ID   ERLN1_HUMAN             Reviewed;         348 AA.
AC   O75477; B0QZ42; D3DR65; Q53HV0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   10-JUN-2026, entry version 185.
DE   RecName: Full=Erlin-1 {ECO:0000303|PubMed:16835267};
DE   AltName: Full=Endoplasmic reticulum lipid raft-associated protein 1;
DE   AltName: Full=Protein KE04 {ECO:0000305|PubMed:11118313};
DE   AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1;
DE            Short=SPFH domain-containing protein 1;
GN   Name=ERLIN1 {ECO:0000312|HGNC:HGNC:16947};
GN   Synonyms=C10orf69 {ECO:0000312|HGNC:HGNC:16947}, KE04
GN   {ECO:0000303|PubMed:11118313}, KEO4, SPFH1
GN   {ECO:0000303|PubMed:19240031};
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Dendritic cell;
RX   PubMed=11118313; DOI=10.1006/bbrc.2000.3935;
RA   Li N., Huang X., Zhao Z., Chen G., Zhang W., Cao X.;
RT   "Identification and characterization of a novel gene KE04 differentially
RT   expressed by activated human dendritic cells.";
RL   Biochem. Biophys. Res. Commun. 279:487-493(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adipose tissue;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [6]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP   AND INTERACTION WITH ERLIN2.
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   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
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   [12]
RP   INTERACTION WITH AMFR AND SYVN1.
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.
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   INVOLVEMENT IN SPG62, AND VARIANT SPG62 VAL-50.
RX   PubMed=24482476; DOI=10.1126/science.1247363;
RA   Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
RA   Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A.,
RA   Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M.,
RA   Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G.,
RA   Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S.,
RA   Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M.,
RA   Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J.,
RA   Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A.,
RA   Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T.,
RA   Gleeson J.G.;
RT   "Exome sequencing links corticospinal motor neuron disease to common
RT   neurodegenerative disorders.";
RL   Science 343:506-511(2014).
RN   [17]
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   [18]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=31810281; DOI=10.3390/cells8121555;
RA   Whitten-Bauer C., Chung J., Gomez-Moreno A., Gomollon-Zueco P., Huber M.D.,
RA   Gerace L., Garaigorta U.;
RT   "The Host Factor Erlin-1 is Required for Efficient Hepatitis C Virus
RT   Infection.";
RL   Cells 8:0-0(2019).
RN   [19]
RP   FUNCTION, AND DEUBIQUITINATION BY USP25.
RX   PubMed=37683630; DOI=10.1016/j.devcel.2023.08.013;
RA   Teo Q.W., Wong H.H., Heunis T., Stancheva V., Hachim A., Lv H., Siu L.,
RA   Ho J., Lan Y., Mok C.K.P., Ulferts R., Sanyal S.;
RT   "Usp25-Erlin1/2 activity limits cholesterol flux to restrict virus
RT   infection.";
RL   Dev. Cell 58:2495-2509(2023).
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       (PubMed:37683630). Binds cholesterol and may promote ER retention of
CC       the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:19240031,
CC       ECO:0000269|PubMed:24217618, ECO:0000269|PubMed:37683630}.
CC   -!- FUNCTION: (Microbial infection) Required early in hepatitis C virus
CC       (HCV) infection to initiate RNA replication, and later in the infection
CC       to support infectious virus production. {ECO:0000269|PubMed:31810281}.
CC   -!- SUBUNIT: Forms a heteromeric complex with ERLIN2 (PubMed:19240031). In
CC       complex with ERLIN2, interacts with RNF170 (PubMed:21610068). Interacts
CC       with AMFR and SYVN1 (PubMed:21343306). {ECO:0000269|PubMed:19240031,
CC       ECO:0000269|PubMed:21343306, ECO:0000269|PubMed:21610068}.
CC   -!- INTERACTION:
CC       O75477; Q8TD06: AGR3; NbExp=6; IntAct=EBI-359299, EBI-3925742;
CC       O75477; Q9UKV5: AMFR; NbExp=2; IntAct=EBI-359299, EBI-1046367;
CC       O75477; Q12982: BNIP2; NbExp=3; IntAct=EBI-359299, EBI-752094;
CC       O75477; Q7Z4R8: C6orf120; NbExp=4; IntAct=EBI-359299, EBI-11050313;
CC       O75477; O94905: ERLIN2; NbExp=5; IntAct=EBI-359299, EBI-4400770;
CC       O75477; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-359299, EBI-11337888;
CC       O75477; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-359299, EBI-3232108;
CC       O75477; Q96IW7: SEC22A; NbExp=6; IntAct=EBI-359299, EBI-8652744;
CC       O75477; Q15436: SEC23A; NbExp=3; IntAct=EBI-359299, EBI-81088;
CC       O75477; Q86TM6: SYVN1; NbExp=2; IntAct=EBI-359299, EBI-947849;
CC       O75477; Q8N511: VMA12; NbExp=3; IntAct=EBI-359299, EBI-10265825;
CC       O75477; B2RDE6; NbExp=3; IntAct=EBI-359299, EBI-10175845;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267,
CC       ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267,
CC       ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like
CC       domains of the endoplasmic reticulum membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, placenta, liver, kidney,
CC       pancreas, prostate, testis, ovary and small intestine.
CC       {ECO:0000269|PubMed:11118313}.
CC   -!- PTM: Deubiquitinated by USP25; leading to stabilization.
CC       {ECO:0000269|PubMed:37683630}.
CC   -!- DISEASE: Spastic paraplegia 62, autosomal recessive (SPG62)
CC       [MIM:615681]: 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.
CC       {ECO:0000269|PubMed:24482476}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC26658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH31791.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD96200.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF064093; AAC26658.1; ALT_INIT; mRNA.
DR   EMBL; AK222480; BAD96200.1; ALT_INIT; mRNA.
DR   EMBL; AL138921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49846.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49847.1; -; Genomic_DNA.
DR   EMBL; BC031791; AAH31791.1; ALT_INIT; mRNA.
DR   CCDS; CCDS7487.2; -.
DR   RefSeq; NP_001094096.1; NM_001100626.2.
DR   RefSeq; NP_001334786.1; NM_001347857.2.
DR   RefSeq; NP_001334788.1; NM_001347859.2.
DR   RefSeq; NP_001334789.1; NM_001347860.2.
DR   RefSeq; NP_001334790.1; NM_001347861.2.
DR   RefSeq; NP_006450.2; NM_006459.4.
DR   PDB; 9O9U; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M=3-348.
DR   PDBsum; 9O9U; -.
DR   AlphaFoldDB; O75477; -.
DR   EMDB; EMD-70263; -.
DR   SMR; O75477; -.
DR   BioGRID; 115859; 216.
DR   ComplexPortal; CPX-7121; ERLIN1-ERLIN2 complex.
DR   CORUM; O75477; -.
DR   FunCoup; O75477; 1234.
DR   IntAct; O75477; 135.
DR   MINT; O75477; -.
DR   STRING; 9606.ENSP00000410964; -.
DR   ChEMBL; CHEMBL6067009; -.
DR   TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family.
DR   TCDB; 8.A.195.1.1; the erlin1/2 complex (erlin) family.
DR   GlyConnect; O75477; 10 N-Linked glycans (1 site).
DR   GlyCosmos; O75477; 1 site, 10 glycans.
DR   GlyGen; O75477; 2 sites, 10 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; O75477; -.
DR   PhosphoSitePlus; O75477; -.
DR   SwissPalm; O75477; -.
DR   BioMuta; ERLIN1; -.
DR   jPOST; O75477; -.
DR   MassIVE; O75477; -.
DR   PaxDb; 9606-ENSP00000410964; -.
DR   PeptideAtlas; O75477; -.
DR   PRIDE; O75477; -.
DR   ProteomicsDB; 50039; -.
DR   Pumba; O75477; -.
DR   Antibodypedia; 2279; 210 antibodies from 30 providers.
DR   DNASU; 10613; -.
DR   Ensembl; ENST00000407654.7; ENSP00000384900.3; ENSG00000107566.15.
DR   Ensembl; ENST00000421367.7; ENSP00000410964.2; ENSG00000107566.15.
DR   GeneID; 10613; -.
DR   KEGG; hsa:10613; -.
DR   MANE-Select; ENST00000421367.7; ENSP00000410964.2; NM_006459.4; NP_006450.2.
DR   UCSC; uc001kqn.5; human.
DR   AGR; HGNC:16947; -.
DR   ClinPGx; PA162385299; -.
DR   CTD; 10613; -.
DR   DisGeNET; 10613; -.
DR   GeneCards; ERLIN1; -.
DR   HGNC; HGNC:16947; ERLIN1.
DR   HPA; ENSG00000107566; Tissue enhanced (liver).
DR   MalaCards; ERLIN1; -.
DR   MIM; 611604; gene.
DR   MIM; 615681; phenotype.
DR   OpenTargets; ENSG00000107566; -.
DR   Orphanet; 401785; Autosomal recessive spastic paraplegia type 62.
DR   Orphanet; 300605; Juvenile amyotrophic lateral sclerosis.
DR   VEuPathDB; HostDB:ENSG00000107566; -.
DR   eggNOG; KOG2962; Eukaryota.
DR   GeneTree; ENSGT00390000014666; -.
DR   InParanoid; O75477; -.
DR   OMA; HIMIPIL; -.
DR   OrthoDB; 77368at2759; -.
DR   PAN-GO; O75477; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; O75477; -.
DR   PathwayCommons; O75477; -.
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-9931269; AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274).
DR   SignaLink; O75477; -.
DR   SIGNOR; O75477; -.
DR   Agora; ENSG00000107566; -.
DR   BioGRID-ORCS; 10613; 21 hits in 1154 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; ERLIN1; human.
DR   GeneWiki; ERLIN1; -.
DR   GenomeRNAi; 10613; -.
DR   Pharos; O75477; Tbio.
DR   PRO; PR:O75477; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O75477; protein.
DR   Bgee; ENSG00000107566; Expressed in secondary oocyte and 214 other cell types or tissues.
DR   ExpressionAtlas; O75477; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; NAS:ComplexPortal.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
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:0036503; P:ERAD pathway; IDA:UniProtKB.
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   CDD; cd03406; SPFH_like_u3; 1.
DR   FunFam; 3.30.479.30:FF:000009; Erlin-2 isoform 1; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR033294; Erlin1/2.
DR   PANTHER; PTHR15351; ERLIN (ER LIPID RAFT ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   PANTHER; PTHR15351:SF2; ERLIN-1; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cholesterol metabolism;
KW   Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW   Glycoprotein; Hereditary spastic paraplegia; Lipid metabolism;
KW   Lipid-binding; Membrane; Neurodegeneration; Proteomics identification;
KW   Reference proteome; Signal-anchor; Steroid metabolism; Sterol metabolism;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..348
FT                   /note="Erlin-1"
FT                   /id="PRO_0000002784"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          325..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   VARIANT         50
FT                   /note="G -> V (in SPG62; dbSNP:rs876661322)"
FT                   /evidence="ECO:0000269|PubMed:24482476"
FT                   /id="VAR_077847"
FT   CONFLICT        259
FT                   /note="K -> R (in Ref. 2; BAD96200)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  39171 MW;  C643FEADBE9095DE CRC64;
     MNMTQARVLV AAVVGLVAVL LYASIHKIEE GHLAVYYRGG ALLTSPSGPG YHIMLPFITT
     FRSVQTTLQT DEVKNVPCGT SGGVMIYIDR IEVVNMLAPY AVFDIVRNYT ADYDKTLIFN
     KIHHELNQFC SAHTLQEVYI ELFDQIDENL KQALQKDLNL MAPGLTIQAV RVTKPKIPEA
     IRRNFELMEA EKTKLLIAAQ KQKVVEKEAE TERKKAVIEA EKIAQVAKIR FQQKVMEKET
     EKRISEIEDA AFLAREKAKA DAEYYAAHKY ATSNKHKLTP EYLELKKYQA IASNSKIYFG
     SNIPNMFVDS SCALKYSDIR TGRESSLPSK EALEPSGENV IQNKESTG
//