SAR1B_MOUSE
ID SAR1B_MOUSE Reviewed; 198 AA.
AC Q9CQC9; Q3UBL6;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=GTP-binding protein SAR1b {ECO:0000305};
GN Name=Sar1b {ECO:0000303|PubMed:33186557, ECO:0000312|MGI:MGI:1913647};
GN Synonyms=Sara1b, Sara2;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Hippocampus, Kidney, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH PREB, AND SUBCELLULAR LOCATION.
RX PubMed=11422940; DOI=10.1034/j.1600-0854.2001.20704.x;
RA Weissman J.T., Plutner H., Balch W.E.;
RT "The mammalian guanine nucleotide exchange factor mSec12 is essential for
RT activation of the Sar1 GTPase directing endoplasmic reticulum export.";
RL Traffic 2:465-475(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 DISRUPTION PHENOTYPE.
RX PubMed=33186557; DOI=10.1016/j.cmet.2020.10.020;
RA Wang X., Wang H., Xu B., Huang D., Nie C., Pu L., Zajac G.J.M., Yan H.,
RA Zhao J., Shi F., Emmer B.T., Lu J., Wang R., Dong X., Dai J., Zhou W.,
RA Wang C., Gao G., Wang Y., Willer C., Lu X., Zhu Y., Chen X.W.;
RT "Receptor-mediated ER export of lipoproteins controls lipid homeostasis in
RT mice and humans.";
RL Cell Metab. 33:350-366(2021).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=33964306; DOI=10.1016/j.jlr.2021.100085;
RA Auclair N., Sane A.T., Ahmarani L., Patey N., Beaulieu J.F., Peretti N.,
RA Spahis S., Levy E.;
RT "Sar1b mutant mice recapitulate gastrointestinal abnormalities associated
RT with chylomicron retention disease.";
RL J. Lipid Res. 62:100085-100085(2021).
CC -!- FUNCTION: GTP-binding protein involved in transport from the
CC endoplasmic reticulum to the Golgi apparatus. Activated by the guanine
CC nucleotide exchange factor PREB. Involved in the selection of the
CC protein cargo and the assembly of the COPII coat complex (By
CC similarity). Synergizes with the cargo receptor SURF4 to mediate the
CC export of lipoproteins from the endoplasmic reticulum, thereby
CC regulating lipoprotein delivery and the maintenance of lipid
CC homeostasis (By similarity). {ECO:0000250|UniProtKB:Q9QVY3,
CC ECO:0000250|UniProtKB:Q9Y6B6}.
CC -!- SUBUNIT: Homodimer (By similarity). Binds PREB (PubMed:11422940). Part
CC of the COPII coat complex. Binds to the cytoplasmic tails of target
CC proteins in the endoplasmic reticulum (By similarity). Interacts with
CC SURF4 (By similarity). {ECO:0000250|UniProtKB:Q9QVY3,
CC ECO:0000250|UniProtKB:Q9Y6B6, ECO:0000269|PubMed:11422940}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11422940}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11422940}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:11422940}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11422940}. Note=Associated with the endoplasmic
CC reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi
CC region. {ECO:0000250|UniProtKB:Q9QVY3}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality during late-gestation
CC (PubMed:33964306). Mice display gastrointestinal abnormalities
CC associated with chylomicron retention disease: they show lower plasma
CC levels of triglycerides, total cholesterol, and HDL-cholesterol, along
CC with reduced chylomicron secretion following gastric lipid gavage
CC (PubMed:33964306). Conditional deletion in the liver depletes plasma
CC lipids (PubMed:33186557). {ECO:0000269|PubMed:33186557,
CC ECO:0000269|PubMed:33964306}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; AK002327; BAB22015.1; -; mRNA.
DR EMBL; AK010187; BAB26755.1; -; mRNA.
DR EMBL; AK013559; BAB28905.1; -; mRNA.
DR EMBL; AK150906; BAE29948.1; -; mRNA.
DR EMBL; BC082550; AAH82550.1; -; mRNA.
DR CCDS; CCDS24661.1; -.
DR RefSeq; NP_079811.1; NM_025535.2.
DR AlphaFoldDB; Q9CQC9; -.
DR SMR; Q9CQC9; -.
DR BioGRID; 211441; 2.
DR STRING; 10090.ENSMUSP00000020653; -.
DR iPTMnet; Q9CQC9; -.
DR PhosphoSitePlus; Q9CQC9; -.
DR EPD; Q9CQC9; -.
DR jPOST; Q9CQC9; -.
DR MaxQB; Q9CQC9; -.
DR PaxDb; Q9CQC9; -.
DR PRIDE; Q9CQC9; -.
DR ProteomicsDB; 256704; -.
DR TopDownProteomics; Q9CQC9; -.
DR Antibodypedia; 26317; 278 antibodies from 33 providers.
DR DNASU; 66397; -.
DR Ensembl; ENSMUST00000020653; ENSMUSP00000020653; ENSMUSG00000020386.
DR GeneID; 66397; -.
DR KEGG; mmu:66397; -.
DR UCSC; uc007iup.2; mouse.
DR CTD; 51128; -.
DR MGI; MGI:1913647; Sar1b.
DR VEuPathDB; HostDB:ENSMUSG00000020386; -.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000160154; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q9CQC9; -.
DR OMA; FRWVAQY; -.
DR OrthoDB; 1168548at2759; -.
DR PhylomeDB; Q9CQC9; -.
DR TreeFam; TF312890; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 66397; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Sar1b; mouse.
DR PRO; PR:Q9CQC9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQC9; protein.
DR Bgee; ENSMUSG00000020386; Expressed in triceps brachii and 257 other tissues.
DR ExpressionAtlas; Q9CQC9; baseline and differential.
DR Genevisible; Q9CQC9; MM.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR GO; GO:0032368; P:regulation of lipid transport; ISS:UniProtKB.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR006687; Small_GTPase_SAR1.
DR PANTHER; PTHR45684; PTHR45684; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51422; SAR1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..198
FT /note="GTP-binding protein SAR1b"
FT /id="PRO_0000206262"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 58
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 75
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT BINDING 180..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9QVY3"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6B6"
SQ SEQUENCE 198 AA; 22382 MW; 9D0173C53FCD7A6B CRC64;
MSFIFDWIYS GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV DCADHERLLE SKEELDSLMT
DETIANVPIL ILGNKIDRPE AISEERLREM FGLYGQTTGK GSVSLKELNA RPLEVFMCSV
LKRQGYGEGF RWMAQYID
