ID   ERLN2_DANRE             Reviewed;         331 AA.
AC   A3QK16;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Erlin-2 {ECO:0000250|UniProtKB:O94905};
DE   AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2 {ECO:0000250|UniProtKB:O94905};
GN   Name=erlin2; ORFNames=si:dkey-204l11.2;
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:0000305, ECO:0000312|EMBL:CAM56585.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the endoplasmic reticulum-associated degradation
CC       (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Promotes
CC       sterol-accelerated ERAD of HMGCR. Involved in regulation of cellular
CC       cholesterol homeostasis by regulation the SREBP signaling pathway (By
CC       similarity). {ECO:0000250|UniProtKB:O94905}.
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; CR762390; CAM56585.1; -; Genomic_DNA.
DR   EMBL; BC074099; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001121887.1; NM_001128415.1.
DR   AlphaFoldDB; A3QK16; -.
DR   SMR; A3QK16; -.
DR   STRING; 7955.ENSDARP00000121177; -.
DR   PaxDb; A3QK16; -.
DR   PeptideAtlas; A3QK16; -.
DR   Ensembl; ENSDART00000131286; ENSDARP00000121177; ENSDARG00000086523.
DR   Ensembl; ENSDART00000142525; ENSDARP00000114597; ENSDARG00000086523.
DR   GeneID; 100151163; -.
DR   KEGG; dre:100151163; -.
DR   CTD; 11160; -.
DR   eggNOG; KOG2962; Eukaryota.
DR   GeneTree; ENSGT00390000014666; -.
DR   HOGENOM; CLU_058701_0_0_1; -.
DR   InParanoid; A3QK16; -.
DR   OMA; YNMVRNF; -.
DR   OrthoDB; 930534at2759; -.
DR   PhylomeDB; A3QK16; -.
DR   TreeFam; TF313059; -.
DR   Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR   PRO; PR:A3QK16; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000086523; Expressed in head kidney and 25 other tissues.
DR   ExpressionAtlas; A3QK16; 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   InterPro; IPR001107; Band_7.
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; Membrane; Reference proteome; Signal-anchor;
KW   Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..331
FT                   /note="Erlin-2"
FT                   /id="PRO_0000378627"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..331
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  36466 MW;  358E0F8E72CAD30B CRC64;
     MTLGAVASLI LAIGGAAVFS ALHKIEEGHV GVYYRGGALL TATSGPGFHL MLPFITTFKS
     VQTTLQTDEV KNVPCGTGGG VMIYFDRIEV VNYLVPSAVY GIVRNFTADY DKALIFNKVH
     HELNQFCSVH TLQDVYIGLF DQIDENLKLT LQEDLTSMAP GLIIQAVRVT KPNIPESIRR
     NYELMESERT KLLIAAQTQK VVEKEAETER KKAVIEAEKV AQVAEIKFGQ KVMEKETEKK
     ISQIEDSAYL ARQKAKADAE FYSAQRAAEA NKLKLTPEYL QLMKFKAIAA NSKIYFGSEI
     PHMFMDSGPG SSSSAASKAI DVLSEGMLDL E