Full text data of TXNDC12
TXNDC12
(TLP19)
[Confidence: low (only semi-automatic identification from reviews)]
Thioredoxin domain-containing protein 12; 1.8.4.2 (Endoplasmic reticulum resident protein 18; ER protein 18; ERp18; Endoplasmic reticulum resident protein 19; ER protein 19; ERp19; Thioredoxin-like protein p19; hTLP19; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thioredoxin domain-containing protein 12; 1.8.4.2 (Endoplasmic reticulum resident protein 18; ER protein 18; ERp18; Endoplasmic reticulum resident protein 19; ER protein 19; ERp19; Thioredoxin-like protein p19; hTLP19; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95881
ID TXD12_HUMAN Reviewed; 172 AA.
AC O95881; B3KQS0; Q5T1T4; Q96H50;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Thioredoxin domain-containing protein 12;
DE EC=1.8.4.2;
DE AltName: Full=Endoplasmic reticulum resident protein 18;
DE Short=ER protein 18;
DE Short=ERp18;
DE AltName: Full=Endoplasmic reticulum resident protein 19;
DE Short=ER protein 19;
DE Short=ERp19;
DE AltName: Full=Thioredoxin-like protein p19;
DE AltName: Full=hTLP19;
DE Flags: Precursor;
GN Name=TXNDC12; Synonyms=TLP19; ORFNames=UNQ713/PRO1376;
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], AND TISSUE SPECIFICITY.
RX PubMed=14557066; DOI=10.1016/S0378-1119(03)00732-7;
RA Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G.;
RT "Isolation and characterization of a novel human thioredoxin-like gene
RT hTLP19 encoding a secretory protein.";
RL Gene 315:71-78(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Kidney, and Ovary;
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 [7]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF
RP CYS-66 AND CYS-69.
RX PubMed=12761212; DOI=10.1074/jbc.M304598200;
RA Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P.,
RA Rautio S.M., Kellokumpu S., Ruddock L.W.;
RT "Functional characterization of ERp18, a new endoplasmic reticulum-
RT located thioredoxin superfamily member.";
RL J. Biol. Chem. 278:28912-28920(2003).
RN [9]
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 [10]
RP STRUCTURE BY NMR OF 24-172, AND DISULFIDE BOND.
RX PubMed=19361226; DOI=10.1021/bi9003342;
RA Rowe M.L., Ruddock L.W., Kelly G., Schmidt J.M., Williamson R.A.,
RA Howard M.J.;
RT "Solution structure and dynamics of ERp18, a small endoplasmic
RT reticulum resident oxidoreductase.";
RL Biochemistry 48:4596-4606(2009).
CC -!- FUNCTION: Possesses significant protein thiol-disulfide oxidase
CC activity.
CC -!- CATALYTIC ACTIVITY: 2 glutathione + protein-disulfide =
CC glutathione disulfide + protein-dithiol.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn;
CC pH dependence:
CC Optimum pH is 6.5;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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; AF543416; AAN34781.1; -; mRNA.
DR EMBL; AF131758; AAD20035.1; -; mRNA.
DR EMBL; AY358982; AAQ89341.1; -; mRNA.
DR EMBL; AK075409; BAG52132.1; -; mRNA.
DR EMBL; AL445685; CAI17031.1; -; Genomic_DNA.
DR EMBL; BC001493; AAH01493.1; -; mRNA.
DR EMBL; BC008953; AAH08953.1; -; mRNA.
DR EMBL; BC008913; AAH08913.1; -; mRNA.
DR RefSeq; NP_056997.1; NM_015913.3.
DR UniGene; Hs.476033; -.
DR PDB; 1SEN; X-ray; 1.20 A; A=23-172.
DR PDB; 2K8V; NMR; -; A=24-172.
DR PDBsum; 1SEN; -.
DR PDBsum; 2K8V; -.
DR ProteinModelPortal; O95881; -.
DR SMR; O95881; 24-172.
DR IntAct; O95881; 1.
DR MINT; MINT-5005906; -.
DR STRING; 9606.ENSP00000360688; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; O95881; -.
DR PaxDb; O95881; -.
DR PeptideAtlas; O95881; -.
DR PRIDE; O95881; -.
DR DNASU; 51060; -.
DR Ensembl; ENST00000371626; ENSP00000360688; ENSG00000117862.
DR GeneID; 51060; -.
DR KEGG; hsa:51060; -.
DR UCSC; uc001cti.4; human.
DR CTD; 51060; -.
DR GeneCards; GC01M052485; -.
DR H-InvDB; HIX0116253; -.
DR HGNC; HGNC:24626; TXNDC12.
DR HPA; HPA015086; -.
DR MIM; 609448; gene.
DR neXtProt; NX_O95881; -.
DR PharmGKB; PA142670665; -.
DR eggNOG; NOG77442; -.
DR HOGENOM; HOG000231100; -.
DR HOVERGEN; HBG107174; -.
DR InParanoid; O95881; -.
DR KO; K05360; -.
DR OMA; SYKYFYT; -.
DR OrthoDB; EOG7DNNX2; -.
DR PhylomeDB; O95881; -.
DR ChiTaRS; TXNDC12; human.
DR EvolutionaryTrace; O95881; -.
DR GeneWiki; TXNDC12; -.
DR GenomeRNAi; 51060; -.
DR NextBio; 53641; -.
DR PRO; PR:O95881; -.
DR Bgee; O95881; -.
DR CleanEx; HS_TXNDC12; -.
DR Genevestigator; O95881; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1 26
FT CHAIN 27 172 Thioredoxin domain-containing protein 12.
FT /FTId=PRO_0000034189.
FT MOTIF 169 172 Prevents secretion from ER (Potential).
FT DISULFID 66 69 Redox-active.
FT MUTAGEN 66 66 C->S: Loss of oxidase activity.
FT MUTAGEN 69 69 C->S: Loss of oxidase activity.
FT CONFLICT 102 102 D -> H (in Ref. 6; AAH08913).
FT STRAND 33 38
FT HELIX 43 53
FT STRAND 57 62
FT HELIX 67 77
FT HELIX 80 86
FT STRAND 89 95
FT HELIX 96 98
FT HELIX 103 105
FT STRAND 112 118
FT TURN 120 122
FT TURN 135 139
FT HELIX 144 158
FT HELIX 159 161
SQ SEQUENCE 172 AA; 19206 MW; 3092E9515A7C4094 CRC64;
METRPRLGAT CLLGFSFLLL VISSDGHNGL GKGFGDHIHW RTLEDGKKEA AASGLPLMVI
IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP KDEDFSPDGG YIPRILFLDP
SGKVHPEIIN ENGNPSYKYF YVSAEQVVQG MKEAQERLTG DAFRKKHLED EL
//
ID TXD12_HUMAN Reviewed; 172 AA.
AC O95881; B3KQS0; Q5T1T4; Q96H50;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Thioredoxin domain-containing protein 12;
DE EC=1.8.4.2;
DE AltName: Full=Endoplasmic reticulum resident protein 18;
DE Short=ER protein 18;
DE Short=ERp18;
DE AltName: Full=Endoplasmic reticulum resident protein 19;
DE Short=ER protein 19;
DE Short=ERp19;
DE AltName: Full=Thioredoxin-like protein p19;
DE AltName: Full=hTLP19;
DE Flags: Precursor;
GN Name=TXNDC12; Synonyms=TLP19; ORFNames=UNQ713/PRO1376;
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], AND TISSUE SPECIFICITY.
RX PubMed=14557066; DOI=10.1016/S0378-1119(03)00732-7;
RA Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G.;
RT "Isolation and characterization of a novel human thioredoxin-like gene
RT hTLP19 encoding a secretory protein.";
RL Gene 315:71-78(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Kidney, and Ovary;
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 [7]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF
RP CYS-66 AND CYS-69.
RX PubMed=12761212; DOI=10.1074/jbc.M304598200;
RA Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P.,
RA Rautio S.M., Kellokumpu S., Ruddock L.W.;
RT "Functional characterization of ERp18, a new endoplasmic reticulum-
RT located thioredoxin superfamily member.";
RL J. Biol. Chem. 278:28912-28920(2003).
RN [9]
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 [10]
RP STRUCTURE BY NMR OF 24-172, AND DISULFIDE BOND.
RX PubMed=19361226; DOI=10.1021/bi9003342;
RA Rowe M.L., Ruddock L.W., Kelly G., Schmidt J.M., Williamson R.A.,
RA Howard M.J.;
RT "Solution structure and dynamics of ERp18, a small endoplasmic
RT reticulum resident oxidoreductase.";
RL Biochemistry 48:4596-4606(2009).
CC -!- FUNCTION: Possesses significant protein thiol-disulfide oxidase
CC activity.
CC -!- CATALYTIC ACTIVITY: 2 glutathione + protein-disulfide =
CC glutathione disulfide + protein-dithiol.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn;
CC pH dependence:
CC Optimum pH is 6.5;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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; AF543416; AAN34781.1; -; mRNA.
DR EMBL; AF131758; AAD20035.1; -; mRNA.
DR EMBL; AY358982; AAQ89341.1; -; mRNA.
DR EMBL; AK075409; BAG52132.1; -; mRNA.
DR EMBL; AL445685; CAI17031.1; -; Genomic_DNA.
DR EMBL; BC001493; AAH01493.1; -; mRNA.
DR EMBL; BC008953; AAH08953.1; -; mRNA.
DR EMBL; BC008913; AAH08913.1; -; mRNA.
DR RefSeq; NP_056997.1; NM_015913.3.
DR UniGene; Hs.476033; -.
DR PDB; 1SEN; X-ray; 1.20 A; A=23-172.
DR PDB; 2K8V; NMR; -; A=24-172.
DR PDBsum; 1SEN; -.
DR PDBsum; 2K8V; -.
DR ProteinModelPortal; O95881; -.
DR SMR; O95881; 24-172.
DR IntAct; O95881; 1.
DR MINT; MINT-5005906; -.
DR STRING; 9606.ENSP00000360688; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; O95881; -.
DR PaxDb; O95881; -.
DR PeptideAtlas; O95881; -.
DR PRIDE; O95881; -.
DR DNASU; 51060; -.
DR Ensembl; ENST00000371626; ENSP00000360688; ENSG00000117862.
DR GeneID; 51060; -.
DR KEGG; hsa:51060; -.
DR UCSC; uc001cti.4; human.
DR CTD; 51060; -.
DR GeneCards; GC01M052485; -.
DR H-InvDB; HIX0116253; -.
DR HGNC; HGNC:24626; TXNDC12.
DR HPA; HPA015086; -.
DR MIM; 609448; gene.
DR neXtProt; NX_O95881; -.
DR PharmGKB; PA142670665; -.
DR eggNOG; NOG77442; -.
DR HOGENOM; HOG000231100; -.
DR HOVERGEN; HBG107174; -.
DR InParanoid; O95881; -.
DR KO; K05360; -.
DR OMA; SYKYFYT; -.
DR OrthoDB; EOG7DNNX2; -.
DR PhylomeDB; O95881; -.
DR ChiTaRS; TXNDC12; human.
DR EvolutionaryTrace; O95881; -.
DR GeneWiki; TXNDC12; -.
DR GenomeRNAi; 51060; -.
DR NextBio; 53641; -.
DR PRO; PR:O95881; -.
DR Bgee; O95881; -.
DR CleanEx; HS_TXNDC12; -.
DR Genevestigator; O95881; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1 26
FT CHAIN 27 172 Thioredoxin domain-containing protein 12.
FT /FTId=PRO_0000034189.
FT MOTIF 169 172 Prevents secretion from ER (Potential).
FT DISULFID 66 69 Redox-active.
FT MUTAGEN 66 66 C->S: Loss of oxidase activity.
FT MUTAGEN 69 69 C->S: Loss of oxidase activity.
FT CONFLICT 102 102 D -> H (in Ref. 6; AAH08913).
FT STRAND 33 38
FT HELIX 43 53
FT STRAND 57 62
FT HELIX 67 77
FT HELIX 80 86
FT STRAND 89 95
FT HELIX 96 98
FT HELIX 103 105
FT STRAND 112 118
FT TURN 120 122
FT TURN 135 139
FT HELIX 144 158
FT HELIX 159 161
SQ SEQUENCE 172 AA; 19206 MW; 3092E9515A7C4094 CRC64;
METRPRLGAT CLLGFSFLLL VISSDGHNGL GKGFGDHIHW RTLEDGKKEA AASGLPLMVI
IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP KDEDFSPDGG YIPRILFLDP
SGKVHPEIIN ENGNPSYKYF YVSAEQVVQG MKEAQERLTG DAFRKKHLED EL
//
MIM
609448
*RECORD*
*FIELD* NO
609448
*FIELD* TI
*609448 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 12; TXNDC12
;;THIOREDOXIN-LIKE PROTEIN p19; TLP19;;
read moreENDOPLASMIC RETICULUM PROTEIN, 18-KD; ERP18;;
ANTERIOR GRADIENT 1, XENOPUS, HOMOLOG OF; AGR1
*FIELD* TX
DESCRIPTION
TXNDC12 belongs to the thioredoxin superfamily (see TXN; 187700).
Members of this superfamily possess a thioredoxin fold with a consensus
active-site sequence (CxxC) and have roles in redox regulation, defense
against oxidative stress, refolding of disulfide-containing proteins,
and regulation of transcription factors (Liu et al., 2003).
CLONING
By searching genomic and EST databases for putative secretory proteins,
followed by RT-PCR of human liver RNA, Liu et al. (2003) cloned TXNDC12,
which they called TLP19. The transcript contains 2 putative poly(A)
signals in its 3-prime UTR. The deduced 172-amino acid protein has a
calculated molecular mass of 19.2 kD. TLP19 has an N-terminal signal
peptide and a central thioredoxin-like domain containing the consensus
active-site motif. Northern blot analysis detected a 1.6-kb TLP19
transcript in all tissues examined, with highest expression in placenta
and liver. Placenta also expressed a 1.2-kb TLP19 transcript.
Epitope-tagged TLP19 was expressed in the Golgi apparatus of transiently
transfected COS-7 cells, and it was secreted into the culture medium.
Alanen et al. (2003) cloned TXNDC12, which they called ERP18, from a
liver cDNA library. They identified a putative C-terminal endoplasmic
reticulum (ER) retention signal (EDEL) within the deduced protein.
Alanen et al. (2003) also noted that the active-site motif of ERP18
(CGAC) is unlike the catalytic motifs of other thioredoxin superfamily
members, including thioredoxins, isomerases, and oxidating enzymes. The
overall structure of the ERP18 catalytic domain most strongly resembles
those of protein disulfide isomerases (PDI; see 176790). In contrast to
the findings of Liu et al. (2003), Alanen et al. (2003) found that
fluorescence-tagged ERP18 was retained in the ER of transfected COS-7
cells, and the staining did not overlap that of a Golgi marker.
BIOCHEMICAL FEATURES
From circular dichroism and NMR measurements, Alanen et al. (2003)
determined that ERP18 undergoes only a minor conformational change upon
dithiol-disulfide exchange in the active site. Guanidinium chloride
denaturation curves indicated that the reduced form of the protein is
more stable than the oxidized form, suggesting that ERP18 is involved in
disulfide bond formation.
GENE FUNCTION
Liu et al. (2003) found that recombinant TLP19 without the signal
peptide showed reducing activity against an insulin-disulfide substrate.
Alanen et al. (2003) found that ERP18 showed significant peptide
thiol-disulfide oxidase activity in vitro, and the activity was
dependent on the presence of both active-site cysteines. The activity
differed from that of the human PDI family in that it was limited by
substrate oxidation and not by enzyme reoxidation.
GENE STRUCTURE
Liu et al. (2003) determined that the TLP19 gene contains 7 exons and
spans more than 35 kb.
MAPPING
By genomic sequence analysis, Liu et al. (2003) mapped the TLP19 gene to
chromosome 1p32.3.
*FIELD* RF
1. Alanen, H. I.; Williamson, R. A.; Howard, M. J.; Lappi, A.-K.;
Jantti, H. P.; Rautio, S. M.; Kellokumpu, S.; Ruddock, L. W.: Functional
characterization of ERp18, a new endoplasmic reticulum-located thioredoxin
superfamily member. J. Biol. Chem. 278: 28912-28920, 2003.
2. Liu, F.; Rong, Y.-P.; Zeng, L.-C.; Zhang, X.; Han, Z.-G.: Isolation
and characterization of a novel human thioredoxin-like gene hTLP19
encoding a secretory protein. Gene 315: 71-78, 2003.
*FIELD* CD
Patricia A. Hartz: 6/28/2005
*FIELD* ED
alopez: 09/09/2008
mgross: 6/28/2005
*RECORD*
*FIELD* NO
609448
*FIELD* TI
*609448 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 12; TXNDC12
;;THIOREDOXIN-LIKE PROTEIN p19; TLP19;;
read moreENDOPLASMIC RETICULUM PROTEIN, 18-KD; ERP18;;
ANTERIOR GRADIENT 1, XENOPUS, HOMOLOG OF; AGR1
*FIELD* TX
DESCRIPTION
TXNDC12 belongs to the thioredoxin superfamily (see TXN; 187700).
Members of this superfamily possess a thioredoxin fold with a consensus
active-site sequence (CxxC) and have roles in redox regulation, defense
against oxidative stress, refolding of disulfide-containing proteins,
and regulation of transcription factors (Liu et al., 2003).
CLONING
By searching genomic and EST databases for putative secretory proteins,
followed by RT-PCR of human liver RNA, Liu et al. (2003) cloned TXNDC12,
which they called TLP19. The transcript contains 2 putative poly(A)
signals in its 3-prime UTR. The deduced 172-amino acid protein has a
calculated molecular mass of 19.2 kD. TLP19 has an N-terminal signal
peptide and a central thioredoxin-like domain containing the consensus
active-site motif. Northern blot analysis detected a 1.6-kb TLP19
transcript in all tissues examined, with highest expression in placenta
and liver. Placenta also expressed a 1.2-kb TLP19 transcript.
Epitope-tagged TLP19 was expressed in the Golgi apparatus of transiently
transfected COS-7 cells, and it was secreted into the culture medium.
Alanen et al. (2003) cloned TXNDC12, which they called ERP18, from a
liver cDNA library. They identified a putative C-terminal endoplasmic
reticulum (ER) retention signal (EDEL) within the deduced protein.
Alanen et al. (2003) also noted that the active-site motif of ERP18
(CGAC) is unlike the catalytic motifs of other thioredoxin superfamily
members, including thioredoxins, isomerases, and oxidating enzymes. The
overall structure of the ERP18 catalytic domain most strongly resembles
those of protein disulfide isomerases (PDI; see 176790). In contrast to
the findings of Liu et al. (2003), Alanen et al. (2003) found that
fluorescence-tagged ERP18 was retained in the ER of transfected COS-7
cells, and the staining did not overlap that of a Golgi marker.
BIOCHEMICAL FEATURES
From circular dichroism and NMR measurements, Alanen et al. (2003)
determined that ERP18 undergoes only a minor conformational change upon
dithiol-disulfide exchange in the active site. Guanidinium chloride
denaturation curves indicated that the reduced form of the protein is
more stable than the oxidized form, suggesting that ERP18 is involved in
disulfide bond formation.
GENE FUNCTION
Liu et al. (2003) found that recombinant TLP19 without the signal
peptide showed reducing activity against an insulin-disulfide substrate.
Alanen et al. (2003) found that ERP18 showed significant peptide
thiol-disulfide oxidase activity in vitro, and the activity was
dependent on the presence of both active-site cysteines. The activity
differed from that of the human PDI family in that it was limited by
substrate oxidation and not by enzyme reoxidation.
GENE STRUCTURE
Liu et al. (2003) determined that the TLP19 gene contains 7 exons and
spans more than 35 kb.
MAPPING
By genomic sequence analysis, Liu et al. (2003) mapped the TLP19 gene to
chromosome 1p32.3.
*FIELD* RF
1. Alanen, H. I.; Williamson, R. A.; Howard, M. J.; Lappi, A.-K.;
Jantti, H. P.; Rautio, S. M.; Kellokumpu, S.; Ruddock, L. W.: Functional
characterization of ERp18, a new endoplasmic reticulum-located thioredoxin
superfamily member. J. Biol. Chem. 278: 28912-28920, 2003.
2. Liu, F.; Rong, Y.-P.; Zeng, L.-C.; Zhang, X.; Han, Z.-G.: Isolation
and characterization of a novel human thioredoxin-like gene hTLP19
encoding a secretory protein. Gene 315: 71-78, 2003.
*FIELD* CD
Patricia A. Hartz: 6/28/2005
*FIELD* ED
alopez: 09/09/2008
mgross: 6/28/2005