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Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein) (TRP14) (Protein 42-9-9) (Thioredoxin-like protein 5)

 TXD17_HUMAN             Reviewed;         123 AA.
Q9BRA2; A8K7E8;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=Thioredoxin domain-containing protein 17;
AltName: Full=14 kDa thioredoxin-related protein;
Short=TRP14;
AltName: Full=Protein 42-9-9;
AltName: Full=Thioredoxin-like protein 5;
Name=TXNDC17; Synonyms=TXNL5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Umbilical vein endothelial cell;
Schmidt T.;
Thesis (2001), University of Goettingen, Germany.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 41-58, FUNCTION, MUTAGENESIS OF CYS-43 AND CYS-46,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=14607844; DOI=10.1074/jbc.M307932200;
Jeong W., Yoon H.W., Lee S.-R., Rhee S.G.;
"Identification and characterization of TRP14, a thioredoxin-related
protein of 14 kDa. New insights into the specificity of thioredoxin
function.";
J. Biol. Chem. 279:3142-3150(2004).
[6]
FUNCTION, AND INTERACTION WITH DYNLL1.
PubMed=14607843; DOI=10.1074/jbc.M307959200;
Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.;
"Roles of TRP14, a thioredoxin-related protein in tumor necrosis
factor-alpha signaling pathways.";
J. Biol. Chem. 279:3151-3159(2004).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BOND.
PubMed=15355959; DOI=10.1074/jbc.M407079200;
Woo J.R., Kim S.J., Jeong W., Cho Y.H., Lee S.C., Chung Y.J.,
Rhee S.G., Ryu S.E.;
"Structural basis of cellular redox regulation by human TRP14.";
J. Biol. Chem. 279:48120-48125(2004).
-!- FUNCTION: Disulfide reductase. May participate in various redox
reactions through the reversible oxidation of its active center
dithiol to a disulfide and catalyze dithiol-disulfide exchange
reactions. Modulates TNF-alpha signaling and NF-kappa-B
activation. Has peroxidase activity and may contribute to the
elimination of cellular hydrogen peroxide.
{ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}.
-!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1.
{ECO:0000269|PubMed:14607843}.
-!- INTERACTION:
Q96B26:EXOSC8; NbExp=5; IntAct=EBI-1055906, EBI-371922;
Q96T51:RUFY1; NbExp=3; IntAct=EBI-1055906, EBI-3941207;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-1055906, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14607844}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in cell lines.
{ECO:0000269|PubMed:14607844}.
-!- PTM: The oxidized protein is reduced by TRXR1.
-!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ344101; CAC51435.1; -; mRNA.
EMBL; AK291963; BAF84652.1; -; mRNA.
EMBL; CH471108; EAW90302.1; -; Genomic_DNA.
EMBL; BC006405; AAH06405.1; -; mRNA.
CCDS; CCDS11077.1; -.
RefSeq; NP_116120.1; NM_032731.3.
UniGene; Hs.408236; -.
PDB; 1WOU; X-ray; 1.80 A; A=1-123.
PDBsum; 1WOU; -.
ProteinModelPortal; Q9BRA2; -.
SMR; Q9BRA2; -.
BioGrid; 124277; 31.
IntAct; Q9BRA2; 6.
STRING; 9606.ENSP00000250101; -.
iPTMnet; Q9BRA2; -.
PhosphoSitePlus; Q9BRA2; -.
BioMuta; TXNDC17; -.
DMDM; 74732856; -.
REPRODUCTION-2DPAGE; IPI00646689; -.
EPD; Q9BRA2; -.
MaxQB; Q9BRA2; -.
PaxDb; Q9BRA2; -.
PeptideAtlas; Q9BRA2; -.
PRIDE; Q9BRA2; -.
TopDownProteomics; Q9BRA2; -.
Ensembl; ENST00000250101; ENSP00000250101; ENSG00000129235.
GeneID; 84817; -.
KEGG; hsa:84817; -.
UCSC; uc002gdf.5; human.
CTD; 84817; -.
DisGeNET; 84817; -.
EuPathDB; HostDB:ENSG00000129235.10; -.
GeneCards; TXNDC17; -.
HGNC; HGNC:28218; TXNDC17.
HPA; HPA022931; -.
neXtProt; NX_Q9BRA2; -.
OpenTargets; ENSG00000129235; -.
PharmGKB; PA162407489; -.
eggNOG; KOG3425; Eukaryota.
eggNOG; ENOG4111Q2V; LUCA.
GeneTree; ENSGT00390000012195; -.
HOGENOM; HOG000241811; -.
HOVERGEN; HBG079628; -.
InParanoid; Q9BRA2; -.
OMA; GESWCPY; -.
OrthoDB; EOG091G0VBT; -.
PhylomeDB; Q9BRA2; -.
TreeFam; TF313854; -.
EvolutionaryTrace; Q9BRA2; -.
GenomeRNAi; 84817; -.
PRO; PR:Q9BRA2; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000129235; -.
CleanEx; HS_TXNDC17; -.
ExpressionAtlas; Q9BRA2; baseline and differential.
Genevisible; Q9BRA2; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO; GO:0047134; F:protein-disulfide reductase activity; IDA:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
InterPro; IPR010357; DUF953_thioredox.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR12452; PTHR12452; 1.
Pfam; PF06110; DUF953; 1.
SUPFAM; SSF52833; SSF52833; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Redox-active center;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 123 Thioredoxin domain-containing protein 17.
/FTId=PRO_0000120022.
DOMAIN 41 123 Thioredoxin. {ECO:0000255}.
ACT_SITE 43 43 Nucleophile.
{ECO:0000269|PubMed:14607844}.
ACT_SITE 46 46 Nucleophile.
{ECO:0000269|PubMed:14607844}.
SITE 44 44 Contributes to redox potential value.
{ECO:0000305|PubMed:15355959}.
SITE 45 45 Contributes to redox potential value.
{ECO:0000305|PubMed:15355959}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
DISULFID 43 46 Redox-active.
{ECO:0000269|PubMed:15355959}.
MUTAGEN 43 43 C->S: Loss of peroxidase activity.
{ECO:0000269|PubMed:14607844}.
MUTAGEN 46 46 C->S: Loss of peroxidase activity.
{ECO:0000269|PubMed:14607844}.
STRAND 5 11 {ECO:0000244|PDB:1WOU}.
HELIX 12 20 {ECO:0000244|PDB:1WOU}.
TURN 21 24 {ECO:0000244|PDB:1WOU}.
STRAND 25 32 {ECO:0000244|PDB:1WOU}.
HELIX 44 56 {ECO:0000244|PDB:1WOU}.
HELIX 57 59 {ECO:0000244|PDB:1WOU}.
STRAND 64 70 {ECO:0000244|PDB:1WOU}.
HELIX 74 78 {ECO:0000244|PDB:1WOU}.
HELIX 83 88 {ECO:0000244|PDB:1WOU}.
STRAND 92 98 {ECO:0000244|PDB:1WOU}.
STRAND 104 106 {ECO:0000244|PDB:1WOU}.
HELIX 107 111 {ECO:0000244|PDB:1WOU}.
HELIX 113 121 {ECO:0000244|PDB:1WOU}.
SEQUENCE 123 AA; 13941 MW; 887ADB4704946B86 CRC64;
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF
SED


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