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GTP-binding protein SAR1b

 SAR1B_MOUSE             Reviewed;         198 AA.
Q9CQC9; Q3UBL6;
09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
05-DEC-2018, entry version 136.
RecName: Full=GTP-binding protein SAR1b;
Name=Sar1b; Synonyms=Sara1b, Sara2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, Hippocampus, Kidney, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH PREB, AND SUBCELLULAR LOCATION.
PubMed=11422940; DOI=10.1034/j.1600-0854.2001.20704.x;
Weissman J.T., Plutner H., Balch W.E.;
"The mammalian guanine nucleotide exchange factor mSec12 is essential
for activation of the Sar1 GTPase directing endoplasmic reticulum
export.";
Traffic 2:465-475(2001).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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.
-!- SUBUNIT: Homodimer. Part of the COPII coat complex. Binds to the
cytoplasmic tails of target proteins in the endoplasmic reticulum
(By similarity). Binds PREB. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11422940}; Peripheral membrane protein
{ECO:0000269|PubMed:11422940}. Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:11422940}; Peripheral membrane
protein {ECO:0000269|PubMed:11422940}. Note=Associated with the
endoplasmic reticulum and Golgi stacks, in particular in the
juxta-nuclear Golgi region.
-!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK002327; BAB22015.1; -; mRNA.
EMBL; AK010187; BAB26755.1; -; mRNA.
EMBL; AK013559; BAB28905.1; -; mRNA.
EMBL; AK150906; BAE29948.1; -; mRNA.
EMBL; BC082550; AAH82550.1; -; mRNA.
CCDS; CCDS24661.1; -.
RefSeq; NP_079811.1; NM_025535.2.
UniGene; Mm.196592; -.
ProteinModelPortal; Q9CQC9; -.
SMR; Q9CQC9; -.
BioGrid; 211441; 1.
STRING; 10090.ENSMUSP00000020653; -.
iPTMnet; Q9CQC9; -.
PhosphoSitePlus; Q9CQC9; -.
EPD; Q9CQC9; -.
MaxQB; Q9CQC9; -.
PaxDb; Q9CQC9; -.
PRIDE; Q9CQC9; -.
TopDownProteomics; Q9CQC9; -.
Ensembl; ENSMUST00000020653; ENSMUSP00000020653; ENSMUSG00000020386.
GeneID; 66397; -.
KEGG; mmu:66397; -.
UCSC; uc007iup.2; mouse.
CTD; 51128; -.
MGI; MGI:1913647; Sar1b.
eggNOG; KOG0077; Eukaryota.
eggNOG; ENOG410YIKI; LUCA.
GeneTree; ENSGT00940000160154; -.
HOGENOM; HOG000163690; -.
HOVERGEN; HBG104997; -.
InParanoid; Q9CQC9; -.
KO; K07953; -.
OMA; WMAQYIN; -.
OrthoDB; EOG091G0KFV; -.
PhylomeDB; Q9CQC9; -.
TreeFam; TF312890; -.
Reactome; R-MMU-204005; COPII-mediated vesicle transport.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-5694530; Cargo concentration in the ER.
Reactome; R-MMU-8963888; Chylomicron assembly.
Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
PRO; PR:Q9CQC9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020386; Expressed in 298 organ(s), highest expression level in vastus lateralis.
CleanEx; MM_SAR1B; -.
ExpressionAtlas; Q9CQC9; baseline and differential.
Genevisible; Q9CQC9; MM.
GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; IBA:GO_Central.
GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR006689; Small_GTPase_ARF/SAR.
InterPro; IPR006687; Small_GTPase_SAR1.
Pfam; PF00025; Arf; 1.
PRINTS; PR00328; SAR1GTPBP.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51422; SAR1; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; GTP-binding; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 198 GTP-binding protein SAR1b.
/FTId=PRO_0000206262.
NP_BIND 32 39 GTP. {ECO:0000250}.
NP_BIND 75 78 GTP. {ECO:0000250}.
NP_BIND 134 137 GTP. {ECO:0000250}.
METAL 34 34 Magnesium. {ECO:0000250}.
METAL 75 75 Magnesium. {ECO:0000250}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6B6}.
SEQUENCE 198 AA; 22382 MW; 9D0173C53FCD7A6B CRC64;
MSFIFDWIYS GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHV QARRVWKNYL PAINGIVFLV DCADHERLLE SKEELDSLMT
DETIANVPIL ILGNKIDRPE AISEERLREM FGLYGQTTGK GSVSLKELNA RPLEVFMCSV
LKRQGYGEGF RWMAQYID


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