ERL2A_XENLA
ID ERL2A_XENLA Reviewed; 335 AA.
AC Q5XH03;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Erlin-2-A;
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 2-A;
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2-A;
DE Short=SPFH domain-containing protein 2-A;
GN Name=erlin2-a; Synonyms=spfh2-a;
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:AAH84273.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH84273.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-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; BC084273; AAH84273.1; -; mRNA.
DR RefSeq; NP_001088269.1; NM_001094800.1.
DR AlphaFoldDB; Q5XH03; -.
DR BioGRID; 105180; 1.
DR DNASU; 495100; -.
DR GeneID; 495100; -.
DR KEGG; xla:495100; -.
DR CTD; 495100; -.
DR Xenbase; XB-GENE-950149; erlin2.L.
DR OrthoDB; 930534at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 495100; Expressed in blastula 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 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..335
FT /note="Erlin-2-A"
FT /id="PRO_0000378628"
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..335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 335 AA; 37292 MW; E97110D0F124EDC3 CRC64;
MSHAGAIVGL GVALIAAALF SAIHKIEEGH VGVYYRGGAL LSTTSGPGFH LMFPFITSFK
SVQSTLQTDE IKNVPCGTSG GVMIYFDRIE VVNYLISSAV YDIVKNFTAD YDKALIFNKI
HHELNQFCSV HNLQEVYIEL FDQIDENLKL ALQEDLNLMA PGIIIQAVRV TKPKIPEAIG
RNFELMEGEK TKLLIAAQKQ KVVEKEAETE RKKAIIEAEK VAQVAQIKYK QKVMEKETEK
KISEIEDFAF VAREKARADA EYYTAHKVAE ANRLKLTPEY LQLVKYQAIA ANSKIYFGQD
IPNMFMDSSA GPRVQSATVF QDDSLGLDEA ASAEE