ERLN2_HUMAN
ID ERLN2_HUMAN Reviewed; 339 AA.
AC O94905; A0JLQ1; A8K5S9; B4DM38; D3DSW0; Q6NW21; Q86VS6; Q86W49;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Erlin-2;
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2;
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2;
DE Short=SPFH domain-containing protein 2;
GN Name=ERLIN2; Synonyms=C8orf2, SPFH2; ORFNames=UNQ2441/PRO5003/PRO9924;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=10449903; DOI=10.1159/000015298;
RA Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.;
RT "Cloning and characterization of a novel gene (C8orf2), a human
RT representative of a novel gene family with homology to C. elegans
RT C42.C1.9.";
RL Cytogenet. Cell Genet. 85:227-231(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-338 (ISOFORM 1).
RC TISSUE=Duodenum, Prostate, and Testis;
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 [7]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP AND INTERACTION WITH ERLIN1.
RX PubMed=19240031; DOI=10.1074/jbc.m809801200;
RA Pearce M.M.P., Wormer D.B., Wilkens S., Wojcikiewicz R.J.H.;
RT "An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2
RT mediates the ER-associated degradation of inositol 1,4,5-trisphosphate
RT receptors.";
RL J. Biol. Chem. 284:10433-10445(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16835267; DOI=10.1242/jcs.03060;
RA Browman D.T., Resek M.E., Zajchowski L.D., Robbins S.M.;
RT "Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins
RT that define lipid-raft-like domains of the ER.";
RL J. Cell Sci. 119:3149-3160(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-106, AND MUTAGENESIS
RP OF ASN-106.
RX PubMed=17502376; DOI=10.1074/jbc.m701862200;
RA Pearce M.M., Wang Y., Kelley G.G., Wojcikiewicz R.J.H.;
RT "SPFH2 mediates the endoplasmic reticulum-associated degradation of
RT inositol 1,4,5-trisphosphate receptors and other substrates in mammalian
RT cells.";
RL J. Biol. Chem. 282:20104-20115(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INVOLVEMENT IN SPG18.
RX PubMed=21330303; DOI=10.1093/hmg/ddr070;
RA Yildirim Y., Orhan E.K., Iseri S.A., Serdaroglu-Oflazer P., Kara B.,
RA Solakoglu S., Tolun A.;
RT "A frameshift mutation of ERLIN2 in recessive intellectual disability,
RT motor dysfunction and multiple joint contractures.";
RL Hum. Mol. Genet. 20:1886-1892(2011).
RN [12]
RP FUNCTION, INTERACTION WITH AMFR; SYVN1; RNF139 AND TMUB1, AND SUBUNIT.
RX PubMed=21343306; DOI=10.1074/jbc.m110.211326;
RA Jo Y., Sguigna P.V., DeBose-Boyd R.A.;
RT "Membrane-associated ubiquitin ligase complex containing gp78 mediates
RT sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A
RT reductase.";
RL J. Biol. Chem. 286:15022-15031(2011).
RN [13]
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).
RN [14]
RP FUNCTION, AND INTERACTION WITH SCAP; INSIG1; SREBF1 AND SREBF2.
RX PubMed=24217618; DOI=10.1083/jcb.201305076;
RA Huber M.D., Vesely P.W., Datta K., Gerace L.;
RT "Erlins restrict SREBP activation in the ER and regulate cellular
RT cholesterol homeostasis.";
RL J. Cell Biol. 203:427-436(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INTERACTION WITH TMEM41B.
RX PubMed=30352685; DOI=10.1016/j.bbrc.2018.10.073;
RA Van Alstyne M., Lotti F., Dal Mas A., Area-Gomez E., Pellizzoni L.;
RT "Stasimon/Tmem41b localizes to mitochondria-associated ER membranes and is
RT essential for mouse embryonic development.";
RL Biochem. Biophys. Res. Commun. 506:463-470(2018).
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) such as ITPR1 (PubMed:19240031,
CC PubMed:17502376). Promotes sterol-accelerated ERAD of HMGCR probably
CC implicating an AMFR/gp78-containing ubiquitin ligase complex
CC (PubMed:21343306). Involved in regulation of cellular cholesterol
CC homeostasis by regulation the SREBP signaling pathway. May promote ER
CC retention of the SCAP-SREBF complex (PubMed:24217618).
CC {ECO:0000269|PubMed:17502376, ECO:0000269|PubMed:19240031,
CC ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:24217618}.
CC -!- SUBUNIT: Forms a heteromeric complex with ERLIN1. In complex with
CC ERLIN1, interacts with RNF170 (PubMed:19240031, PubMed:21610068).
CC Interacts with activated ITPR1, independently of the degree of ITPR1
CC polyubiquitination (By similarity). Interacts with SCAP, INSIG1, SREBF1
CC and SREBF2 under cholesterol sufficiency conditions; indicative for an
CC association with the SCAP-SREBP-INSIG complex (PubMed:24217618).
CC Probably part of an AMFR/gp78 and INSIG1-containing ubiquitin ligase
CC complex involved in ERAD of HMGCR. Interacts with TMUB1; TMUB1 bridges
CC the association with AMFR. Interacts with SYVN1 and RNF139
CC (PubMed:21343306). Interacts with TMEM259 (By similarity). Interacts
CC with TMEM41B (PubMed:30352685). {ECO:0000250|UniProtKB:Q8BFZ9,
CC ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:21343306,
CC ECO:0000269|PubMed:21610068, ECO:0000269|PubMed:24217618,
CC ECO:0000269|PubMed:30352685, ECO:0000305|PubMed:21343306}.
CC -!- INTERACTION:
CC O94905; Q9UKV5: AMFR; NbExp=10; IntAct=EBI-4400770, EBI-1046367;
CC O94905; O75477: ERLIN1; NbExp=4; IntAct=EBI-4400770, EBI-359299;
CC O94905; Q86TM6: SYVN1; NbExp=2; IntAct=EBI-4400770, EBI-947849;
CC O94905; Q9BVT8: TMUB1; NbExp=5; IntAct=EBI-4400770, EBI-11425701;
CC O94905; P00347: HMGCR; Xeno; NbExp=2; IntAct=EBI-4400770, EBI-11426687;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376,
CC ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:17502376,
CC ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like
CC domains of the endoplasmic reticulum membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94905-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94905-2; Sequence=VSP_008713, VSP_008714;
CC Name=3;
CC IsoId=O94905-3; Sequence=VSP_013940, VSP_013941;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10449903}.
CC -!- DISEASE: Spastic paraplegia 18, autosomal recessive (SPG18)
CC [MIM:611225]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG18 is a severe form
CC with onset in early childhood. Most affected individuals have severe
CC psychomotor retardation. Some may develop significant joint
CC contractures. {ECO:0000269|PubMed:21330303}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB018790; BAA36845.1; -; Genomic_DNA.
DR EMBL; AL442077; CAC09443.1; -; mRNA.
DR EMBL; AY358108; AAQ88475.1; -; mRNA.
DR EMBL; AY358851; AAQ89210.1; -; mRNA.
DR EMBL; AK291394; BAF84083.1; -; mRNA.
DR EMBL; AK297279; BAG59750.1; -; mRNA.
DR EMBL; CH471080; EAW63365.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63366.1; -; Genomic_DNA.
DR EMBL; BC005950; AAH05950.1; ALT_TERM; mRNA.
DR EMBL; BC048308; AAH48308.1; -; mRNA.
DR EMBL; BC050611; AAH50611.1; ALT_INIT; mRNA.
DR EMBL; BC067765; AAH67765.1; -; mRNA.
DR CCDS; CCDS34879.1; -. [O94905-2]
DR CCDS; CCDS6095.1; -. [O94905-1]
DR RefSeq; NP_001003790.1; NM_001003790.3. [O94905-2]
DR RefSeq; NP_001003791.1; NM_001003791.2. [O94905-2]
DR RefSeq; NP_009106.1; NM_007175.6. [O94905-1]
DR RefSeq; XP_005273449.1; XM_005273392.2.
DR RefSeq; XP_016868489.1; XM_017013000.1.
DR AlphaFoldDB; O94905; -.
DR SMR; O94905; -.
DR BioGRID; 116331; 270.
DR ComplexPortal; CPX-7121; ERLIN1-ERLIN2 complex.
DR CORUM; O94905; -.
DR IntAct; O94905; 107.
DR MINT; O94905; -.
DR STRING; 9606.ENSP00000276461; -.
DR ChEMBL; CHEMBL4739672; -.
DR TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family.
DR GlyConnect; 1222; 10 N-Linked glycans (1 site).
DR GlyGen; O94905; 2 sites, 10 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; O94905; -.
DR PhosphoSitePlus; O94905; -.
DR SwissPalm; O94905; -.
DR BioMuta; ERLIN2; -.
DR CPTAC; CPTAC-361; -.
DR CPTAC; CPTAC-362; -.
DR EPD; O94905; -.
DR jPOST; O94905; -.
DR MassIVE; O94905; -.
DR MaxQB; O94905; -.
DR PaxDb; O94905; -.
DR PeptideAtlas; O94905; -.
DR PRIDE; O94905; -.
DR ProteomicsDB; 50538; -. [O94905-1]
DR ProteomicsDB; 50539; -. [O94905-2]
DR ProteomicsDB; 50540; -. [O94905-3]
DR Antibodypedia; 719; 264 antibodies from 33 providers.
DR DNASU; 11160; -.
DR Ensembl; ENST00000335171.10; ENSP00000335220.6; ENSG00000147475.17. [O94905-2]
DR Ensembl; ENST00000518586.5; ENSP00000427847.1; ENSG00000147475.17. [O94905-3]
DR Ensembl; ENST00000519638.3; ENSP00000428112.1; ENSG00000147475.17. [O94905-1]
DR Ensembl; ENST00000523107.5; ENSP00000473292.1; ENSG00000147475.17. [O94905-3]
DR Ensembl; ENST00000523887.5; ENSP00000429903.1; ENSG00000147475.17. [O94905-3]
DR Ensembl; ENST00000648919.1; ENSP00000497100.1; ENSG00000147475.17. [O94905-2]
DR GeneID; 11160; -.
DR KEGG; hsa:11160; -.
DR MANE-Select; ENST00000519638.3; ENSP00000428112.1; NM_007175.8; NP_009106.1.
DR UCSC; uc003xkc.5; human. [O94905-1]
DR CTD; 11160; -.
DR DisGeNET; 11160; -.
DR GeneCards; ERLIN2; -.
DR HGNC; HGNC:1356; ERLIN2.
DR HPA; ENSG00000147475; Low tissue specificity.
DR MalaCards; ERLIN2; -.
DR MIM; 611225; phenotype.
DR MIM; 611605; gene.
DR neXtProt; NX_O94905; -.
DR OpenTargets; ENSG00000147475; -.
DR Orphanet; 209951; Autosomal recessive spastic paraplegia type 18.
DR Orphanet; 247604; Juvenile primary lateral sclerosis.
DR Orphanet; 280384; Recessive intellectual disability-motor dysfunction-multiple joint contractures syndrome.
DR PharmGKB; PA25961; -.
DR VEuPathDB; HostDB:ENSG00000147475; -.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR HOGENOM; CLU_1643079_0_0_1; -.
DR InParanoid; O94905; -.
DR OMA; YNMVRNF; -.
DR OrthoDB; 930534at2759; -.
DR PhylomeDB; O94905; -.
DR TreeFam; TF313059; -.
DR PathwayCommons; O94905; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions.
DR SignaLink; O94905; -.
DR BioGRID-ORCS; 11160; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; ERLIN2; human.
DR GeneWiki; ERLIN2; -.
DR GenomeRNAi; 11160; -.
DR Pharos; O94905; Tbio.
DR PRO; PR:O94905; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O94905; protein.
DR Bgee; ENSG00000147475; Expressed in choroid plexus epithelium and 197 other tissues.
DR ExpressionAtlas; O94905; baseline and differential.
DR Genevisible; O94905; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cholesterol metabolism;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Hereditary spastic paraplegia; Lipid metabolism; Membrane;
KW Neurodegeneration; Reference proteome; Signal-anchor; Steroid metabolism;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..339
FT /note="Erlin-2"
FT /id="PRO_0000002787"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..339
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 177..309
FT /note="Interaction with ERLIN1"
FT /evidence="ECO:0000269|PubMed:19240031"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75477"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17502376"
FT VAR_SEQ 142..206
FT /note="DQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKL
FT LIAAQKQKVVEKE -> GKKVSPEHAVLKQGSWNPASLHCLKPGCLQGVMVTYGQEMLK
FT NLVLRSWSQRSSWRMLIAMQQDP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013940"
FT VAR_SEQ 142..152
FT /note="DQIDENLKLAL -> GLENDFSQESS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008713"
FT VAR_SEQ 153..339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008714"
FT VAR_SEQ 207..339
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013941"
FT VARIANT 71
FT /note="V -> A (in dbSNP:rs2032066)"
FT /id="VAR_059140"
FT MUTAGEN 106
FT /note="N->Q: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:17502376"
FT CONFLICT 61
FT /note="S -> P (in Ref. 6; AAH05950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37840 MW; 3CF322548FD58DB0 CRC64;
MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK
SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV YDIVKNYTAD YDKALIFNKI
HHELNQFCSV HTLQEVYIEL FDQIDENLKL ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR
RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK
KISEIEDAAF LAREKAKADA ECYTAMKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD
IPNMFMDSAG SVSKQFEGLA DKLSFGLEDE PLETATKEN
