Full text data of TXNDC17
TXNDC17
(TXNL5)
[Confidence: low (only semi-automatic identification from reviews)]
Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein; TRP14; Protein 42-9-9; Thioredoxin-like protein 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein; TRP14; Protein 42-9-9; Thioredoxin-like protein 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRA2
ID TXD17_HUMAN Reviewed; 123 AA.
AC Q9BRA2; A8K7E8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT factor-alpha signaling pathways.";
RL J. Biol. Chem. 279:3151-3159(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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.,
RA Rhee S.G., 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
CC dithiol to a disulfide and catalyze dithiol-disulfide exchange
CC reactions. Modulates TNF-alpha signaling and NF-kappa-B
CC activation. Has peroxidase activity and may contribute to the
CC elimination of cellular hydrogen peroxide.
CC -!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in cell lines.
CC -!- PTM: The oxidized protein is reduced by TRXR1.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_116120.1; NM_032731.3.
DR UniGene; Hs.408236; -.
DR PDB; 1WOU; X-ray; 1.80 A; A=1-123.
DR PDBsum; 1WOU; -.
DR ProteinModelPortal; Q9BRA2; -.
DR SMR; Q9BRA2; 4-122.
DR STRING; 9606.ENSP00000250101; -.
DR PhosphoSite; Q9BRA2; -.
DR DMDM; 74732856; -.
DR REPRODUCTION-2DPAGE; IPI00646689; -.
DR PaxDb; Q9BRA2; -.
DR PRIDE; Q9BRA2; -.
DR Ensembl; ENST00000250101; ENSP00000250101; ENSG00000129235.
DR GeneID; 84817; -.
DR KEGG; hsa:84817; -.
DR UCSC; uc002gdf.4; human.
DR CTD; 84817; -.
DR GeneCards; GC17P006486; -.
DR HGNC; HGNC:28218; TXNDC17.
DR HPA; HPA022931; -.
DR neXtProt; NX_Q9BRA2; -.
DR PharmGKB; PA162407489; -.
DR eggNOG; NOG285127; -.
DR HOGENOM; HOG000241811; -.
DR HOVERGEN; HBG079628; -.
DR InParanoid; Q9BRA2; -.
DR OMA; SGFEEFN; -.
DR OrthoDB; EOG70CR8Q; -.
DR PhylomeDB; Q9BRA2; -.
DR EvolutionaryTrace; Q9BRA2; -.
DR GenomeRNAi; 84817; -.
DR NextBio; 75010; -.
DR PRO; PR:Q9BRA2; -.
DR ArrayExpress; Q9BRA2; -.
DR Bgee; Q9BRA2; -.
DR CleanEx; HS_TXNDC17; -.
DR Genevestigator; Q9BRA2; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0047134; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010357; DUF953_thioredox.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR12452; PTHR12452; 1.
DR Pfam; PF06110; DUF953; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Redox-active center;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 123 Thioredoxin domain-containing protein 17.
FT /FTId=PRO_0000120022.
FT DOMAIN 41 123 Thioredoxin.
FT ACT_SITE 43 43 Nucleophile.
FT ACT_SITE 46 46 Nucleophile.
FT SITE 44 44 Contributes to redox potential value.
FT SITE 45 45 Contributes to redox potential value.
FT MOD_RES 2 2 N-acetylalanine.
FT DISULFID 43 46 Redox-active.
FT MUTAGEN 43 43 C->S: Loss of peroxidase activity.
FT MUTAGEN 46 46 C->S: Loss of peroxidase activity.
FT STRAND 5 11
FT HELIX 12 20
FT TURN 21 24
FT STRAND 25 32
FT HELIX 44 56
FT HELIX 57 59
FT STRAND 64 70
FT HELIX 74 78
FT HELIX 83 88
FT STRAND 92 98
FT STRAND 104 106
FT HELIX 107 111
FT HELIX 113 121
SQ SEQUENCE 123 AA; 13941 MW; 887ADB4704946B86 CRC64;
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF
SED
//
ID TXD17_HUMAN Reviewed; 123 AA.
AC Q9BRA2; A8K7E8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT factor-alpha signaling pathways.";
RL J. Biol. Chem. 279:3151-3159(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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.,
RA Rhee S.G., 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
CC dithiol to a disulfide and catalyze dithiol-disulfide exchange
CC reactions. Modulates TNF-alpha signaling and NF-kappa-B
CC activation. Has peroxidase activity and may contribute to the
CC elimination of cellular hydrogen peroxide.
CC -!- SUBUNIT: Interacts with TRXR1 and DYNLL1/DNCL1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in cell lines.
CC -!- PTM: The oxidized protein is reduced by TRXR1.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_116120.1; NM_032731.3.
DR UniGene; Hs.408236; -.
DR PDB; 1WOU; X-ray; 1.80 A; A=1-123.
DR PDBsum; 1WOU; -.
DR ProteinModelPortal; Q9BRA2; -.
DR SMR; Q9BRA2; 4-122.
DR STRING; 9606.ENSP00000250101; -.
DR PhosphoSite; Q9BRA2; -.
DR DMDM; 74732856; -.
DR REPRODUCTION-2DPAGE; IPI00646689; -.
DR PaxDb; Q9BRA2; -.
DR PRIDE; Q9BRA2; -.
DR Ensembl; ENST00000250101; ENSP00000250101; ENSG00000129235.
DR GeneID; 84817; -.
DR KEGG; hsa:84817; -.
DR UCSC; uc002gdf.4; human.
DR CTD; 84817; -.
DR GeneCards; GC17P006486; -.
DR HGNC; HGNC:28218; TXNDC17.
DR HPA; HPA022931; -.
DR neXtProt; NX_Q9BRA2; -.
DR PharmGKB; PA162407489; -.
DR eggNOG; NOG285127; -.
DR HOGENOM; HOG000241811; -.
DR HOVERGEN; HBG079628; -.
DR InParanoid; Q9BRA2; -.
DR OMA; SGFEEFN; -.
DR OrthoDB; EOG70CR8Q; -.
DR PhylomeDB; Q9BRA2; -.
DR EvolutionaryTrace; Q9BRA2; -.
DR GenomeRNAi; 84817; -.
DR NextBio; 75010; -.
DR PRO; PR:Q9BRA2; -.
DR ArrayExpress; Q9BRA2; -.
DR Bgee; Q9BRA2; -.
DR CleanEx; HS_TXNDC17; -.
DR Genevestigator; Q9BRA2; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0047134; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010357; DUF953_thioredox.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR12452; PTHR12452; 1.
DR Pfam; PF06110; DUF953; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
DR PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Redox-active center;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 123 Thioredoxin domain-containing protein 17.
FT /FTId=PRO_0000120022.
FT DOMAIN 41 123 Thioredoxin.
FT ACT_SITE 43 43 Nucleophile.
FT ACT_SITE 46 46 Nucleophile.
FT SITE 44 44 Contributes to redox potential value.
FT SITE 45 45 Contributes to redox potential value.
FT MOD_RES 2 2 N-acetylalanine.
FT DISULFID 43 46 Redox-active.
FT MUTAGEN 43 43 C->S: Loss of peroxidase activity.
FT MUTAGEN 46 46 C->S: Loss of peroxidase activity.
FT STRAND 5 11
FT HELIX 12 20
FT TURN 21 24
FT STRAND 25 32
FT HELIX 44 56
FT HELIX 57 59
FT STRAND 64 70
FT HELIX 74 78
FT HELIX 83 88
FT STRAND 92 98
FT STRAND 104 106
FT HELIX 107 111
FT HELIX 113 121
SQ SEQUENCE 123 AA; 13941 MW; 887ADB4704946B86 CRC64;
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF
SED
//