SAR1B_RAT
ID SAR1B_RAT Reviewed; 198 AA.
AC Q5HZY2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=GTP-binding protein SAR1b {ECO:0000305};
GN Name=Sar1b {ECO:0000312|RGD:1305590};
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=Ovary;
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).
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. Binds PREB. Part of the COPII coat complex. Binds
CC to the cytoplasmic tails of target proteins in the endoplasmic
CC reticulum (By similarity). Interacts with SURF4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QVY3, ECO:0000250|UniProtKB:Q9Y6B6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9QVY3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9QVY3}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q9QVY3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9QVY3}. Note=Associated with the endoplasmic
CC reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi
CC region. {ECO:0000250|UniProtKB:Q9QVY3}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; BC088842; AAH88842.1; -; mRNA.
DR RefSeq; NP_001009622.1; NM_001009622.1.
DR AlphaFoldDB; Q5HZY2; -.
DR SMR; Q5HZY2; -.
DR STRING; 10116.ENSRNOP00000006567; -.
DR iPTMnet; Q5HZY2; -.
DR PhosphoSitePlus; Q5HZY2; -.
DR jPOST; Q5HZY2; -.
DR PaxDb; Q5HZY2; -.
DR PRIDE; Q5HZY2; -.
DR Ensembl; ENSRNOT00000006567; ENSRNOP00000006567; ENSRNOG00000004820.
DR GeneID; 287276; -.
DR KEGG; rno:287276; -.
DR UCSC; RGD:1305590; rat.
DR CTD; 51128; -.
DR RGD; 1305590; Sar1b.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000164397; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q5HZY2; -.
DR OMA; FRWVAQY; -.
DR OrthoDB; 1168548at2759; -.
DR PhylomeDB; Q5HZY2; -.
DR TreeFam; TF312890; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q5HZY2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004820; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q5HZY2; RN.
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 2: Evidence at transcript 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_0000312558"
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; 22410 MW; 3556769075CE9221 CRC64;
MSFIFDWIYS GFSSVLQFLG LYKKTGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHL QARRVWKNYL PAINGIVFLV DCADHERLLE SKEELDSLMT
DETIANVPIL ILGNKIDRPE AISEERLREM FGLYGQTTGK GSVSLKELNA RPLEVFMCSV
LKRQGYGEGF RWMAQYID
