ASTRC_MOUSE
ID ASTRC_MOUSE Reviewed; 662 AA.
AC Q8CI52; A0A1L1SSU1; Q8BI24;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein Aster-C {ECO:0000303|PubMed:30220461};
DE AltName: Full=GRAM domain-containing protein 1C;
GN Name=Gramd1c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-325.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-662.
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAINS GRAM AND
RP VAST/ASTER, AND GENE STRUCTURE.
RX PubMed=30220461; DOI=10.1016/j.cell.2018.08.033;
RA Sandhu J., Li S., Fairall L., Pfisterer S.G., Gurnett J.E., Xiao X.,
RA Weston T.A., Vashi D., Ferrari A., Orozco J.L., Hartman C.L.,
RA Strugatsky D., Lee S.D., He C., Hong C., Jiang H., Bentolila L.A.,
RA Gatta A.T., Levine T.P., Ferng A., Lee R., Ford D.A., Young S.G.,
RA Ikonen E., Schwabe J.W.R., Tontonoz P.;
RT "Aster proteins facilitate nonvesicular plasma membrane to ER cholesterol
RT transport in mammalian cells.";
RL Cell 175:514-529(2018).
CC -!- FUNCTION: Cholesterol transporter that mediates non-vesicular transport
CC of cholesterol from the plasma membrane (PM) to the endoplasmic
CC reticulum (ER) (PubMed:30220461). 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 (PubMed:30220461). Plays
CC a crucial role in cholesterol homeostasis and has the unique ability to
CC localize to the PM based on the level of membrane cholesterol
CC (PubMed:30220461). In lipid-poor conditions localizes to the ER
CC membrane and in response to excess cholesterol in the PM is recruited
CC to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which
CC is mediated by the GRAM domain (PubMed:30220461). At the EPCS, the
CC sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and
CC facilitates its transfer from the PM to ER (PubMed:30220461).
CC {ECO:0000269|PubMed:30220461}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30220461}; Single-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass
CC membrane protein {ECO:0000255}. 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). {ECO:0000269|PubMed:30220461}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver. Also found in the
CC testis. {ECO:0000269|PubMed:30220461}.
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:0000269|PubMed:30220461}.
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:0000269|PubMed:30220461}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37472.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC26506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC125098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK029543; BAC26506.1; ALT_INIT; mRNA.
DR EMBL; BC037472; AAH37472.1; ALT_INIT; mRNA.
DR RefSeq; NP_001165578.1; NM_001172107.1.
DR RefSeq; NP_705756.1; NM_153528.2.
DR RefSeq; XP_006521957.1; XM_006521894.2.
DR PDB; 7AZN; X-ray; 2.09 A; A=327-503.
DR PDBsum; 7AZN; -.
DR AlphaFoldDB; Q8CI52; -.
DR SMR; Q8CI52; -.
DR STRING; 10090.ENSMUSP00000036739; -.
DR iPTMnet; Q8CI52; -.
DR PhosphoSitePlus; Q8CI52; -.
DR MaxQB; Q8CI52; -.
DR PaxDb; Q8CI52; -.
DR PRIDE; Q8CI52; -.
DR ProteomicsDB; 271097; -.
DR ProteomicsDB; 359743; -.
DR Antibodypedia; 2647; 14 antibodies from 8 providers.
DR DNASU; 207798; -.
DR Ensembl; ENSMUST00000214098; ENSMUSP00000150056; ENSMUSG00000036292.
DR GeneID; 207798; -.
DR KEGG; mmu:207798; -.
DR UCSC; uc007zgt.2; mouse.
DR CTD; 54762; -.
DR MGI; MGI:2443024; Gramd1c.
DR VEuPathDB; HostDB:ENSMUSG00000036292; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000158013; -.
DR HOGENOM; CLU_015189_2_0_1; -.
DR InParanoid; Q8CI52; -.
DR OMA; VFWGTKI; -.
DR OrthoDB; 944155at2759; -.
DR PhylomeDB; Q8CI52; -.
DR TreeFam; TF327695; -.
DR BioGRID-ORCS; 207798; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Gramd1c; mouse.
DR PRO; PR:Q8CI52; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CI52; protein.
DR Bgee; ENSMUSG00000036292; Expressed in olfactory epithelium and 156 other tissues.
DR ExpressionAtlas; Q8CI52; baseline and differential.
DR Genevisible; Q8CI52; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA: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:0071397; P:cellular response to cholesterol; IDA: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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..662
FT /note="Protein Aster-C"
FT /id="PRO_0000287452"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 70..176
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 326..497
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 328..337
FT /evidence="ECO:0007829|PDB:7AZN"
FT HELIX 339..347
FT /evidence="ECO:0007829|PDB:7AZN"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 378..387
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:7AZN"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 414..426
FT /evidence="ECO:0007829|PDB:7AZN"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 432..442
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:7AZN"
FT STRAND 448..458
FT /evidence="ECO:0007829|PDB:7AZN"
FT HELIX 465..472
FT /evidence="ECO:0007829|PDB:7AZN"
FT HELIX 475..502
FT /evidence="ECO:0007829|PDB:7AZN"
SQ SEQUENCE 662 AA; 76009 MW; 2C9E72DF5929BB01 CRC64;
MEGALTARQI VNEGDSSLAT ELQEEPEESP GPVVDENIVS AKKQGQSTHN WSGDWSFWIS
SSTYKDRNEE YRQQFTHLPD SEKLIADYAC ALQKDILVQG RLYLSEKWLC FYSNIFRWET
TISIALKNIT FMTKEKTARL IPNAIQIITE GEKFFFTSFG ARDRSYLIIF RLWQNVLLDK
SLTRQEFWQL LQQNYGTELG LNAEEMEHLL SVEENVQPRS PGRSSVDDAG ERDEKFSKAV
SFTQESVSRA SETEPLDGNS PKRGLGKEDS QSERNVRKSP SLASEKRISR APSKSLDLNK
NEYLSLDKSS TSDSVDEENI PEKDLQGRLY INRVFHISAE RMFELLFTSS HFMQRFANSR
NIIDVVSTPW TVESGGNQLR TMTYTIVLSN PLTGKYTAAT EKQTLYKESR EAQFYLVDSE
VLTHDVPYHD YFYTLNRYCI VRSAKQRCRL RVSTDLKYRK QPWGLIKSLI EKNSWSSLES
YFKKLESDLL MEESVLSQSI EDAGKHSSLR RRRRTLNRTA EPVPKLSSQR SSTDLGFEAK
VDVTGKRKTV DSYDTALIVV MSIFLLLLVL LNVTLFLKLS KIEHATQSFY QLHLQGEKSL
NLVSDRFSRT ENIQKNKDQA HRLKGVLQDS IVMLEQLKSS LIMLQKTFDL LNKNKSGVAV
ES
