ID   ERLN1_PONAB             Reviewed;         348 AA.
AC   Q5RCJ9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 3.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Erlin-1 {ECO:0000250|UniProtKB:O75477};
DE   AltName: Full=Endoplasmic reticulum lipid raft-associated protein 1;
DE   AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1;
DE            Short=SPFH domain-containing protein 1;
GN   Name=ERLIN1 {ECO:0000250|UniProtKB:O75477}; Synonyms=SPFH1;
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). Involved in regulation of cellular
CC       cholesterol homeostasis by regulation the SREBP signaling pathway.
CC       Binds cholesterol and may promote ER retention of the SCAP-SREBF
CC       complex (By similarity). {ECO:0000250|UniProtKB:O75477}.
CC   -!- SUBUNIT: Forms a heteromeric complex with ERLIN2. In complex with
CC       ERLIN2, interacts with RNF170. Interacts with AMFR and SYVN1 (By
CC       similarity). {ECO:0000250|UniProtKB:O75477}.
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}.
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DR   EMBL; CR858271; CAH90508.1; -; mRNA.
DR   RefSeq; NP_001125267.1; NM_001131795.1.
DR   AlphaFoldDB; Q5RCJ9; -.
DR   Ensembl; ENSPPYT00000059003; ENSPPYP00000034475; ENSPPYG00000002560.
DR   GeneID; 100172164; -.
DR   KEGG; pon:100172164; -.
DR   CTD; 10613; -.
DR   GeneTree; ENSGT00390000014666; -.
DR   InParanoid; Q5RCJ9; -.
DR   Proteomes; UP000001595; Chromosome 10.
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:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032933; P:SREBP signaling pathway; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Cholesterol metabolism; Endoplasmic reticulum; Glycoprotein;
KW   Lipid metabolism; Lipid-binding; Membrane; Reference proteome;
KW   Signal-anchor; Steroid metabolism; Sterol metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..348
FT                   /note="Erlin-1"
FT                   /id="PRO_0000002786"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          321..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75477"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   348 AA;  39209 MW;  DAB1FEADBE97F81E CRC64;
     MNMTQARVLV AAVVGLVAVL LYASIHKIEE GHLAVYYRGG ALLTSPSGPG YHIMLPFITT
     FRSVQTTLQT DEVKNVPCGT SGGVMIYIDR IEVVNMLAPY AVFDIVRNYT ADYDKTLIFN
     KIHHELNQFC SAHTLQEVYI ELFDQIDENL KQALQKDLNL MAPGLTIQAV RVTKPKIPEA
     IRRNFELMEA EKTKLLIAAQ KQKVVEKEAE TERKKAVIEA EKIAQVAKIR FQQKVMEKET
     EKRISEIEDA AFLAREKAKA DAEYYAAHKY ATSNKHKLTP EYLELKKYQA IASNSKIYFG
     SNIPNMFVDS SCALKYSDIR TGRESSHPSK EALEPSGENL IQNKESTG