TXD17_HUMAN
ID TXD17_HUMAN Reviewed; 123 AA.
AC Q9BRA2; A8K7E8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Thioredoxin domain-containing protein 17;
DE AltName: Full=14 kDa thioredoxin-related protein;
DE Short=TRP14;
DE AltName: Full=Protein 42-9-9;
DE AltName: Full=Thioredoxin-like protein 5;
GN Name=TXNDC17; Synonyms=TXNL5;
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].
RC TISSUE=Umbilical vein endothelial cell;
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP PROTEIN SEQUENCE OF 41-58, FUNCTION, MUTAGENESIS OF CYS-43 AND CYS-46,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14607844; DOI=10.1074/jbc.m307932200;
RA Jeong W., Yoon H.W., Lee S.-R., Rhee S.G.;
RT "Identification and characterization of TRP14, a thioredoxin-related
RT protein of 14 kDa. New insights into the specificity of thioredoxin
RT function.";
RL J. Biol. Chem. 279:3142-3150(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH DYNLL1.
RX PubMed=14607843; DOI=10.1074/jbc.m307959200;
RA Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.;
RT "Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-
RT alpha signaling pathways.";
RL J. Biol. Chem. 279:3151-3159(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=15355959; DOI=10.1074/jbc.m407079200;
RA Woo J.R., Kim S.J., Jeong W., Cho Y.H., Lee S.C., Chung Y.J., Rhee S.G.,
RA Ryu S.E.;
RT "Structural basis of cellular redox regulation by human TRP14.";
RL J. Biol. Chem. 279:48120-48125(2004).
CC -!- FUNCTION: Disulfide reductase. May participate in various redox
CC reactions through the reversible oxidation of its active center dithiol
CC to a disulfide and catalyze dithiol-disulfide exchange reactions.
CC Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase
CC activity and may contribute to the elimination of cellular hydrogen
CC peroxide. {ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}.
CC -!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1.
CC {ECO:0000269|PubMed:14607843}.
CC -!- INTERACTION:
CC Q9BRA2; Q96B26: EXOSC8; NbExp=6; IntAct=EBI-1055906, EBI-371922;
CC Q9BRA2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1055906, EBI-6509505;
CC Q9BRA2; Q96T51: RUFY1; NbExp=3; IntAct=EBI-1055906, EBI-3941207;
CC Q9BRA2; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1055906, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14607844}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in cell lines.
CC {ECO:0000269|PubMed:14607844}.
CC -!- PTM: The oxidized protein is reduced by TRXR1.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AJ344101; CAC51435.1; -; mRNA.
DR EMBL; AK291963; BAF84652.1; -; mRNA.
DR EMBL; CH471108; EAW90302.1; -; Genomic_DNA.
DR EMBL; BC006405; AAH06405.1; -; mRNA.
DR CCDS; CCDS11077.1; -.
DR RefSeq; NP_116120.1; NM_032731.3.
DR PDB; 1WOU; X-ray; 1.80 A; A=1-123.
DR PDBsum; 1WOU; -.
DR AlphaFoldDB; Q9BRA2; -.
DR SMR; Q9BRA2; -.
DR BioGRID; 124277; 43.
DR IntAct; Q9BRA2; 7.
DR STRING; 9606.ENSP00000250101; -.
DR ChEMBL; CHEMBL4295935; -.
DR iPTMnet; Q9BRA2; -.
DR PhosphoSitePlus; Q9BRA2; -.
DR BioMuta; TXNDC17; -.
DR DMDM; 74732856; -.
DR REPRODUCTION-2DPAGE; IPI00646689; -.
DR EPD; Q9BRA2; -.
DR jPOST; Q9BRA2; -.
DR MassIVE; Q9BRA2; -.
DR MaxQB; Q9BRA2; -.
DR PaxDb; Q9BRA2; -.
DR PeptideAtlas; Q9BRA2; -.
DR PRIDE; Q9BRA2; -.
DR ProteomicsDB; 78752; -.
DR TopDownProteomics; Q9BRA2; -.
DR Antibodypedia; 11673; 88 antibodies from 24 providers.
DR DNASU; 84817; -.
DR Ensembl; ENST00000250101.10; ENSP00000250101.5; ENSG00000129235.11.
DR GeneID; 84817; -.
DR KEGG; hsa:84817; -.
DR MANE-Select; ENST00000250101.10; ENSP00000250101.5; NM_032731.4; NP_116120.1.
DR UCSC; uc002gdf.5; human.
DR CTD; 84817; -.
DR DisGeNET; 84817; -.
DR GeneCards; TXNDC17; -.
DR HGNC; HGNC:28218; TXNDC17.
DR HPA; ENSG00000129235; Tissue enhanced (esophagus).
DR neXtProt; NX_Q9BRA2; -.
DR OpenTargets; ENSG00000129235; -.
DR PharmGKB; PA162407489; -.
DR VEuPathDB; HostDB:ENSG00000129235; -.
DR eggNOG; KOG3425; Eukaryota.
DR GeneTree; ENSGT00390000012195; -.
DR HOGENOM; CLU_120161_0_1_1; -.
DR InParanoid; Q9BRA2; -.
DR OMA; IMVVTHN; -.
DR OrthoDB; 1624076at2759; -.
DR PhylomeDB; Q9BRA2; -.
DR TreeFam; TF313854; -.
DR BRENDA; 1.8.1.6; 2681.
DR PathwayCommons; Q9BRA2; -.
DR SignaLink; Q9BRA2; -.
DR BioGRID-ORCS; 84817; 74 hits in 1086 CRISPR screens.
DR ChiTaRS; TXNDC17; human.
DR EvolutionaryTrace; Q9BRA2; -.
DR GenomeRNAi; 84817; -.
DR Pharos; Q9BRA2; Tbio.
DR PRO; PR:Q9BRA2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BRA2; protein.
DR Bgee; ENSG00000129235; Expressed in pancreatic ductal cell and 179 other tissues.
DR ExpressionAtlas; Q9BRA2; baseline and differential.
DR Genevisible; Q9BRA2; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR045108; TXNDC17-like.
DR InterPro; IPR010357; TXNDC17_dom.
DR PANTHER; PTHR12452; PTHR12452; 1.
DR Pfam; PF06110; DUF953; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..123
FT /note="Thioredoxin domain-containing protein 17"
FT /id="PRO_0000120022"
FT DOMAIN 41..123
FT /note="Thioredoxin"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:14607844"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:14607844"
FT SITE 44
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000305|PubMed:15355959"
FT SITE 45
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000305|PubMed:15355959"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT DISULFID 43..46
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:15355959"
FT MUTAGEN 43
FT /note="C->S: Loss of peroxidase activity."
FT /evidence="ECO:0000269|PubMed:14607844"
FT MUTAGEN 46
FT /note="C->S: Loss of peroxidase activity."
FT /evidence="ECO:0000269|PubMed:14607844"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1WOU"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1WOU"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1WOU"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1WOU"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1WOU"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1WOU"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1WOU"
SQ SEQUENCE 123 AA; 13941 MW; 887ADB4704946B86 CRC64;
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF
SED
