TXND5_MOUSE
ID TXND5_MOUSE Reviewed; 417 AA.
AC Q91W90; Q8R1I6;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Thioredoxin domain-containing protein 5 {ECO:0000305|PubMed:12930873};
DE EC=1.8.4.- {ECO:0000269|PubMed:14971039};
DE EC=5.3.4.1 {ECO:0000269|PubMed:12930873};
DE AltName: Full=Endoplasmic reticulum resident protein 46 {ECO:0000303|PubMed:12930873};
DE Short=ER protein 46 {ECO:0000303|PubMed:12930873};
DE Short=ERp46 {ECO:0000303|PubMed:12930873};
DE AltName: Full=Plasma cell-specific thioredoxin-related protein {ECO:0000303|PubMed:14971039};
DE Short=PC-TRP {ECO:0000303|PubMed:14971039};
DE AltName: Full=Thioredoxin-like protein p46;
DE Flags: Precursor;
GN Name=Txndc5 {ECO:0000312|MGI:MGI:2145316}; Synonyms=Tlp46;
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], PROTEIN SEQUENCE OF 316-329 AND 401-411,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=BALB/cJ;
RX PubMed=12930873; DOI=10.1074/mcp.m300053-mcp200;
RA Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D.,
RA Li L., Michalak M.;
RT "ERp19 and ERp46, new members of the thioredoxin family of endoplasmic
RT reticulum proteins.";
RL Mol. Cell. Proteomics 2:1104-1119(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=B-cell;
RX PubMed=14971039; DOI=10.1002/eji.200324225;
RA Wrammert J., Kallberg E., Leanderson T.;
RT "Identification of a novel thioredoxin-related protein, PC-TRP, which is
RT preferentially expressed in plasma cells.";
RL Eur. J. Immunol. 34:137-146(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Salivary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and 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: Protein disulfide isomerase of the endoplasmic reticulum
CC lumen involved in the formation of disulfide bonds in proteins
CC (PubMed:12930873, PubMed:14971039). Can reduce insulin disulfide bonds
CC (PubMed:14971039). {ECO:0000269|PubMed:12930873,
CC ECO:0000269|PubMed:14971039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000269|PubMed:12930873};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12930873}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in plasma cells and at
CC very low levels in all other cells and tissues examined (at protein
CC level). {ECO:0000269|PubMed:14971039}.
CC -!- MASS SPECTROMETRY: Mass=51200; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12930873};
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AY548112; AAS55652.1; -; mRNA.
DR EMBL; AY243534; AAP68841.1; -; mRNA.
DR EMBL; BC016252; AAH16252.2; -; mRNA.
DR EMBL; BC024505; AAH24505.1; -; mRNA.
DR EMBL; BC046789; AAH46789.3; -; mRNA.
DR CCDS; CCDS26463.1; -.
DR RefSeq; NP_001276527.1; NM_001289598.1.
DR RefSeq; NP_001276528.1; NM_001289599.1.
DR RefSeq; NP_663342.3; NM_145367.4.
DR AlphaFoldDB; Q91W90; -.
DR SMR; Q91W90; -.
DR BioGRID; 222795; 17.
DR STRING; 10090.ENSMUSP00000041839; -.
DR iPTMnet; Q91W90; -.
DR PhosphoSitePlus; Q91W90; -.
DR SwissPalm; Q91W90; -.
DR REPRODUCTION-2DPAGE; Q91W90; -.
DR EPD; Q91W90; -.
DR jPOST; Q91W90; -.
DR MaxQB; Q91W90; -.
DR PaxDb; Q91W90; -.
DR PeptideAtlas; Q91W90; -.
DR PRIDE; Q91W90; -.
DR ProteomicsDB; 298074; -.
DR Antibodypedia; 34993; 565 antibodies from 34 providers.
DR DNASU; 105245; -.
DR Ensembl; ENSMUST00000035988; ENSMUSP00000041839; ENSMUSG00000038991.
DR GeneID; 105245; -.
DR KEGG; mmu:105245; -.
DR UCSC; uc007qdq.2; mouse.
DR CTD; 81567; -.
DR MGI; MGI:2145316; Txndc5.
DR VEuPathDB; HostDB:ENSMUSG00000038991; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000156920; -.
DR InParanoid; Q91W90; -.
DR OMA; TKHQTLC; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q91W90; -.
DR TreeFam; TF106379; -.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 105245; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Txndc5; mouse.
DR PRO; PR:Q91W90; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91W90; protein.
DR Bgee; ENSMUSG00000038991; Expressed in lacrimal gland and 254 other tissues.
DR ExpressionAtlas; Q91W90; baseline and differential.
DR Genevisible; Q91W90; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IGI:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Oxidoreductase; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..417
FT /note="Thioredoxin domain-containing protein 5"
FT /id="PRO_0000034184"
FT DOMAIN 35..155
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 156..281
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 289..417
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..417
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 75..78
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 203..206
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 335..338
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 171
FT /note="P -> L (in Ref. 2; AAP68841 and 3; AAH16252)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> Q (in Ref. 2; AAP68841 and 3; AAH16252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46415 MW; 0F2811DA5F5804AA CRC64;
MPPRPGRLLQ PLAGLPALAT LLLLLGARKG ARAQEVEADS GVEQDPHAKH LYTADMFTHG
IQSAAHFVMF FAPWCGHCQR LQPTWNDLGD KYNSMEDAKV YVAKVDCTAD SDVCSAQGVR
GYPTLKFFKP GQEAVKYQGP RDFETLENWM LQTLNEEPAT PEPEAEPPRA PELKQGLYEL
SANNFELHVS QGNHFIKFFA PWCGHCKALA PTWEQLALGL EHSETVKIGK VDCTQHYAVC
SEHQVRGYPT LLWFRDGKKV DQYKGKRDLE SLRDYVQSQL QGSEAAPETV EPSEAPVMAA
EPTGDKGTVL ALTEKSFEDT IAQGITFVKF YAPWCGHCKN LAPTWEELSK KEFPGLSDVT
IAEVDCTAER NVCSKYSVRG YPTLLLFRGG EKVGEHNGGR DLDSLHSFVL RQAKDEL
