ERLN_CAEEL
ID ERLN_CAEEL Reviewed; 312 AA.
AC A3QMC6;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Erlin {ECO:0000303|PubMed:22269071};
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein 1 {ECO:0000303|PubMed:22269071};
GN Name=erl-1 {ECO:0000303|PubMed:22269071, ECO:0000312|WormBase:C42C1.15};
GN ORFNames=C42C1.15 {ECO:0000312|WormBase:C42C1.15};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PHE-303.
RX PubMed=22269071; DOI=10.1186/1471-2121-13-2;
RA Hoegg M.B., Robbins S.M., McGhee J.D.;
RT "Characterization of the C. elegans erlin homologue.";
RL BMC Cell Biol. 13:2-2(2012).
CC -!- SUBUNIT: Seems to form a multimeric complex.
CC {ECO:0000269|PubMed:22269071}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22269071}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O75477}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline only.
CC {ECO:0000269|PubMed:22269071}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development (at protein
CC level) (PubMed:22269071). Highly expressed in embryos and L1 stage
CC larvae (at protein level) (PubMed:22269071).
CC {ECO:0000269|PubMed:22269071}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, with no change in growth
CC rate at 20 or 26 degrees Celsius, general morphology or lifespan
CC compared to wild-type (PubMed:22269071). Does not affect brood size,
CC embryonic development or defecation rates of itr-1 (sa73) mutants
CC (PubMed:22269071). No change in development or survival compared to
CC wild-type animals following exposure to ER stress inducing agents such
CC as tunicamycin and dithiothreitol (PubMed:22269071).
CC {ECO:0000269|PubMed:22269071}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
CC -!- CAUTION: Unlike mammalian homologs, does not play an essential role in
CC the endoplasmic reticulum-associated degradation (ERAD) of inositol
CC 1,4,5-triphosphate receptors (IP3Rs). {ECO:0000269|PubMed:22269071}.
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DR EMBL; BX284604; CAM36358.1; -; Genomic_DNA.
DR RefSeq; NP_502339.1; NM_069938.4.
DR AlphaFoldDB; A3QMC6; -.
DR SMR; A3QMC6; -.
DR STRING; 6239.C42C1.15; -.
DR EPD; A3QMC6; -.
DR PaxDb; A3QMC6; -.
DR PeptideAtlas; A3QMC6; -.
DR EnsemblMetazoa; C42C1.15.1; C42C1.15.1; WBGene00016592.
DR GeneID; 178178; -.
DR KEGG; cel:CELE_C42C1.15; -.
DR UCSC; C42C1.15; c. elegans.
DR CTD; 178178; -.
DR WormBase; C42C1.15; CE26912; WBGene00016592; erl-1.
DR eggNOG; KOG2962; Eukaryota.
DR GeneTree; ENSGT00390000014666; -.
DR HOGENOM; CLU_058701_0_0_1; -.
DR InParanoid; A3QMC6; -.
DR OMA; YNMVRNF; -.
DR OrthoDB; 930534at2759; -.
DR PhylomeDB; A3QMC6; -.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR PRO; PR:A3QMC6; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016592; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0032933; P:SREBP signaling pathway; IBA:GO_Central.
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.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..312
FT /note="Erlin"
FT /id="PRO_5002658006"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..312
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 303
FT /note="F->A: Fails to form multimeric complexes."
FT /evidence="ECO:0000305|PubMed:22269071"
SQ SEQUENCE 312 AA; 35325 MW; 390DEF4A9B247CE4 CRC64;
MLTELALGLF ALWIAIFSQA LHKIEEGHVG VYYRGGALLK AVTNPGYHMH IPFLTTVKSV
QVTLQTDEAT NVPCGTSGGV LIYFDRIEVV NFLSQDSVYA IVKNYTVDYD RPLIFNKVHH
EVNQFCSVHT LQEVYIDLFD KIDEEIKNAL QEDLVKMAPG LYVQAVRVTK PKIPEAIRLN
YEKMEAEKTK LLVAQETQKV VEKLAETERK KAVIEAEKAA QVALIHQKRL LSEKETEKLL
NQMEAESNLA SERSKADAEF YKAQKQADSN KILLTKEYLE LQKIRAIASN NKIYYGDSIP
QAFVMGTTQQ TV
