ERLN1_DANRE
ID ERLN1_DANRE Reviewed; 342 AA.
AC Q58EG2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Erlin-1 {ECO:0000312|EMBL:AL929005};
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 1 {ECO:0000312|EMBL:AL929005};
GN Name=erlin1 {ECO:0000312|ZFIN:ZDB-GENE-050327-13};
GN ORFNames=si:ch211-223p8.2, zgc:110547;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AL929005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH91924.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the endoplasmic reticulum-associated degradation
CC (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in
CC regulation of cellular cholesterol homeostasis by regulation the SREBP
CC signaling pathway. Binds cholesterol and may promote ER retention of
CC the SCAP-SREBF complex. {ECO:0000250|UniProtKB:O75477}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O94905, ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:O94905, ECO:0000255}.
CC Note=Associated with lipid raft-like domains of the endoplasmic
CC reticulum membrane. {ECO:0000250|UniProtKB:O94905, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000255}.
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DR EMBL; AL929005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091924; AAH91924.1; -; mRNA.
DR RefSeq; NP_001014325.1; NM_001014303.1.
DR RefSeq; XP_005156890.1; XM_005156833.3.
DR RefSeq; XP_005156891.1; XM_005156834.3.
DR AlphaFoldDB; Q58EG2; -.
DR SMR; Q58EG2; -.
DR IntAct; Q58EG2; 1.
DR MINT; Q58EG2; -.
DR STRING; 7955.ENSDARP00000015815; -.
DR PaxDb; Q58EG2; -.
DR Ensembl; ENSDART00000003922; ENSDARP00000015815; ENSDARG00000021991.
DR Ensembl; ENSDART00000172156; ENSDARP00000140094; ENSDARG00000021991.
DR GeneID; 541490; -.
DR KEGG; dre:541490; -.
DR CTD; 10613; -.
DR ZFIN; ZDB-GENE-050327-13; erlin1.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR InParanoid; Q58EG2; -.
DR OMA; CAFQQAS; -.
DR OrthoDB; 930534at2759; -.
DR PhylomeDB; Q58EG2; -.
DR TreeFam; TF313059; -.
DR Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR PRO; PR:Q58EG2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000021991; Expressed in early embryo and 27 other tissues.
DR ExpressionAtlas; Q58EG2; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
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:0032933; P:SREBP signaling pathway; IBA:GO_Central.
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 2: Evidence at transcript level;
KW 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..342
FT /note="Erlin-1"
FT /id="PRO_0000378625"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..342
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 308..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 38319 MW; 7B9789D4EFACE1C4 CRC64;
MAHVGAVVAA MAGLMAILLH SSIHKIEEGH LAVYYRGGAL LTSPNGPGYH IMLPFITSYR
SVQTTLQTDE IKNVPCGTSG GVMIYFDRIE VVNMLIPTSV VDIVRNYTAD YDKTLIFNKI
HHELNQFCSV HTLQEVYIEL FDIIDENLKT ALQKDLNCMA PGLTIQAVRV TKPKIPEAIR
RNYELMEAEK TRLLITVQTQ KVVEKEAETE RKKAIIEAQK VAQVAEIQFQ QKVMEKETEK
KISEIEDAAF LAREKARADA EYYTAAKFAE ANTLKLTPEY LQLMKYQAIA ANSKIYFGQD
IPNMFVDSSA SRPAAGESEQ LESLSMRESL KKASKPKASE GH
