminiferous tubule of testis and 21 other cell types or tissues.
DR   ExpressionAtlas; H7BX21; baseline and differential.
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   Proteomics identification {ECO:0007829|PeptideAtlas:H7BX21,
KW   ECO:0007829|ProteomicsDB:H7BX21};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          433..550
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  61690 MW;  F17AC964826F2357 CRC64;
     MDLAIEEMFK KDKQKNKDKG LDMNSVQAGA PEESDMTLNN GGKANERGSN ENPLQALSKN
     EAFLVPEFLD TAQSKEKAIA SKVSNTLHMS TEESEFPQQV SSTPMFSENT VHPRHEVSPK
     PSSKNTQLKQ ENISKSSGYS KQTNYSNTPK SLAKTTHPKQ GSTLKPATNS THYREDDIPK
     SSEDIIQPKK GDRPKSSEDI IQSKKEDRPK SSEDIIQSKK EDRPKSSEDI IQSKKEDRPK
     SSEDIIQSKK EDRPKSSEDI IQPKKEDRPK SSEDSVPSKK GDRPKSSEDS VQPKKEDRPK
     SSEDSVQSKE GEVHKPLKDS IQSKETKVPK SPQDSIQSKE DKTHRPLKDS VQSKESEEPK
     SSHESIQSKE DKIHKPLKDS IPSKEGDIPK SPEDTIQSQE EITASEEDTI QSQEGNTIKS
     SEEDVQLSES KLLGLGAEIE TLEEGLVRVI KDKEEFEEVL KDAGEKLVAV DFSAAWCGPC
     RMMKPLFHSL SLKHEDVIFL EVDTEDCEQL VQDCEIFHLP TFQFYKNEEK VGEFSGALVG
     KLERSISELK
//