ERLN2_PONAB
ID ERLN2_PONAB Reviewed; 339 AA.
AC Q5R7C5; Q5RBV6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Erlin-2;
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2;
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2;
DE Short=SPFH domain-containing protein 2;
GN Name=ERLIN2; Synonyms=SPFH2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90754.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR858527; CAH90754.1; ALT_INIT; mRNA.
DR EMBL; CR860193; CAH92335.1; -; mRNA.
DR RefSeq; NP_001126372.1; NM_001132900.1.
DR RefSeq; XP_009241970.1; XM_009243695.1.
DR RefSeq; XP_009241971.1; XM_009243696.1.
DR RefSeq; XP_009241972.1; XM_009243697.1.
DR AlphaFoldDB; Q5R7C5; -.
DR SMR; Q5R7C5; -.
DR STRING; 9601.ENSPPYP00000020748; -.
DR PRIDE; Q5R7C5; -.
DR Ensembl; ENSPPYT00000061314; ENSPPYP00000043710; ENSPPYG00000018510.
DR GeneID; 100173353; -.
DR KEGG; pon:100173353; -.
DR CTD; 11160; -.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR HOGENOM; CLU_058701_0_0_1; -.
DR InParanoid; Q5R7C5; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
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 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_0000002789"
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="Lumenal"
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"
FT CONFLICT 269
FT /note="A -> G (in Ref. 1; CAH90754)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="N -> K (in Ref. 1; CAH90754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37840 MW; 3CF322548FD58DB0 CRC64;
MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK
SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV YDIVKNYTAD YDKALIFNKI
HHELNQFCSV HTLQEVYIEL FDQIDENLKL ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR
RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK
KISEIEDAAF LAREKAKADA ECYTAMKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD
IPNMFMDSAG SVSKQFEGLA DKLSFGLEDE PLETATKEN
