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ERLN2_RAT
ID   ERLN2_RAT               Reviewed;         339 AA.
AC   B5DEH2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Erlin-2 {ECO:0000250|UniProtKB:Q8BFZ9};
DE   AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2 {ECO:0000250|UniProtKB:Q8BFZ9, ECO:0000312|EMBL:AAI68668.1};
DE   AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2 {ECO:0000250|UniProtKB:Q8BFZ9};
DE            Short=SPFH domain-containing protein 2 {ECO:0000250|UniProtKB:Q8BFZ9, ECO:0000312|EMBL:AAI68668.1};
GN   Name=Erlin2 {ECO:0000312|EMBL:AAI68668.1, ECO:0000312|RGD:1309010};
GN   Synonyms=Spfh2 {ECO:0000250|UniProtKB:Q8BFZ9};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:EDM09088.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000312|EMBL:EDM09088.1};
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAI68668.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate {ECO:0000312|EMBL:AAI68668.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:EDM09088.1}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Maurya D.K., Bhargava P.;
RL   Submitted (MAR-2009) to UniProtKB.
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. Promotes sterol-
CC       accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing
CC       ubiquitin ligase complex. Involved in regulation of cellular
CC       cholesterol homeostasis by regulation the SREBP signaling pathway. May
CC       promote ER retention of the SCAP-SREBF complex (By similarity).
CC       {ECO:0000250|UniProtKB:O94905}.
CC   -!- SUBUNIT: Forms a heteromeric complex with ERLIN1. In complex with
CC       ERLIN1, interacts with RNF170. Interacts with activated ITPR1,
CC       independently of the degree of ITPR1 polyubiquitination. Interacts with
CC       SCAP, INSIG1, SREBF1 and SREBF2 under cholesterol sufficiency
CC       conditions; indicative for an association with the SCAP-SREBP-INSIG
CC       complex. Probably part of an AMFR/gp78 and INSIG1-containing ubiquitin
CC       ligase complex involved in ERAD of HMGCR. Interacts with TMUB1; TMUB1
CC       bridges the association with AMFR. Interacts with SYVN1 and RNF139.
CC       Interacts with TMEM259 (By similarity). Interacts with TMEM41B (By
CC       similarity). {ECO:0000250|UniProtKB:O94905,
CC       ECO:0000250|UniProtKB:Q8BFZ9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}. Note=Associated
CC       with lipid raft-like domains of the endoplasmic reticulum membrane.
CC       {ECO:0000250|UniProtKB:O94905}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000255}.
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DR   EMBL; CH473970; EDM09088.1; -; Genomic_DNA.
DR   EMBL; BC168668; AAI68668.1; -; mRNA.
DR   RefSeq; NP_001099558.1; NM_001106088.2.
DR   RefSeq; XP_008769545.1; XM_008771323.2.
DR   RefSeq; XP_008769546.1; XM_008771324.2.
DR   AlphaFoldDB; B5DEH2; -.
DR   BioGRID; 253334; 8.
DR   IntAct; B5DEH2; 4.
DR   MINT; B5DEH2; -.
DR   STRING; 10116.ENSRNOP00000018973; -.
DR   GlyGen; B5DEH2; 1 site.
DR   iPTMnet; B5DEH2; -.
DR   PhosphoSitePlus; B5DEH2; -.
DR   jPOST; B5DEH2; -.
DR   PaxDb; B5DEH2; -.
DR   PeptideAtlas; B5DEH2; -.
DR   PRIDE; B5DEH2; -.
DR   Ensembl; ENSRNOT00000018973; ENSRNOP00000018973; ENSRNOG00000013763.
DR   GeneID; 290823; -.
DR   KEGG; rno:290823; -.
DR   UCSC; RGD:1309010; rat.
DR   CTD; 11160; -.
DR   RGD; 1309010; Erlin2.
DR   eggNOG; KOG2962; Eukaryota.
DR   GeneTree; ENSGT00390000014666; -.
DR   HOGENOM; CLU_058701_0_0_1; -.
DR   InParanoid; B5DEH2; -.
DR   OMA; YNMVRNF; -.
DR   OrthoDB; 930534at2759; -.
DR   PhylomeDB; B5DEH2; -.
DR   TreeFam; TF313059; -.
DR   Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR   PRO; PR:B5DEH2; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Proteomes; UP000234681; Chromosome 16.
DR   Bgee; ENSRNOG00000013763; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; B5DEH2; RN.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISO:RGD.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:RGD.
DR   GO; GO:0032933; P:SREBP signaling pathway; ISO:RGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
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; Cholesterol metabolism; Endoplasmic reticulum; Glycoprotein;
KW   Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW   Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Erlin-2"
FT                   /id="PRO_0000371230"
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="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          177..309
FT                   /note="Interaction with ERLIN1"
FT                   /evidence="ECO:0000250"
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:0000255"
SQ   SEQUENCE   339 AA;  37710 MW;  A777F11C4B1A47D7 CRC64;
     MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK
     SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPHAV YDIVKNYTAD YDKALIFNKI
     HHELNQFCSV HTLQEVYIEL FDQIDENLKL ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR
     RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK
     KISEIEDAAF LAREKAKADA ECYTALKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD
     IPNMFMDSAG GLGKQSEGLS DKLGFGLEDE PLETATKDN
 
 
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