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Q8BFZ9 (ERLN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Erlin-2
Alternative name(s):
Endoplasmic reticulum lipid raft-associated protein 2
Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2
Short name=SPFH domain-containing protein 2
Gene names
Name:Erlin2
Synonyms:Spfh2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Also involved in ITPR1 degradation by the ERAD pathway By similarity.

Subunit structure

Forms a heteromeric complex ERLIN1. In complex with ERLIN1, interacts with RNF170. Interacts with activated ITPR1, independently of the degree of ITPR1 polyubiquitination By similarity. Ref.3 Ref.4

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Note: Associated with lipid raft-like domains of the endoplasmic reticulum membrane By similarity.

Sequence similarities

Belongs to the band 7/mec-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Erlin-2
PRO_0000002788

Regions

Topological domain1 – 33Cytoplasmic Potential
Transmembrane4 – 2421Helical; Potential
Topological domain25 – 340316Lumenal Potential
Region177 – 309133Interaction with ERLIN1 By similarity

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2811L → Q in BAC27019. Ref.1
Sequence conflict3041M → I in BAC27019. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BFZ9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DA76718E5DCB7664

FASTA34037,873
        10         20         30         40         50         60 
MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK 

        70         80         90        100        110        120 
SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV YDIVKNYTAD YDKALIFNKI 

       130        140        150        160        170        180 
HHELNQFCSV HTLQEVYIEL FDQIDENLKL ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR 

       190        200        210        220        230        240 
RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK 

       250        260        270        280        290        300 
KISEIEDAAF LAREKAKADA ECYTALKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD 

       310        320        330        340 
IPNMFMDSAG GLGKQFEGLS DDKLGFGLED EPLEAPTKEN

« Hide

References

« Hide 'large scale' 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: Pituitary.
[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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[3]"SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells."
Pearce M.M., Wang Y., Kelley G.G., Wojcikiewicz R.J.H.
J. Biol. Chem. 282:20104-20115(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITPR1.
[4]"RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation."
Lu J.P., Wang Y., Sliter D.A., Pearce M.M., Wojcikiewicz R.J.
J. Biol. Chem. 286:24426-24433(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK030557 mRNA. Translation: BAC27019.1.
BC036333 mRNA. Translation: AAH36333.1.
BC038374 mRNA. Translation: AAH38374.1.
IPIIPI00221540.
RefSeqNP_705820.1. NM_153592.2.
UniGeneMm.277699.

3D structure databases

ProteinModelPortalQ8BFZ9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8BFZ9. 2 interactions.
STRING10090.ENSMUSP00000033873.

PTM databases

PhosphoSiteQ8BFZ9.

Proteomic databases

PaxDbQ8BFZ9.
PRIDEQ8BFZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033873; ENSMUSP00000033873; ENSMUSG00000031483.
GeneID244373.
KEGGmmu:244373.
UCSCuc009lhr.1. mouse.

Organism-specific databases

CTD11160.
MGIMGI:2387215. Erlin2.

Phylogenomic databases

eggNOGNOG307809.
GeneTreeENSGT00390000014666.
HOGENOMHOG000251613.
HOVERGENHBG050934.
InParanoidQ8BFZ9.
OMAAECYTAL.
OrthoDBEOG4ZPDVS.

Gene expression databases

BgeeQ8BFZ9.
CleanExMM_ERLIN2.
GenevestigatorQ8BFZ9.
GermOnlineENSMUSG00000031483. Mus musculus.

Family and domain databases

InterProIPR001107. Band_7.
[Graphical view]
PfamPF01145. Band_7. 1 hit.
[Graphical view]
SMARTSM00244. PHB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio386244.
SOURCESearch...

Entry information

Entry nameERLN2_MOUSE
AccessionPrimary (citable) accession number: Q8BFZ9
Secondary accession number(s): Q8BML8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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