ASTRC_PONAB
ID ASTRC_PONAB Reviewed; 662 AA.
AC Q5RC33;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Protein Aster-C {ECO:0000250|UniProtKB:Q8CI52};
DE AltName: Full=GRAM domain-containing protein 1C;
GN Name=GRAMD1C;
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: Cholesterol transporter that mediates non-vesicular transport
CC of cholesterol from the plasma membrane (PM) to the endoplasmic
CC reticulum (ER) (By similarity). Contains unique domains for binding
CC cholesterol and the PM, thereby serving as a molecular bridge for the
CC transfer of cholesterol from the PM to the ER (By similarity). Plays a
CC crucial role in cholesterol homeostasis and has the unique ability to
CC localize to the PM based on the level of membrane cholesterol (By
CC similarity). In lipid-poor conditions localizes to the ER membrane and
CC in response to excess cholesterol in the PM is recruited to the
CC endoplasmic reticulum-plasma membrane contact sites (EPCS) which is
CC mediated by the GRAM domain (By similarity). At the EPCS, the sterol-
CC binding VASt/ASTER domain binds to the cholesterol in the PM and
CC facilitates its transfer from the PM to ER (By similarity).
CC {ECO:0000250|UniProtKB:Q8CI52}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8CI52}; Single-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8CI52}; Single-
CC pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions
CC localizes to the ER membrane and in response to excess cholesterol in
CC the PM is recruited to the endoplasmic reticulum-plasma membrane
CC contact sites (EPCS). {ECO:0000250|UniProtKB:Q8CI52}.
CC -!- DOMAIN: GRAM domain binds phosphatidylserine in the PM and mediates
CC protein recruitment to endoplasmic reticulum-plasma membrane contact
CC sites (EPCS) in response to excess cholesterol in the PM.
CC {ECO:0000250|UniProtKB:Q8CI52}.
CC -!- DOMAIN: VASt (VAD1 Analog of StAR-related lipid transfer) domain, also
CC known as ASTER (Greek for star) domain is a sterol-binding domain.
CC {ECO:0000250|UniProtKB:Q8CI52}.
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DR EMBL; CR858449; CAH90677.1; -; mRNA.
DR RefSeq; NP_001125369.1; NM_001131897.2.
DR AlphaFoldDB; Q5RC33; -.
DR SMR; Q5RC33; -.
DR STRING; 9601.ENSPPYP00000015133; -.
DR GeneID; 100172272; -.
DR KEGG; pon:100172272; -.
DR CTD; 54762; -.
DR eggNOG; KOG1032; Eukaryota.
DR InParanoid; Q5RC33; -.
DR OrthoDB; 944155at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR031968; VASt.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00568; GRAM; 1.
DR PROSITE; PS51778; VAST; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Lipid transport; Lipid-binding;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..662
FT /note="Protein Aster-C"
FT /id="PRO_0000287453"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..136
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 326..497
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 76115 MW; F0091D372D6B0C39 CRC64;
MEGAPTVRQV MNEGDSSLAT ELQEDVEENP SPTVEENNVV VKKQGPNLHN WSGDWSFWIS
SSTYKDRNEE YRRQFTHLPD TERLIADYAC ALQRDILLQG RLYLSENWLC FYSNIFRWET
TISIALKNIT FMTKEKTARL IPNAIQIVTE SEKFFFTSFG ARDRSYLSIF RLWQNVLLDK
SLTRQEFWQL LQQNYGTELG LNAEEMENLS LSIEDVRPRS PGRSSLDDSG ERDEKLSKSI
SFTSESISRV SETESFDGNS SKGGLGKEES QNEKQTKKSL LPTLEKKLTR VPSKSLDLNK
NEYLSLEKSS TSDSVDEENV PEKDLHGRLF INRIFHISAD RMFELLFTSS RFMQKFASSR
NIIDVVSTPW TAELGGDQLR TMTYTIVLNS PLTGKCTAAT EKQTLYKESR EARFYMVDSE
VLTHDVPYHD YFYTVDRYCI IRSSKQKCRL RVSTDLKYRK QPWGLVKSLI EKNSWGSLED
YFKHLESDLL IEESILNQAI EDPGKLTGLR RRRRTFNRTA ETVPKLSSQH SSGDVGLGTK
ADITGKKKEM ENYNITLIVV MSIFVLLLVL LNVTLFLKLS KIEHAAQSFY RLRLQEEKSL
NLASDVVSRA ETIQNNKDQA HRLKGVLRDS IVMLEQLKSS LIMLQKTFDL LNKNKTGMAV
ES
