ERLN1_HUMAN
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 03-AUG-2022, entry version 167.
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},
GN KE04 {ECO:0000303|PubMed:11118313}, KEO4,
GN SPFH1 {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).
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 (PubMed:24217618). {ECO:0000269|PubMed:19240031,
CC ECO:0000269|PubMed:24217618}.
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; O94905: ERLIN2; NbExp=4; 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: TMEM199; 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 -!- 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_001100626.1.
DR RefSeq; NP_001334786.1; NM_001347857.1.
DR RefSeq; NP_001334788.1; NM_001347859.1.
DR RefSeq; NP_001334789.1; NM_001347860.1.
DR RefSeq; NP_001334790.1; NM_001347861.1.
DR RefSeq; NP_006450.2; NM_006459.3.
DR AlphaFoldDB; O75477; -.
DR SMR; O75477; -.
DR BioGRID; 115859; 139.
DR ComplexPortal; CPX-7121; ERLIN1-ERLIN2 complex.
DR CORUM; O75477; -.
DR IntAct; O75477; 81.
DR MINT; O75477; -.
DR STRING; 9606.ENSP00000410964; -.
DR TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family.
DR GlyConnect; 1221; 10 N-Linked glycans (1 site).
DR GlyGen; O75477; 1 site, 10 N-linked glycans (1 site).
DR iPTMnet; O75477; -.
DR PhosphoSitePlus; O75477; -.
DR SwissPalm; O75477; -.
DR BioMuta; ERLIN1; -.
DR EPD; O75477; -.
DR jPOST; O75477; -.
DR MassIVE; O75477; -.
DR MaxQB; O75477; -.
DR PaxDb; O75477; -.
DR PeptideAtlas; O75477; -.
DR PRIDE; O75477; -.
DR ProteomicsDB; 50039; -.
DR Antibodypedia; 2279; 212 antibodies from 31 providers.
DR DNASU; 10613; -.
DR Ensembl; ENST00000407654.7; ENSP00000384900.3; ENSG00000107566.14.
DR Ensembl; ENST00000421367.7; ENSP00000410964.2; ENSG00000107566.14.
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 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 neXtProt; NX_O75477; -.
DR OpenTargets; ENSG00000107566; -.
DR Orphanet; 401785; Autosomal recessive spastic paraplegia type 62.
DR PharmGKB; PA162385299; -.
DR VEuPathDB; HostDB:ENSG00000107566; -.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR InParanoid; O75477; -.
DR OMA; CAFQQAS; -.
DR OrthoDB; 930534at2759; -.
DR PhylomeDB; O75477; -.
DR TreeFam; TF313059; -.
DR PathwayCommons; O75477; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR SignaLink; O75477; -.
DR BioGRID-ORCS; 10613; 19 hits in 1080 CRISPR screens.
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 212 other tissues.
DR ExpressionAtlas; O75477; baseline and differential.
DR Genevisible; O75477; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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; IC: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: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.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol metabolism; Direct protein sequencing;
KW Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Hereditary spastic paraplegia; Lipid metabolism; Lipid-binding; Membrane;
KW Neurodegeneration; Reference proteome; Signal-anchor; Steroid metabolism;
KW Sterol metabolism; 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 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
