Reviewed, UniProtKB/Swiss-Prot O95881 (TXD12_HUMAN)

Names and origin

Protein names

Recommended name:
    Thioredoxin domain-containing protein 12
    EC=1.8.4.2
Alternative name(s):
    Thioredoxin-like protein p19
    Endoplasmic reticulum protein ERp19
    ERp18
    hTLP19

Gene names

Name:	TXNDC12
Synonyms:	TLP19
ORF Names:	UNQ713/PRO1376

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Possesses significant protein thiol-disulfide oxidase activity. Ref.7
Catalytic activity	2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.
Subcellular location	Endoplasmic reticulum lumen. Ref.7
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 component	Endoplasmic reticulum
Domain	Redox-active center Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-disulfide reductase (glutathione) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.6

Chain

27 – 172

146

Thioredoxin domain-containing protein 12

PRO_0000034189

Regions

Motif

169 – 172

4

Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond

66 ↔ 69

Redox-active Ref.7

Experimental info

Mutagenesis

66

1

C → S: Loss of oxidase activity. Ref.7

Mutagenesis

69

1

C → S: Loss of oxidase activity. Ref.7

Sequence conflict

102

1

D → H in AAH08913. Ref.5

Secondary structure

1

.

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172

Helix Strand Turn

Details...

Helix

43 – 53

11

Beta strand

57 – 62

6

Helix

67 – 77

11

Helix

80 – 86

7

Beta strand

89 – 95

7

Helix

96 – 98

3

Helix

103 – 105

3

Beta strand

112 – 118

7

Helix

144 – 158

15

Helix

159 – 161

3

Sequences

	Sequence		Length	Mass (Da)
	O95881-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 3092E9515A7C4094	FASTA	172	19,206
	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

References

	« Hide 'large scale' referencesShow '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: 14557066] [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. , 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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Kidney and Ovary.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41.
[7]	"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: 12761212] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-66 AND CYS-69.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF543416 mRNA. Translation: AAN34781.1.
AF131758 mRNA. Translation: AAD20035.1.
AY358982 mRNA. Translation: AAQ89341.1.
AL445685 Genomic DNA. Translation: CAI17031.1.
BC001493 mRNA. Translation: AAH01493.1.
BC008953 mRNA. Translation: AAH08953.1.
BC008913 mRNA. Translation: AAH08913.1.

IPI

IPI00026328.

RefSeq

NP_056997.1.

UniGene

Hs.476033

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SEN	X-ray	1.20	A	23-172	[»]

SMR

O95881. Positions 30-163.

ModBase

Search...

Proteomic databases

PeptideAtlas

O95881.

PRIDE

O95881.

Genome annotation databases

Ensembl

ENSG00000117862. Homo sapiens. [Contig view]

GeneID

51060.

KEGG

hsa:51060.

Organism-specific databases

GeneCards

GC01M052199.

H-InvDB

HIX0000579.
HIX0029114.

HGNC

HGNC:24626. TXNDC12.

MIM

609448. gene.

PharmGKB

PA142670665.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O95881.

HOVERGEN

O95881.

OMA

O95881. CHACKAL.

Enzyme and pathway databases

BRENDA

1.8.4.2. 247.

Gene expression databases

ArrayExpress

O95881.

Bgee

O95881.

CleanEx

HS_TXNDC12.

GermOnline

ENSG00000117862. Homo sapiens.

Family and domain databases

InterPro

IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

53641.

SOURCE

Search...

Entry information

Entry name

TXD12_HUMAN

Accession

Primary (citable) accession number: O95881
Secondary accession number(s): Q5T1T4, Q96H50

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)