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O95881 (TXD12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin domain-containing protein 12

EC=1.8.4.2
Alternative name(s):
Endoplasmic reticulum resident protein 18
Short name=ER protein 18
Short name=ERp18
Endoplasmic reticulum resident protein 19
Short name=ER protein 19
Short name=ERp19
Thioredoxin-like protein p19
hTLP19
Gene names
Name:TXNDC12
Synonyms:TLP19
ORF Names:UNQ713/PRO1376
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses significant protein thiol-disulfide oxidase activity. Ref.8

Catalytic activity

2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.

Subcellular location

Endoplasmic reticulum lumen Ref.8.

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Contains 1 thioredoxin domain.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn

pH dependence:

Optimum pH is 6.5.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRedox-active center
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-disulfide reductase (glutathione) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.7
Chain27 – 172146Thioredoxin domain-containing protein 12
PRO_0000034189

Regions

Motif169 – 1724Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond66 ↔ 69Redox-active Ref.8 Ref.10

Experimental info

Mutagenesis661C → S: Loss of oxidase activity. Ref.8
Mutagenesis691C → S: Loss of oxidase activity. Ref.8
Sequence conflict1021D → H in AAH08913. Ref.6

Secondary structure

......................... 172
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95881 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3092E9515A7C4094

FASTA17219,206
        10         20         30         40         50         60 
METRPRLGAT CLLGFSFLLL VISSDGHNGL GKGFGDHIHW RTLEDGKKEA AASGLPLMVI 

        70         80         90        100        110        120 
IHKSWCGACK ALKPKFAEST EISELSHNFV MVNLEDEEEP KDEDFSPDGG YIPRILFLDP 

       130        140        150        160        170 
SGKVHPEIIN ENGNPSYKYF YVSAEQVVQG MKEAQERLTG DAFRKKHLED EL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein."
Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G.
Gene 315:71-78(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]Mei G., Yu W., Gibbs R.A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon, Kidney and Ovary.
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41.
[8]"Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member."
Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P., Rautio S.M., Kellokumpu S., Ruddock L.W.
J. Biol. Chem. 278:28912-28920(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-66 AND CYS-69.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Solution structure and dynamics of ERp18, a small endoplasmic reticulum resident oxidoreductase."
Rowe M.L., Ruddock L.W., Kelly G., Schmidt J.M., Williamson R.A., Howard M.J.
Biochemistry 48:4596-4606(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-172, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF543416 mRNA. Translation: AAN34781.1.
AF131758 mRNA. Translation: AAD20035.1.
AY358982 mRNA. Translation: AAQ89341.1.
AK075409 mRNA. Translation: BAG52132.1.
AL445685 Genomic DNA. Translation: CAI17031.1.
BC001493 mRNA. Translation: AAH01493.1.
BC008953 mRNA. Translation: AAH08953.1.
BC008913 mRNA. Translation: AAH08913.1.
RefSeqNP_056997.1. NM_015913.3.
UniGeneHs.476033.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SENX-ray1.20A23-172[»]
2K8VNMR-A24-172[»]
ProteinModelPortalO95881.
SMRO95881. Positions 24-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119252. 6 interactions.
IntActO95881. 1 interaction.
MINTMINT-5005906.
STRING9606.ENSP00000360688.

Chemistry

DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteO95881.

Proteomic databases

PaxDbO95881.
PeptideAtlasO95881.
PRIDEO95881.

Protocols and materials databases

DNASU51060.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371626; ENSP00000360688; ENSG00000117862.
GeneID51060.
KEGGhsa:51060.
UCSCuc001cti.4. human.

Organism-specific databases

CTD51060.
GeneCardsGC01M052485.
H-InvDBHIX0116253.
HGNCHGNC:24626. TXNDC12.
HPAHPA015086.
MIM609448. gene.
neXtProtNX_O95881.
PharmGKBPA142670665.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77442.
HOGENOMHOG000231100.
HOVERGENHBG107174.
InParanoidO95881.
KOK05360.
OMASYKYFYT.
OrthoDBEOG7DNNX2.
PhylomeDBO95881.
TreeFamTF321449.

Gene expression databases

BgeeO95881.
CleanExHS_TXNDC12.
GenevestigatorO95881.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTXNDC12. human.
EvolutionaryTraceO95881.
GeneWikiTXNDC12.
GenomeRNAi51060.
NextBio53641.
PROO95881.
SOURCESearch...

Entry information

Entry nameTXD12_HUMAN
AccessionPrimary (citable) accession number: O95881
Secondary accession number(s): B3KQS0, Q5T1T4, Q96H50
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM