SAR1B_BOVIN
ID SAR1B_BOVIN Reviewed; 198 AA.
AC Q3T0T7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=GTP-binding protein SAR1b {ECO:0000305};
GN Name=SAR1B {ECO:0000250|UniProtKB:Q9Y6B6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102266; AAI02267.1; -; mRNA.
DR RefSeq; NP_001030392.1; NM_001035315.2.
DR AlphaFoldDB; Q3T0T7; -.
DR SMR; Q3T0T7; -.
DR STRING; 9913.ENSBTAP00000028280; -.
DR PaxDb; Q3T0T7; -.
DR PeptideAtlas; Q3T0T7; -.
DR PRIDE; Q3T0T7; -.
DR Ensembl; ENSBTAT00000028280; ENSBTAP00000028280; ENSBTAG00000021226.
DR GeneID; 515999; -.
DR KEGG; bta:515999; -.
DR CTD; 51128; -.
DR VEuPathDB; HostDB:ENSBTAG00000021226; -.
DR VGNC; VGNC:34287; SAR1B.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000160154; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q3T0T7; -.
DR OMA; FRWVAQY; -.
DR OrthoDB; 1168548at2759; -.
DR TreeFam; TF312890; -.
DR Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR Reactome; R-BTA-5694530; Cargo concentration in the ER.
DR Reactome; R-BTA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000021226; Expressed in semitendinosus and 109 other tissues.
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_0000239866"
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; 22409 MW; 3F566E2BDC382CB5 CRC64;
MSFIFDWIYS GFSSVLQFLG LYKKTGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV DCADHERLLE SKEELDSLMT
DETVANVPIL ILGNKIDRPE AISEERLREM FGLYGQTTGK GNVSLKELNA RPLEVFMCSV
LKRQGYGEGF RWMAQYID
