ID TXD12_HUMAN Reviewed; 172 AA. AC O95881; Q5T1T4; Q96H50; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 07-JUL-2009, entry version 79. DE RecName: Full=Thioredoxin domain-containing protein 12; DE EC=1.8.4.2; DE AltName: Full=Thioredoxin-like protein p19; DE AltName: Full=Endoplasmic reticulum protein ERp19; DE AltName: Full=ERp18; 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 MEDLINE=22919389; 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 MEDLINE=22887296; 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 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 [5] 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 [6] 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 [7] 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 [8] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. 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; AL445685; CAI17031.1; -; Genomic_DNA. DR EMBL; BC001493; AAH01493.1; -; mRNA. DR EMBL; BC008953; AAH08953.1; -; mRNA. DR EMBL; BC008913; AAH08913.1; -; mRNA. DR IPI; IPI00026328; -. DR RefSeq; NP_056997.1; -. DR UniGene; Hs.476033; -. DR PDB; 1SEN; X-ray; 1.20 A; A=23-172. DR PDBsum; 1SEN; -. DR SMR; O95881; 30-163. DR PeptideAtlas; O95881; -. DR PRIDE; O95881; -. DR Ensembl; ENSG00000117862; Homo sapiens. DR GeneID; 51060; -. DR KEGG; hsa:51060; -. DR UCSC; uc001cti.1; human. DR GeneCards; GC01M052199; -. DR H-InvDB; HIX0000579; -. DR H-InvDB; HIX0029114; -. DR HGNC; HGNC:24626; TXNDC12. DR MIM; 609448; gene. DR PharmGKB; PA142670665; -. DR HOGENOM; O95881; -. DR HOVERGEN; O95881; -. DR OMA; O95881; CHACKAL. DR BRENDA; 1.8.4.2; 247. DR DrugBank; DB00143; Glutathione. DR NextBio; 53641; -. DR ArrayExpress; O95881; -. DR Bgee; O95881; -. DR CleanEx; HS_TXNDC12; -. DR GermOnline; ENSG00000117862; Homo sapiens. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) a...; IEA:EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR017936; Thioredoxin-like. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 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; 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. 5; AAH08913). 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 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 //