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SAR1A_PIG
ID   SAR1A_PIG               Reviewed;         198 AA.
AC   Q52NJ3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=GTP-binding protein SAR1a;
GN   Name=SAR1A;
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 [LARGE SCALE MRNA].
RA   Liu G.Y., Xiong Z.Y.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in transport from the endoplasmic reticulum to the
CC       Golgi apparatus. Required to maintain SEC16A localization at discrete
CC       locations on the ER membrane perhaps by preventing its dissociation.
CC       SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an
CC       organized scaffold defining endoplasmic reticulum exit sites (ERES) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with B3GAT1. {ECO:0000250|UniProtKB:Q9NR31}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC       apparatus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC       {ECO:0000305}.
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DR   EMBL; AY996812; AAY17508.1; -; mRNA.
DR   RefSeq; NP_001026956.1; NM_001031786.1.
DR   RefSeq; XP_005657450.1; XM_005657393.2.
DR   RefSeq; XP_005657451.1; XM_005657394.2.
DR   AlphaFoldDB; Q52NJ3; -.
DR   SMR; Q52NJ3; -.
DR   STRING; 9823.ENSSSCP00000010938; -.
DR   PaxDb; Q52NJ3; -.
DR   PeptideAtlas; Q52NJ3; -.
DR   PRIDE; Q52NJ3; -.
DR   Ensembl; ENSSSCT00000048887; ENSSSCP00000039382; ENSSSCG00000010260.
DR   Ensembl; ENSSSCT00005022381; ENSSSCP00005013404; ENSSSCG00005014369.
DR   Ensembl; ENSSSCT00005022424; ENSSSCP00005013432; ENSSSCG00005014369.
DR   Ensembl; ENSSSCT00005022449; ENSSSCP00005013450; ENSSSCG00005014369.
DR   Ensembl; ENSSSCT00005022466; ENSSSCP00005013464; ENSSSCG00005014369.
DR   Ensembl; ENSSSCT00015011505; ENSSSCP00015004545; ENSSSCG00015008721.
DR   Ensembl; ENSSSCT00015011702; ENSSSCP00015004613; ENSSSCG00015008721.
DR   Ensembl; ENSSSCT00015011765; ENSSSCP00015004643; ENSSSCG00015008721.
DR   Ensembl; ENSSSCT00015011834; ENSSSCP00015004674; ENSSSCG00015008721.
DR   Ensembl; ENSSSCT00025102577; ENSSSCP00025045404; ENSSSCG00025074388.
DR   Ensembl; ENSSSCT00030096926; ENSSSCP00030044684; ENSSSCG00030069190.
DR   Ensembl; ENSSSCT00035038239; ENSSSCP00035015256; ENSSSCG00035028884.
DR   Ensembl; ENSSSCT00040037980; ENSSSCP00040015839; ENSSSCG00040028216.
DR   Ensembl; ENSSSCT00045023669; ENSSSCP00045016348; ENSSSCG00045013863.
DR   Ensembl; ENSSSCT00050053942; ENSSSCP00050022714; ENSSSCG00050039932.
DR   Ensembl; ENSSSCT00055061375; ENSSSCP00055049240; ENSSSCG00055030759.
DR   Ensembl; ENSSSCT00060081404; ENSSSCP00060035247; ENSSSCG00060059655.
DR   Ensembl; ENSSSCT00065099938; ENSSSCP00065043885; ENSSSCG00065072673.
DR   Ensembl; ENSSSCT00070016497; ENSSSCP00070013664; ENSSSCG00070008532.
DR   Ensembl; ENSSSCT00070016507; ENSSSCP00070013671; ENSSSCG00070008532.
DR   Ensembl; ENSSSCT00070016512; ENSSSCP00070013675; ENSSSCG00070008532.
DR   GeneID; 595115; -.
DR   KEGG; ssc:595115; -.
DR   CTD; 56681; -.
DR   VGNC; VGNC:92579; SAR1A.
DR   eggNOG; KOG0077; Eukaryota.
DR   GeneTree; ENSGT00940000155276; -.
DR   HOGENOM; CLU_040729_6_0_1; -.
DR   InParanoid; Q52NJ3; -.
DR   OMA; DDRIAQH; -.
DR   OrthoDB; 1168548at2759; -.
DR   TreeFam; TF312890; -.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Proteomes; UP000314985; Chromosome 14.
DR   Bgee; ENSSSCG00000010260; Expressed in granulosa cell and 46 other tissues.
DR   ExpressionAtlas; Q52NJ3; baseline and differential.
DR   Genevisible; Q52NJ3; 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:0005794; C:Golgi apparatus; 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:0090110; P:COPII-coated vesicle cargo loading; IEA:Ensembl.
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: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: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   Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..198
FT                   /note="GTP-binding protein SAR1a"
FT                   /id="PRO_0000249776"
FT   BINDING         32..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..78
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         139
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR31"
SQ   SEQUENCE   198 AA;  22409 MW;  17603DDDEE224D68 CRC64;
     MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
     SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHPRLME SKVELNALMT
     DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV
     LKRQGYGEGF RWLSQYID
 
 
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