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Q9D8U3 (ERP27_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Endoplasmic reticulum resident protein 27

Short name=ER protein 27
Short name=ERp27
Gene names
Name:Erp27
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Subunit structure

Interacts with PDIA3 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Miscellaneous

Does not contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 272247Endoplasmic reticulum resident protein 27
PRO_0000281119

Regions

Domain39 – 152114Thioredoxin
Region230 – 2334PDIA3-binding site By similarity
Motif269 – 2724Prevents secretion from ER By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1041N → S in AAI04407. Ref.2
Sequence conflict1041N → S in AAI04408. Ref.2
Sequence conflict1381V → M in AAI04407. Ref.2
Sequence conflict1381V → M in AAI04408. Ref.2
Sequence conflict2611H → L in AAI04407. Ref.2
Sequence conflict2611H → L in AAI04408. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D8U3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B4BC442A4C54E60C

FASTA27230,693
        10         20         30         40         50         60 
MKITRSRCLI LSFVLVCGLV PEVTADVEEA TDGLSTTQEP IWLTDVPATV ELIAAAEVAV 

        70         80         90        100        110        120 
IGFFQDLEIP IVSVFRSMAR QFQDVSFGIS NHSEVLTHYN VTSNSICLFR LVDDQQLHLN 

       130        140        150        160        170        180 
AEDIENLDAA KLSRFIHVNN LHWVTEYSPM IAAGLFNTMV QTHLLLMMKK TSPEYEESMR 

       190        200        210        220        230        240 
RYREAAKLFQ GQILFVLVDS GKRENGKVMS YFKLKESQLP ALAIYESVDD KWDTLPIAEV 

       250        260        270 
TVEKVRGFCE GFLKGLLQRD HEAEGDSGKE EL 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK007684 mRNA. Translation: BAB25188.1.
AK131830 mRNA. Translation: BAE20822.1.
BC104406 mRNA. Translation: AAI04407.1.
BC104407 mRNA. Translation: AAI04408.1.
RefSeqNP_081259.1. NM_026983.2.
UniGeneMm.33692.

3D structure databases

ProteinModelPortalQ9D8U3.
SMRQ9D8U3. Positions 38-255.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9D8U3.
PRIDEQ9D8U3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032343; ENSMUSP00000032343; ENSMUSG00000030219.
GeneID69187.
KEGGmmu:69187.
UCSCuc009emm.1. mouse.

Organism-specific databases

CTD121506.
MGIMGI:1916437. Erp27.

Phylogenomic databases

eggNOGNOG255456.
GeneTreeENSGT00740000115202.
HOGENOMHOG000112391.
HOVERGENHBG081481.
InParanoidQ9D8U3.
OMAEHVQNFC.
OrthoDBEOG7P2XT5.
PhylomeDBQ9D8U3.
TreeFamTF106381.

Gene expression databases

BgeeQ9D8U3.
CleanExMM_ERP27.
GenevestigatorQ9D8U3.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMSSF52833. SSF52833. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERP27. mouse.
NextBio328798.
PROQ9D8U3.
SOURCESearch...

Entry information

Entry nameERP27_MOUSE
AccessionPrimary (citable) accession number: Q9D8U3
Secondary accession number(s): Q3SX97
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot