Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q91X78 (ERLN1_MOUSE)

Last modified January 19, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Erlin-1
Alternative name(s):
    Endoplasmic reticulum lipid raft-associated protein 1
    Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1
      Short name=SPFH domain-containing protein 1
    Protein KE04 homolog
Gene names
Name: Erlin1
Synonyms: Keo4, Spfh1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

Hide | Top

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) By similarity.

Subunit structure

Forms a heteromeric complex with ERLIN2 By similarity.

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.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Erlin-1
PRO_0000002785

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621 Potential
Topological domain27 – 346320Lumenal Potential

Amino acid modifications

Modified residue2671N6-acetyllysine By similarity
Glycosylation1061N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict551F → S in AAH23849. Ref.2

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q91X78-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2AE4EC53DBDADBCA

FASTA34638,937
        10         20         30         40         50         60 
MTQARLLVAA VVGLVAILLY ASIHKIEEGH LAVYYRGGAL LTSPSGPGYH IMLPFITTFR 

        70         80         90        100        110        120 
SVQTTLQTDE VKNVPCGTSG GVMIYIDRIE VVNMLAPYAV FDIVRNYTAD YDKTLIFNKI 

       130        140        150        160        170        180 
HHELNQFCSA HTLQEVYIEL FDQIDENLKQ ALQKDLNTMA PGLTIQAVRV TKPKIPEAIR 

       190        200        210        220        230        240 
RNFELMEAEK TKLLIAAQKQ KVVEKEAETE RKRAVIEAEK IAQVAKIRFQ QKVMEKETEK 

       250        260        270        280        290        300 
RISEIEDAAF LAREKAKADA EYYAAHKYAT SNKHKLTPEY LELKKYQAIA SNSKIYFGSN 

       310        320        330        340 
IPSMFVDSSC ALKYSDGRTG REDSLPPEEA REPSGESPIQ NKENAG

« Hide

Hide | Top

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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pituitary and Placenta.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon and Mammary gland.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK133557 mRNA. Translation: BAE21724.1. Different initiation.
AK145990 mRNA. Translation: BAE26812.1. Different initiation.
BC011220 mRNA. Translation: AAH11220.1.
BC023849 mRNA. Translation: AAH23849.1.
IPIIPI00762654.
RefSeqNP_001157831.1.
NP_001157832.1.
NP_663477.3.
UniGeneMm.279865
Mm.476850

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ91X78.

Proteomic databases

PRIDEQ91X78.

Genome annotation databases

EnsemblENSMUST00000071698; ENSMUSP00000071618; ENSMUSG00000025198; Mus musculus. [Genome view]
ENSMUST00000112028; ENSMUSP00000107659; ENSMUSG00000025198; Mus musculus. [Genome view]
GeneID226144.
KEGGmmu:226144.
UCSCuc008hpd.1. mouse.

Organism-specific databases

CTD226144.
MGIMGI:2387613. Erlin1.

Phylogenomic databases

eggNOGroNOG09284.
HOGENOMHBG384947.
HOVERGENQ91X78.
InParanoidQ91X78.
OrthoDBEOG9RR93Q.
PhylomeDBQ91X78.

Gene expression databases

ArrayExpressQ91X78.
BgeeQ91X78.
CleanExMM_ERLIN1.
GenevestigatorQ91X78.
GermOnlineENSMUSG00000025198. 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 Resources

NextBio378024.
SOURCESearch...

Hide | Top

Entry information

Entry nameERLN1_MOUSE
AccessionPrimary (citable) accession number: Q91X78
Secondary accession number(s): Q3UKI9, Q8CIH7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents