ERL2B_XENLA
ID ERL2B_XENLA Reviewed; 330 AA.
AC Q6DKC0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Erlin-2-B;
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2-B;
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2-B;
DE Short=SPFH domain-containing protein 2-B;
GN Name=erlin2-b; Synonyms=spfh2-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH74372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH74372.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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; BC074372; AAH74372.1; -; mRNA.
DR RefSeq; NP_001086246.1; NM_001092777.1.
DR AlphaFoldDB; Q6DKC0; -.
DR SMR; Q6DKC0; -.
DR DNASU; 444675; -.
DR GeneID; 444675; -.
DR KEGG; xla:444675; -.
DR CTD; 444675; -.
DR Xenbase; XB-GENE-6254593; erlin2.S.
DR OMA; YNMVRNF; -.
DR OrthoDB; 930534at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 444675; Expressed in lung and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 Cholesterol metabolism; Endoplasmic reticulum; Glycoprotein;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor;
KW Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="Erlin-2-B"
FT /id="PRO_0000378629"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 36846 MW; 765B45071D965129 CRC64;
MSHAGAIAAL GVALIAAALF SAIHKIEEGH VGVYYRGGAL LTTTSGPGFH LMLPFITSFK
SVQSTLQTDE VKNVPCGTSG GVMIYFDRIE VVNYLISSAV YDIVKNYTAD YDKALIFNKI
HHELNQFCSV HNLQEVYIEL FDQIDEDLKL ALQKDLNLMA PGIIIQAVRV TKPNIPEAIR
RNYELMESEK TKLLIAAQKQ KVVEKEAETE RKKAIIEAEK VAQVAQIKYG QKVMEKETEK
KISEIEDFAF LAREKARADA EYYTAQKAAE ANKLKLTPEY LQLMKYQAIA ANSKIYFGQD
IPNMFMDSSS AGPRVQSAKR NEPAAAEELK