ID A0A2K5D453_AOTNA Unreviewed; 152 AA.
AC A0A2K5D453;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Erlin {ECO:0000256|RuleBase:RU369041};
DE Short=SPFH domain-containing protein {ECO:0000256|RuleBase:RU369041};
DE AltName: Full=Endoplasmic reticulum lipid raft-associated protein {ECO:0000256|RuleBase:RU369041};
DE AltName: Full=Stomatin-prohibitin-flotillin-HflC/K domain-containing protein {ECO:0000256|RuleBase:RU369041};
GN Name=ERLIN2 {ECO:0000313|Ensembl:ENSANAP00000015724.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000015724.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000015724.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the endoplasmic reticulum-associated degradation
CC (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in
CC regulation of cellular cholesterol homeostasis by regulation the SREBP
CC signaling pathway. {ECO:0000256|RuleBase:RU369041}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369041}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU369041}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC {ECO:0000256|ARBA:ARBA00008164, ECO:0000256|RuleBase:RU369041}.
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DR AlphaFoldDB; A0A2K5D453; -.
DR Ensembl; ENSANAT00000033566.1; ENSANAP00000015724.1; ENSANAG00000025720.1.
DR GeneTree; ENSGT00390000014666; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR033294; Erlin1/2.
DR PANTHER; PTHR15351; ERLIN (ER LIPID RAFT ASSOCIATED PROTEIN) HOMOLOG; 1.
DR PANTHER; PTHR15351:SF4; ERLIN-2; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
PE 3: Inferred from homology;
KW Cholesterol metabolism {ECO:0000256|RuleBase:RU369041};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU369041};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU369041};
KW Lipid metabolism {ECO:0000256|RuleBase:RU369041};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU369041};
KW Steroid metabolism {ECO:0000256|RuleBase:RU369041};
KW Sterol metabolism {ECO:0000256|RuleBase:RU369041};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..152
FT /note="Erlin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014462158"
FT DOMAIN 21..151
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 152 AA; 16842 MW; C4BE2B8942730A00 CRC64;
MAQLGAVVAV VSSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH LMLPFITSYK
SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV YDIVKNYTAD YDKALIFNKI
HHELNQFCSV HTLQEVYIEL FGLENDFSQE SS
//