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FLASH GENE
Symbol SAR1A contributors: mct - updated : 31-01-2017
HGNC name SAR1a gene homolog 1 (S. cerevisiae)
HGNC id 10534
DNA
TYPE functioning gene
STRUCTURE 20.33 kb     8 Exon(s)
MAPPING cloned Y linked N status provisional
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
7 - 3018 - 198 - 2010 20624903
8 - 3088 - 198 - 2010 20624903
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Cardiovascularheart   highly
Digestivemouthtongue   
Lymphoid/Immunelymph node   highly
Nervousnerve   highly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Muscularstriatumskeletal  
cell lineage
cell lines
fluid/secretion
at STAGE
physiological period fetal
Text eye
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal amphipathic alpha helix
  • conserved residues located on a unique C-terminal loop involved in SAR1A organization
  • HOMOLOGY
    interspecies homolog to S.cerevisiae Sar1a
    intraspecies paralog to SAR1B
    homolog to ZFYVE16
    Homologene
    FAMILY
  • small GTPase superfamily
  • SAR1 family
  • CATEGORY transport carrier
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    basic FUNCTION
  • involved in transport from the endoplasmic reticulum to the golgi apparatus
  • regulates cell surface expression of CASR
  • SAR1A organization regulates membrane constriction
  • controls the assembly and fission of COPII vesicles
  • play critical roles in the assembly and budding of COPII-coated vesicles in the ER
  • SAR1A GTPase activity is critical for procollagen export
  • SAR1A and SAR1B proteins lower membrane rigidity at low concentrations, and at high concentrations, increase membrane rigidity
  • SAR1A, SAR1B GTPase coordinates the assembly of coat protein complex-II (COPII) at specific sites of the endoplasmic reticulum (ER)
  • SAR1A antagonizes the lipoprotein secretion-promoting activity of SAR1B, both isoforms modulate the expression of genes encoding cholesterol biosynthetic enzymes and the synthesis of cholesterol (
  • SAR1A, SAR1B dimerization is responsible for the formation of constrictive membrane curvature
  • activated SAR1A introduces membrane curvature through its N-terminal amphiphatic helix at the ER-mitochondria interphase and thereby reducing contact size
  • regulates the size of ER-mitochondria contact sites through its effects on membrane curvature
  • GTPase cycle of SAR1A appears to be responsible for collagen VII exit from the ER
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • during COPII assembly, SAR1A deforms the membrane and recruits the SEC23A-SEC24A complex (SEC23/24), which is the primary cargo-binding adaptor for the system
  • TRAPPC2 bound and promoted efficient cycling of SAR1A, a guanosine triphosphatase that can constrict membranes, and thus allowed nascent carriers to grow and incorporate PC prefibrils
  • recruitment of PREB by MIA2 contributes to efficient activation of SAR1A in the vicinity of ER exit sites
  • MIA2 complex interacts with the GEF and the GAP of SAR1A and tightly regulates its GTPase cycle to accomplish large cargo secretion
  • cell & other
    REGULATION
    induced by Hydroxyurea (HU), (HU induces SAR1A, which in turn activates gamma-globin expression, predominantly through the Gialpha/JNK/Jun pathway
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    attenuates cell surface expression of CASR
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    bloodhemoglobin 
    SAR1A is an alternative therapeutic target for beta-globin disorders
    ANIMAL & CELL MODELS