SAR1A_MOUSE
ID SAR1A_MOUSE Reviewed; 198 AA.
AC P36536;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=GTP-binding protein SAR1a;
GN Name=Sar1a; Synonyms=Sara, Sara1;
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 [MRNA].
RC STRAIN=LAF1;
RX PubMed=8262187; DOI=10.1016/0014-5793(93)80423-r;
RA Shen K.A., Hammond C.M., Moore H.P.;
RT "Molecular analysis of SAR1-related cDNAs from a mouse pituitary cell
RT line.";
RL FEBS Lett. 335:380-385(1993).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Involved in transport from the endoplasmic reticulum to the
CC Golgi apparatus. Required to maintain SEC16A localization at discrete
CC locations on the ER membrane perhaps by preventing its dissociation.
CC SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an
CC organized scaffold defining endoplasmic reticulum exit sites (ERES) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with B3GAT1. {ECO:0000250|UniProtKB:Q9NR31}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues including liver, heart,
CC brain, skeletal muscle and kidney.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L20294; AAA16323.1; -; mRNA.
DR AlphaFoldDB; P36536; -.
DR SMR; P36536; -.
DR STRING; 10090.ENSMUSP00000020285; -.
DR iPTMnet; P36536; -.
DR PhosphoSitePlus; P36536; -.
DR EPD; P36536; -.
DR jPOST; P36536; -.
DR MaxQB; P36536; -.
DR PaxDb; P36536; -.
DR PeptideAtlas; P36536; -.
DR PRIDE; P36536; -.
DR ProteomicsDB; 256703; -.
DR MGI; MGI:98230; Sar1a.
DR eggNOG; KOG0077; Eukaryota.
DR InParanoid; P36536; -.
DR PhylomeDB; P36536; -.
DR ChiTaRS; Sar1a; mouse.
DR PRO; PR:P36536; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P36536; protein.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:MGI.
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:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:1901303; P:negative regulation of cargo loading into COPII-coated vesicle; IDA:MGI.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IMP:MGI.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
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 Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..198
FT /note="GTP-binding protein SAR1a"
FT /id="PRO_0000206259"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 198 AA; 22371 MW; F3C93E570EE4EFDF CRC64;
MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLQMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLME SKVELNALMT
DETISNVPIL ILGNKIDRTD AISEEKLREI KGLYGQTTGK GNVTLKELNA RPMEVFMCSV
LKRQGYGEGF RWLSQYID
