ERLN1_MOUSE
ID ERLN1_MOUSE Reviewed; 348 AA.
AC Q91X78; A0A0R4J1G5; Q3UKI9; Q8CIH7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Erlin-1 {ECO:0000250|UniProtKB:O75477};
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 1;
DE AltName: Full=Protein KE04 homolog {ECO:0000305};
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1;
DE Short=SPFH domain-containing protein 1;
GN Name=Erlin1 {ECO:0000312|MGI:MGI:2387613};
GN Synonyms=Keo4, Spfh1 {ECO:0000250|UniProtKB:O75477};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH RNF170.
RX PubMed=21610068; DOI=10.1074/jbc.m111.251983;
RA Lu J.P., Wang Y., Sliter D.A., Pearce M.M., Wojcikiewicz R.J.;
RT "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase,
RT mediates inositol 1,4,5-trisphosphate receptor ubiquitination and
RT degradation.";
RL J. Biol. Chem. 286:24426-24433(2011).
CC -!- FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the
CC endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-
CC trisphosphate receptors (IP3Rs). Involved in regulation of cellular
CC cholesterol homeostasis by regulation the SREBP signaling pathway.
CC Binds cholesterol and may promote ER retention of the SCAP-SREBF
CC complex (By similarity). {ECO:0000250|UniProtKB:O75477}.
CC -!- SUBUNIT: Forms a heteromeric complex with ERLIN2 (By similarity). In
CC complex with ERLIN2, interacts with RNF170 (PubMed:21610068). Interacts
CC with AMFR and SYVN1 (By similarity). {ECO:0000250|UniProtKB:O75477,
CC ECO:0000269|PubMed:21610068}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Note=Associated
CC with lipid raft-like domains of the endoplasmic reticulum membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11220.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH23849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK133557; BAE21724.1; -; mRNA.
DR EMBL; AK145990; BAE26812.1; -; mRNA.
DR EMBL; AC124693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466534; EDL41918.1; -; Genomic_DNA.
DR EMBL; BC011220; AAH11220.1; ALT_INIT; mRNA.
DR EMBL; BC023849; AAH23849.1; ALT_INIT; mRNA.
DR CCDS; CCDS29842.2; -.
DR RefSeq; NP_001157831.1; NM_001164359.1.
DR RefSeq; NP_001157832.1; NM_001164360.1.
DR RefSeq; NP_663477.3; NM_145502.3.
DR RefSeq; XP_006527061.1; XM_006526998.3.
DR AlphaFoldDB; Q91X78; -.
DR BioGRID; 230480; 5.
DR IntAct; Q91X78; 2.
DR STRING; 10090.ENSMUSP00000129684; -.
DR GlyConnect; 2300; 1 N-Linked glycan (1 site).
DR GlyGen; Q91X78; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q91X78; -.
DR PhosphoSitePlus; Q91X78; -.
DR EPD; Q91X78; -.
DR jPOST; Q91X78; -.
DR MaxQB; Q91X78; -.
DR PaxDb; Q91X78; -.
DR PeptideAtlas; Q91X78; -.
DR PRIDE; Q91X78; -.
DR ProteomicsDB; 275473; -.
DR ProteomicsDB; 330844; -.
DR Antibodypedia; 2279; 212 antibodies from 31 providers.
DR DNASU; 226144; -.
DR Ensembl; ENSMUST00000071698; ENSMUSP00000071618; ENSMUSG00000025198.
DR Ensembl; ENSMUST00000112028; ENSMUSP00000107659; ENSMUSG00000025198.
DR Ensembl; ENSMUST00000170801; ENSMUSP00000129684; ENSMUSG00000025198.
DR GeneID; 226144; -.
DR KEGG; mmu:226144; -.
DR UCSC; uc008hpd.2; mouse.
DR CTD; 10613; -.
DR MGI; MGI:2387613; Erlin1.
DR VEuPathDB; HostDB:ENSMUSG00000025198; -.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR InParanoid; Q91X78; -.
DR OMA; CAFQQAS; -.
DR OrthoDB; 930534at2759; -.
DR PhylomeDB; Q91X78; -.
DR TreeFam; TF313059; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 226144; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Erlin1; mouse.
DR PRO; PR:Q91X78; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91X78; protein.
DR Bgee; ENSMUSG00000025198; Expressed in mucous cell of stomach and 241 other tissues.
DR ExpressionAtlas; Q91X78; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0032933; P:SREBP signaling pathway; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR CDD; cd03406; SPFH_like_u3; 1.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR033294; Erlin1/2.
DR PANTHER; PTHR15351; PTHR15351; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol metabolism; Endoplasmic reticulum; Glycoprotein;
KW Lipid metabolism; Lipid-binding; Membrane; Reference proteome;
KW Signal-anchor; Steroid metabolism; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..348
FT /note="Erlin-1"
FT /id="PRO_0000002785"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..348
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75477"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 57
FT /note="F -> S (in Ref. 4; AAH23849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39182 MW; 3BA4BE035662EC6F CRC64;
MNMTQARLLV AAVVGLVAIL LYASIHKIEE GHLAVYYRGG ALLTSPSGPG YHIMLPFITT
FRSVQTTLQT DEVKNVPCGT SGGVMIYIDR IEVVNMLAPY AVFDIVRNYT ADYDKTLIFN
KIHHELNQFC SAHTLQEVYI ELFDQIDENL KQALQKDLNT MAPGLTIQAV RVTKPKIPEA
IRRNFELMEA EKTKLLIAAQ KQKVVEKEAE TERKRAVIEA EKIAQVAKIR FQQKVMEKET
EKRISEIEDA AFLAREKAKA DAEYYAAHKY ATSNKHKLTP EYLELKKYQA IASNSKIYFG
SNIPSMFVDS SCALKYSDGR TGREDSLPPE EAREPSGESP IQNKENAG
