ASTRA_RAT
ID ASTRA_RAT Reviewed; 723 AA.
AC Q3KR56; Q6Y8E7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Protein Aster-A {ECO:0000250|UniProtKB:Q8VEF1};
DE AltName: Full=EG1RVC;
DE AltName: Full=GRAM domain-containing protein 1A {ECO:0000305};
GN Name=Gramd1a {ECO:0000312|RGD:1311022};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-723, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD Charles River;
RX PubMed=15033532; DOI=10.1016/j.gene.2003.12.021;
RA Feng Y., Liang H.L., Wong-Riley M.;
RT "Differential gene expressions in the visual cortex of postnatal day 1
RT versus day 21 rats revealed by suppression subtractive hybridization.";
RL Gene 329:93-101(2004).
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). May play a
CC role in tumor progression (By similarity). Plays a role in autophagy
CC regulation and is required for biogenesis of the autophagosome. This
CC function in autophagy requires its cholesterol-transfer activity (By
CC similarity). {ECO:0000250|UniProtKB:Q8VEF1,
CC ECO:0000250|UniProtKB:Q96CP6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96CP6}; Single-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q96CP6}; Single-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:Q96CP6}. Note=In lipid-poor conditions localizes
CC to the ER membrane and in response to excess cholesterol in the PM is
CC recruited to the endoplasmic reticulum-plasma membrane contact sites
CC (EPCS) (By similarity). Localizes to distinct EPCS than GRAMD2A and
CC ESYT2/3 (By similarity). {ECO:0000250|UniProtKB:Q8VEF1,
CC ECO:0000250|UniProtKB:Q96CP6}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a significantly higher level in
CC postnatal day 1 (PND1) than in PND21 visual cortical.
CC {ECO:0000269|PubMed:15033532}.
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:Q8VEF1}.
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:Q8VEF1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05897.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO45419.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC105896; AAI05897.1; ALT_INIT; mRNA.
DR EMBL; AY171575; AAO45419.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014182.1; NM_001014160.1.
DR RefSeq; XP_006228897.1; XM_006228835.3.
DR AlphaFoldDB; Q3KR56; -.
DR SMR; Q3KR56; -.
DR STRING; 10116.ENSRNOP00000028660; -.
DR iPTMnet; Q3KR56; -.
DR PhosphoSitePlus; Q3KR56; -.
DR PaxDb; Q3KR56; -.
DR PRIDE; Q3KR56; -.
DR GeneID; 361550; -.
DR KEGG; rno:361550; -.
DR UCSC; RGD:1311022; rat.
DR CTD; 57655; -.
DR RGD; 1311022; Gramd1a.
DR eggNOG; KOG1032; Eukaryota.
DR HOGENOM; CLU_015189_1_0_1; -.
DR InParanoid; Q3KR56; -.
DR OrthoDB; 944155at2759; -.
DR PhylomeDB; Q3KR56; -.
DR TreeFam; TF327695; -.
DR PRO; PR:Q3KR56; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
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:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0032366; P:intracellular sterol transport; IBA:GO_Central.
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 Autophagy; Cell membrane; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..723
FT /note="Protein Aster-A"
FT /id="PRO_0000287448"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 93..160
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 370..541
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CP6"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CP6"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEF1"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CP6"
FT CONFLICT 287
FT /note="S -> G (in Ref. 2; AAO45419)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="E -> G (in Ref. 2; AAO45419)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="I -> T (in Ref. 2; AAO45419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 80684 MW; 4ED8576BE66A2EF4 CRC64;
MFDTTPHSGR SSPSSSPSLR KRLQLLPPSR PPSAPEPEPG TMVEKGSDSS SEKSGVSGTL
STQSLGSRNF IRNSKKMQSW YSMLCPTYKQ RNEDFRKLFS KLPEAERLIV DYSCALQREI
LLQGRLYLSE NWICFYSNIF RWETTISIQL KEVTCLKKEK TAKLIPNAIQ ICTESEKHFF
TSFGARDRCF LLIFRLWQNA LLEKTLSPRE LWHLVHQCYG SELGLTSEDE DYVCPLQLNG
LGSPKEVGDV IALSDISPSG AADRSQEPSP VGSRCGRVTP NLSRASSDAD HGAEEDKEDQ
TDSQLDASSS QTVTPVAEPL SAEPAPPDGP TSNLGPLDLL SREELLTDTS NSSSSTGEEG
DLAALLPDLS GRLLINSVFH VGAERLQQML FSDSPFLQGF LQQRKFTDVT LSPWSSDSKC
HQRRVLTYTI PISNQLGPKS ASVVETQTLF RRGPQAGGCV VDSEVLTQGI PYQDYFYTAH
RYCILGLARN KARLRVSSEI RYRKQPWSLV KSLIEKSSWT GIEDYFHHLD RELAKAEKVS
LEEGGKDARG LLSGLRRRKR PLSWRGHRDG PQHPDPDPCT QTSMHTSGSL SSRFSEPSVD
QGPGAGIPSA LVLISIVLIV LIALNALLFY RLWSLERTAH TFESWHSLAL AKGKFPQTAT
EWAEILALQK HFHSVEVHKW RQILRASVEL LDEMKFSLEK LHQGITVPDP PLDTQPHPDD
SFP
