Q96DN0 (ERP27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoplasmic reticulum resident protein 27
Short name=ER protein 27
Short name=ERp27

Gene names

Name:	ERP27
Synonyms:	C12orf46
ORF Names:	UNQ781/PRO1575

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	273 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)

Subunit structure	Interacts with PDIA3. Binds somatostatin-14 via hydrophobic interactions. Ref.4
Subcellular location	Endoplasmic reticulum lumen Ref.4.
Miscellaneous	Does not contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 273

248

Endoplasmic reticulum resident protein 27

PRO_0000281118

Regions

Domain

39 – 152

114

Thioredoxin

Region

230 – 233

4

PDIA3-binding site

Motif

270 – 273

4

Prevents secretion from ER

Natural variations

Natural variant

52

1

F → L.
Corresponds to variant rs35030722 [ dbSNP | Ensembl ].

VAR_052582

Experimental info

Mutagenesis

168

1

M → W: Decreases somatostatin-14 binding. Ref.4

Mutagenesis

196

1

I → A, L or W: Decreases somatostatin-14 binding. Ref.4

Mutagenesis

196

1

I → W: Conserved PDIA3 binding in vivo and in vitro. Ref.4

Mutagenesis

231

1

E → K or A: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4

Mutagenesis

232

1

W → A: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4

Mutagenesis

233

1

D → G: Greatly reduces PDIA3 binding in vivo and in vitro. Ref.4

Secondary structure

1

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273

Helix Strand Turn

Details...

Helix

46 – 54

9

Beta strand

56 – 63

8

Helix

71 – 78

8

Turn

79 – 81

3

Beta strand

85 – 90

6

Helix

93 – 98

6

Beta strand

103 – 110

8

Turn

111 – 114

4

Beta strand

115 – 119

5

Helix

121 – 125

5

Helix

129 – 139

11

Beta strand

143 – 146

4

Helix

149 – 157

9

Beta strand

162 – 168

7

Helix

175 – 188

14

Turn

189 – 192

4

Beta strand

194 – 199

6

Helix

203 – 205

3

Helix

206 – 211

6

Helix

216 – 218

3

Beta strand

220 – 229

10

Beta strand

232 – 235

4

Helix

242 – 253

12

Sequences

	Sequence		Length	Mass (Da)
	Q96DN0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: D47280F6F6FDE419	FASTA	273	30,480
	10 20 30 40 50 60 MEAAPSRFMF LLFLLTCELA AEVAAEVEKS SDGPGAAQEP TWLTDVPAAM EFIAATEVAV 70 80 90 100 110 120 IGFFQDLEIP AVPILHSMVQ KFPGVSFGIS TDSEVLTHYN ITGNTICLFR LVDNEQLNLE 130 140 150 160 170 180 DEDIESIDAT KLSRFIEINS LHMVTEYNPV TVIGLFNSVI QIHLLLIMNK ASPEYEENMH 190 200 210 220 230 240 RYQKAAKLFQ GKILFILVDS GMKENGKVIS FFKLKESQLP ALAIYQTLDD EWDTLPTAEV 250 260 270 SVEHVQNFCD GFLSGKLLKE NRESEGKTPK VEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[3]	"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: Lung.
[4]	"ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57." Alanen H.I., Williamson R.A., Howard M.J., Hatahet F.S., Salo K.E.H., Kauppila A., Kellokumpu S., Ruddock L.W. J. Biol. Chem. 281:33727-33738(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, INTERACTION WITH PDIA3, MUTAGENESIS OF MET-168; ILE-196; GLU-231; TRP-232 AND ASP-233.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY358536 mRNA. Translation: AAQ88900.1.
AK056677 mRNA. Translation: BAB71251.1.
BC030218 mRNA. Translation: AAH30218.1.

IPI

IPI00061005.

RefSeq

NP_689534.1. NM_152321.2.

UniGene

Hs.162143.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L4C	NMR	-	A	26-141	[»]
4F9Z	X-ray	2.20	A/B/C/D/E	30-256	[»]

ProteinModelPortal

Q96DN0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96DN0. 1 interaction.

MINT

MINT-2878436.

STRING

9606.ENSP00000266397.

Polymorphism databases

DMDM

74731474.

Proteomic databases

PaxDb

Q96DN0.

PRIDE

Q96DN0.

Protocols and materials databases

DNASU

121506.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266397; ENSP00000266397; ENSG00000139055.

GeneID

121506.

KEGG

hsa:121506.

UCSC

uc001rco.3. human.

Organism-specific databases

CTD

121506.

GeneCards

GC12M015066.

HGNC

HGNC:26495. ERP27.

HPA

HPA039636.

MIM

610642. gene.

neXtProt

NX_Q96DN0.

PharmGKB

PA162385401.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG255456.

HOGENOM

HOG000112391.

HOVERGEN

HBG081481.

InParanoid

Q96DN0.

OMA

EHVQNFC.

OrthoDB

EOG40GCS1.

PhylomeDB

Q96DN0.

Enzyme and pathway databases

BRENDA

5.3.4.1. 2681.

Gene expression databases

ArrayExpress

Q96DN0.

Bgee

Q96DN0.

CleanEx

HS_ERP27.

Genevestigator

Q96DN0.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR012336. Thioredoxin-like_fold.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 2 hits.

PROSITE

PS51352. THIOREDOXIN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ERP27. human.

GenomeRNAi

121506.

NextBio

80755.

SOURCE

Search...

Entry information

Entry name

ERP27_HUMAN

Accession

Primary (citable) accession number: Q96DN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 92 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.