位置:首页 > 蛋白库 > SAR1B_PIG
SAR1B_PIG
ID   SAR1B_PIG               Reviewed;         198 AA.
AC   Q5PYH3; Q4ZJK0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=GTP-binding protein SAR1b {ECO:0000305};
GN   Name=SAR1B {ECO:0000303|PubMed:16621763};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16621763; DOI=10.1080/10495390600608794;
RA   Wang X.M., Liu B., Zhao S.H., Fan B., Zhu M.J., Yu M., Xiong T.A., Li K.;
RT   "Sequence identification, tissue distribution, mapping and polymorphism of
RT   the porcine sar1b gene.";
RL   Anim. Biotechnol. 17:99-107(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y., Xiong Z.Y.;
RL   Submitted (APR-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}.
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; AY819557; AAV68380.1; -; mRNA.
DR   EMBL; DQ002890; AAY23007.1; -; mRNA.
DR   RefSeq; NP_001008689.1; NM_001008689.2.
DR   AlphaFoldDB; Q5PYH3; -.
DR   SMR; Q5PYH3; -.
DR   STRING; 9823.ENSSSCP00000015216; -.
DR   PaxDb; Q5PYH3; -.
DR   PeptideAtlas; Q5PYH3; -.
DR   PRIDE; Q5PYH3; -.
DR   Ensembl; ENSSSCT00000054541; ENSSSCP00000042292; ENSSSCG00000014305.
DR   Ensembl; ENSSSCT00005047514; ENSSSCP00005029259; ENSSSCG00005029904.
DR   Ensembl; ENSSSCT00005047557; ENSSSCP00005029285; ENSSSCG00005029904.
DR   Ensembl; ENSSSCT00015033357; ENSSSCP00015013273; ENSSSCG00015024942.
DR   Ensembl; ENSSSCT00025064988; ENSSSCP00025027689; ENSSSCG00025047696.
DR   Ensembl; ENSSSCT00030006806; ENSSSCP00030003035; ENSSSCG00030005005.
DR   Ensembl; ENSSSCT00035072599; ENSSSCP00035029456; ENSSSCG00035054397.
DR   Ensembl; ENSSSCT00040018980; ENSSSCP00040007789; ENSSSCG00040014173.
DR   Ensembl; ENSSSCT00045025809; ENSSSCP00045017804; ENSSSCG00045015205.
DR   Ensembl; ENSSSCT00050106063; ENSSSCP00050046787; ENSSSCG00050077089.
DR   Ensembl; ENSSSCT00055022089; ENSSSCP00055017491; ENSSSCG00055011242.
DR   Ensembl; ENSSSCT00060060360; ENSSSCP00060025866; ENSSSCG00060044503.
DR   Ensembl; ENSSSCT00065078006; ENSSSCP00065033914; ENSSSCG00065056983.
DR   Ensembl; ENSSSCT00065078015; ENSSSCP00065033921; ENSSSCG00065056983.
DR   Ensembl; ENSSSCT00070041701; ENSSSCP00070035012; ENSSSCG00070020976.
DR   Ensembl; ENSSSCT00070041710; ENSSSCP00070035021; ENSSSCG00070020976.
DR   GeneID; 494017; -.
DR   KEGG; ssc:494017; -.
DR   CTD; 51128; -.
DR   VGNC; VGNC:92580; SAR1B.
DR   eggNOG; KOG0077; Eukaryota.
DR   GeneTree; ENSGT00940000160154; -.
DR   HOGENOM; CLU_040729_6_0_1; -.
DR   InParanoid; Q5PYH3; -.
DR   OMA; FRWVAQY; -.
DR   OrthoDB; 330236at2759; -.
DR   TreeFam; TF312890; -.
DR   Reactome; R-SSC-204005; COPII-mediated vesicle transport.
DR   Reactome; R-SSC-2132295; MHC class II antigen presentation.
DR   Reactome; R-SSC-5694530; Cargo concentration in the ER.
DR   Reactome; R-SSC-8963888; Chylomicron assembly.
DR   Reactome; R-SSC-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Proteomes; UP000314985; Chromosome 2.
DR   Bgee; ENSSSCG00000014305; Expressed in muscle tissue and 44 other tissues.
DR   ExpressionAtlas; Q5PYH3; baseline and differential.
DR   Genevisible; Q5PYH3; SS.
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_0000249778"
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"
FT   CONFLICT        93
FT                   /note="I -> V (in Ref. 2; AAY23007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   198 AA;  22382 MW;  3F566E2BCCD62245 CRC64;
     MSFIFDWIYS GFSSVLQFLG LYKKTGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
     SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV DCADHERLLE SKEELDSLMT
     DETVANVPIL ILGNKIDRPE AISEERLREM FGLYGQTTGK GSVSLKELNA RPLEVFMCSV
     LKRQGYGEGF RWMAQYID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024