ASTRB_MOUSE
ID ASTRB_MOUSE Reviewed; 738 AA.
AC Q80TI0; Q6NS56; Q8BZZ1; Q9CTQ2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein Aster-B {ECO:0000303|PubMed:30220461};
DE AltName: Full=GRAM domain-containing protein 1B;
GN Name=Gramd1b; Synonyms=Kiaa1201;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-158 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina, and 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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-30; SER-274; THR-584;
RP THR-585 AND THR-587, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP INDUCTION, DOMAINS GRAM AND 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 in the adrenal gland and has
CC the unique ability to localize to the PM based on the level of membrane
CC cholesterol (PubMed:30220461). In lipid-poor conditions localizes to
CC 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) which is mediated by the GRAM domain (PubMed:30220461). At the
CC EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in
CC the PM and facilitates its transfer from the PM to ER
CC (PubMed:30220461). {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80TI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TI0-2; Sequence=VSP_025473;
CC Name=3;
CC IsoId=Q80TI0-3; Sequence=VSP_025474;
CC Name=4;
CC IsoId=Q80TI0-4; Sequence=VSP_025475, VSP_025476;
CC -!- TISSUE SPECIFICITY: Highly expressed in the adrenal gland (at protein
CC level) and brain. Also found in the kidney, testis and macrophages.
CC {ECO:0000269|PubMed:30220461}.
CC -!- INDUCTION: By NR1H2/LXRB and NR1H3/LXRA. {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 -!- DISRUPTION PHENOTYPE: Mice exhibit deficiency in adrenal cholesterol
CC ester storage and steroidogenesis. {ECO:0000269|PubMed:30220461}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65747.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122465; BAC65747.1; ALT_INIT; mRNA.
DR EMBL; AK020827; BAB32220.1; -; mRNA.
DR EMBL; AK033156; BAC28174.1; -; mRNA.
DR EMBL; BC070451; AAH70451.1; -; mRNA.
DR CCDS; CCDS23081.1; -. [Q80TI0-4]
DR RefSeq; NP_766356.1; NM_172768.1. [Q80TI0-4]
DR RefSeq; XP_006510310.1; XM_006510247.3.
DR RefSeq; XP_006510314.1; XM_006510251.3.
DR RefSeq; XP_006510315.1; XM_006510252.3. [Q80TI0-2]
DR AlphaFoldDB; Q80TI0; -.
DR SMR; Q80TI0; -.
DR BioGRID; 231633; 3.
DR STRING; 10090.ENSMUSP00000130050; -.
DR iPTMnet; Q80TI0; -.
DR PhosphoSitePlus; Q80TI0; -.
DR EPD; Q80TI0; -.
DR jPOST; Q80TI0; -.
DR MaxQB; Q80TI0; -.
DR PaxDb; Q80TI0; -.
DR PeptideAtlas; Q80TI0; -.
DR PRIDE; Q80TI0; -.
DR ProteomicsDB; 271093; -. [Q80TI0-1]
DR ProteomicsDB; 271094; -. [Q80TI0-2]
DR ProteomicsDB; 271095; -. [Q80TI0-3]
DR ProteomicsDB; 271096; -. [Q80TI0-4]
DR Antibodypedia; 2247; 67 antibodies from 18 providers.
DR DNASU; 235283; -.
DR Ensembl; ENSMUST00000045682; ENSMUSP00000048126; ENSMUSG00000040111. [Q80TI0-4]
DR Ensembl; ENSMUST00000118159; ENSMUSP00000112417; ENSMUSG00000040111. [Q80TI0-2]
DR Ensembl; ENSMUST00000121357; ENSMUSP00000112564; ENSMUSG00000040111. [Q80TI0-3]
DR Ensembl; ENSMUST00000165104; ENSMUSP00000130050; ENSMUSG00000040111. [Q80TI0-4]
DR GeneID; 235283; -.
DR KEGG; mmu:235283; -.
DR UCSC; uc009ozn.1; mouse. [Q80TI0-4]
DR UCSC; uc009ozo.1; mouse. [Q80TI0-3]
DR UCSC; uc009ozp.1; mouse. [Q80TI0-1]
DR CTD; 57476; -.
DR MGI; MGI:1925037; Gramd1b.
DR VEuPathDB; HostDB:ENSMUSG00000040111; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000156649; -.
DR HOGENOM; CLU_015189_1_0_1; -.
DR InParanoid; Q80TI0; -.
DR OMA; PGGFAFY; -.
DR OrthoDB; 944155at2759; -.
DR PhylomeDB; Q80TI0; -.
DR TreeFam; TF327695; -.
DR BioGRID-ORCS; 235283; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gramd1b; mouse.
DR PRO; PR:Q80TI0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80TI0; protein.
DR Bgee; ENSMUSG00000040111; Expressed in retinal neural layer and 220 other tissues.
DR ExpressionAtlas; Q80TI0; baseline and differential.
DR Genevisible; Q80TI0; 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; IMP:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; 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:0042632; P:cholesterol homeostasis; IMP: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 Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..738
FT /note="Protein Aster-B"
FT /id="PRO_0000287450"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 96..163
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 372..543
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3KR37"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KR37"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KR37"
FT MOD_RES 584
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 587
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025473"
FT VAR_SEQ 1..8
FT /note="MKGFKLSC -> MASS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025474"
FT VAR_SEQ 1..8
FT /note="MKGFKLSC -> MPAANMMENLQLPALQVPEPQGAPEGSAVWSSSSTPTLRR
FT RRFKMRRMKNVQEQSLEAGLVAPDLPGVLAPGKEFLQLPSIEITPSSDEDTPWSNCSTP
FT SASPRRKRFLLRKWLRVRERKECSESSSQQSSQQSSHDDDSSRFLSPRVRDES (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025475"
FT VAR_SEQ 631..634
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025476"
SQ SEQUENCE 738 AA; 85355 MW; DF329AE53B090858 CRC64;
MKGFKLSCTA SNSNRSTPAC SPILRKRSRS PTPQNQDGDT MVEKGSDHSS DKSPSTPEQG
VQRSCSSQSG RSGGKNSKKS QSWYNVLSPT YKQRNEDFRK LFKQLPDTER LIVDYSCALQ
RDILLQGRLY LSENWICFYS NIFRWETLLT VRLKDICSMT KEKTARLIPN AIQVCTDSEK
HFFTSFGARD RTYMMMFRLW QNALLEKPLC PKELWHFVHQ CYGNELGLTS DDEDYVPPDD
DFNTMGYCEE IPIEENEVND SSSKSSIETK PDASPQLPKK SITNSTLTST GSSEAPVSFD
GLPLEEEVME GDGSLEKELA IDNIIGEKIE IMAPVTSPSL DFNDNEDIPT ELSDSSDTHD
EGEVQAFYED LSGRQYVNEV FNFSVDKLYD LLFTNSPFLR DFMEQRRFSD IIFHPWKKEE
NGNQSRVILY TITLTNPLAP KTATVRETQT MYKASQESEC YVIDAEVLTH DVPYHDYFYT
INRYTLTRVA RNKSRLRVST ELRYRKQPWG FVKTFIEKNF WSGLEDYFRH LETELTKTES
TYLAEIHRQS PKEKASKSSA VRRRKRPHAH LRVPHLEEVM SPVTTPTDED VGHRIKHVAG
STQTRHIPED TPDGFHLQSV SKLLLVISCV ICFSLVLLVV LNMMLFYKLW MLEYTTQTLT
AWQGLRLQER LPQSQTEWAQ LLESQQKYHD TELQKWREII KSSVLLLDQM KDSLINLQNG
IRSRDYTAES DEKRNRYH
