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Protein

GTP-binding protein SAR1b

Gene

SAR1B

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Activated by the guanine nucleotide exchange factor PREB. Involved in the selection of the protein cargo and the assembly of the COPII coat complex.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Magnesium
Metal bindingi75 – 751Magnesium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398GTPBy similarity
Nucleotide bindingi75 – 784GTPBy similarity
Nucleotide bindingi134 – 1374GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein SAR1b
Short name:
Sar1
Gene namesi
Name:SAR1B
Synonyms:SAR1, SARA2
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51F → D: Decreases recruitment to the endoplasmic reticulum. 1 Publication
Mutagenesisi15 – 195VLQFL → AAAA: Blocks export of proteins from the ER to the Golgi. No effect on nucleotide binding. Abolishes localization to the endoplasmic reticulum. 1 Publication
Mutagenesisi39 – 391T → N: Lowers affinity for GTP, but not for GDP. Inhibits export of proteins from the ER to the Golgi. 1 Publication
Mutagenesisi158 – 1581T → A: Blocks export of proteins from the ER to the Golgi. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198GTP-binding protein SAR1bPRO_0000206260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9QVY3.

Interactioni

Subunit structurei

Homodimer. Binds PREB. Part of the COPII coat complex. Binds to the cytoplasmic tails of target proteins in the endoplasmic reticulum.1 Publication

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 185Combined sources
Beta strandi26 – 338Combined sources
Helixi38 – 458Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 768Combined sources
Beta strandi79 – 813Combined sources
Helixi85 – 928Combined sources
Beta strandi94 – 1018Combined sources
Helixi105 – 1073Combined sources
Helixi108 – 11912Combined sources
Helixi122 – 1243Combined sources
Beta strandi129 – 1346Combined sources
Helixi144 – 1518Combined sources
Turni154 – 1563Combined sources
Turni165 – 1673Combined sources
Beta strandi173 – 1775Combined sources
Turni180 – 1834Combined sources
Helixi186 – 1949Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6BX-ray1.70A/B1-198[»]
2FA9X-ray2.50A/B10-198[»]
2FMXX-ray1.82A/B10-198[»]
ProteinModelPortaliQ9QVY3.
SMRiQ9QVY3. Positions 13-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QVY3.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. SAR1 family.Curated

Phylogenomic databases

HOVERGENiHBG104997.
KOiK07953.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR006689. Small_GTPase_ARF/SAR.
IPR006687. Small_GTPase_SAR1.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51422. SAR1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QVY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFIFDWIYS GFSSVLQFLG LYKKTGKLVF LGLDNAGKTT LLHMLKDDRL
60 70 80 90 100
GQHVPTLHPT SEELTIAGMT FTTFDLGGHI QARRVWKNYL PAINGIVFLV
110 120 130 140 150
DCADHERLLE SKEELDSLMT DETIANVPIL ILGNKIDRPE AISEERLREM
160 170 180 190
FGLYGQTTGK GSVSLKELNA RPLEVFMCSV LKRQGYGEGF RWMAQYID
Length:198
Mass (Da):22,410
Last modified:May 1, 2000 - v1
Checksum:i6056769070CE91FA
GO

Sequence databases

RefSeqiXP_003498539.1. XM_003498491.2.
XP_007611226.1. XM_007613036.1.
XP_007611227.1. XM_007613037.1.
XP_007626894.1. XM_007628704.1.

Genome annotation databases

GeneIDi100758826.
KEGGicge:100758826.

Cross-referencesi

Sequence databases

RefSeqiXP_003498539.1. XM_003498491.2.
XP_007611226.1. XM_007613036.1.
XP_007611227.1. XM_007613037.1.
XP_007626894.1. XM_007628704.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6BX-ray1.70A/B1-198[»]
2FA9X-ray2.50A/B10-198[»]
2FMXX-ray1.82A/B10-198[»]
ProteinModelPortaliQ9QVY3.
SMRiQ9QVY3. Positions 13-198.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9QVY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100758826.
KEGGicge:100758826.

Organism-specific databases

CTDi51128.

Phylogenomic databases

HOVERGENiHBG104997.
KOiK07953.

Miscellaneous databases

EvolutionaryTraceiQ9QVY3.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR006689. Small_GTPase_ARF/SAR.
IPR006687. Small_GTPase_SAR1.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51422. SAR1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments."
    Kuge O., Dascher C., Orci L., Rowe T., Amherdt M., Plutner H., Ravazzola M., Tanigawa G., Rothman J.E., Balch W.E.
    J. Cell Biol. 125:51-65(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, MUTAGENESIS OF THR-39, SUBCELLULAR LOCATION.
    Tissue: Ovary.
  2. "The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly."
    Aridor M., Fish K.N., Bannykh S., Weissman J., Roberts T.H., Lippincott-Schwartz J., Balch W.E.
    J. Cell Biol. 152:213-229(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Protein engineering for crystallization of the GTPase Sar1 that regulates ER vesicle budding."
    Huang M., Weissman J.T., Wang C., Balch W.E., Wilson I.A.
    Acta Crystallogr. D 58:700-703(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  4. "Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export."
    Huang M., Weissman J.T., Beraud-Dufour S., Luan P., Wang C., Chen W., Aridor M., Wilson I.A., Balch W.E.
    J. Cell Biol. 155:937-948(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 10-198 IN COMPLEX WITH GDP, MUTAGENESIS OF PHE-5; 15-VAL--LEU-19 AND THR-158, INTERACTION WITH PREB.

Entry informationi

Entry nameiSAR1B_CRIGR
AccessioniPrimary (citable) accession number: Q9QVY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.