O95881 (TXD12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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 component	Endoplasmic reticulum
Domain	Redox-active center Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular_component	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.7

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.8 Ref.10

Experimental info

Mutagenesis

66

1

C → S: Loss of oxidase activity. Ref.8

Mutagenesis

69

1

C → S: Loss of oxidase activity. Ref.8

Sequence conflict

102

1

D → H in AAH08913. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

172

Helix Strand Turn

Details...

Beta strand

33 – 38

6

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

Turn

120 – 122

3

Turn

135 – 139

5

Helix

144 – 158

15

Helix

159 – 161

3

Sequences

	Sequence		Length	Mass (Da)
	O95881 [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] [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. , 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. , 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. , 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.

IPI

IPI00026328.

RefSeq

NP_056997.1. NM_015913.3.

UniGene

Hs.476033.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SEN	X-ray	1.20	A	23-172	[»]
2K8V	NMR	-	A	24-172	[»]

ProteinModelPortal

O95881.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95881. 1 interaction.

STRING

9606.ENSP00000360688.

PTM databases

PhosphoSite

O95881.

Proteomic databases

PaxDb

O95881.

PeptideAtlas

O95881.

PRIDE

O95881.

Protocols and materials databases

DNASU

51060.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371626; ENSP00000360688; ENSG00000117862.

GeneID

51060.

KEGG

hsa:51060.

UCSC

uc001cti.3. human.

Organism-specific databases

CTD

51060.

GeneCards

GC01M052485.

H-InvDB

HIX0116253.

HGNC

HGNC:24626. TXNDC12.

HPA

HPA015086.

MIM

609448. gene.

neXtProt

NX_O95881.

PharmGKB

PA142670665.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG77442.

HOGENOM

HOG000231100.

HOVERGEN

HBG107174.

InParanoid

O95881.

KO

K05360.

OMA

NGNPNYK.

OrthoDB

EOG4W3SP9.

PhylomeDB

O95881.

Gene expression databases

Bgee

O95881.

CleanEx

HS_TXNDC12.

Genevestigator

O95881.

GermOnline

ENSG00000117862. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

TXNDC12. human.

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

O95881.

GenomeRNAi

51060.

NextBio

53641.

SOURCE

Search...

Entry information

Entry name

TXD12_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.