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GTP-binding protein SAR1a (COPII-associated small GTPase)

 SAR1A_HUMAN             Reviewed;         198 AA.
Q9NR31; B4DQ19;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 166.
RecName: Full=GTP-binding protein SAR1a;
AltName: Full=COPII-associated small GTPase;
Name=SAR1A; Synonyms=SAR1, SARA, SARA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10871277; DOI=10.1083/jcb.149.7.1345;
South S.T., Sacksteder K.A., Li X., Liu Y., Gould S.J.;
"Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome
synthesis.";
J. Cell Biol. 149:1345-1360(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
Pietas A., Petersen I., Schluens K., Petersen S.;
"Identification of putative target genes involved in lung
carcinogenesis.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[7]
FUNCTION.
PubMed=17005010; DOI=10.1111/j.1600-0854.2006.00493.x;
Watson P., Townley A.K., Koka P., Palmer K.J., Stephens D.J.;
"Sec16 defines endoplasmic reticulum exit sites and is required for
secretory cargo export in mammalian cells.";
Traffic 7:1678-1687(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
INTERACTION WITH B3GAT1.
PubMed=19181664; DOI=10.1074/jbc.M807517200;
Kizuka Y., Tonoyama Y., Oka S.;
"Distinct transport and intracellular activities of two GlcAT-P
isoforms.";
J. Biol. Chem. 284:9247-9256(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in transport from the endoplasmic reticulum to
the Golgi apparatus (By similarity). Required to maintain SEC16A
localization at discrete locations on the ER membrane perhaps by
preventing its dissociation. SAR1A-GTP-dependent assembly of
SEC16A on the ER membrane forms an organized scaffold defining
endoplasmic reticulum exit sites (ERES). {ECO:0000250,
ECO:0000269|PubMed:17005010}.
-!- SUBUNIT: Interacts with B3GAT1. {ECO:0000269|PubMed:19181664}.
-!- INTERACTION:
Q01405:Sec23a (xeno); NbExp=2; IntAct=EBI-3920694, EBI-775901;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
apparatus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NR31-1; Sequence=Displayed;
Name=2;
IsoId=Q9NR31-2; Sequence=VSP_056220;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF261717; AAF81741.1; -; mRNA.
EMBL; AL136724; CAB66658.1; -; mRNA.
EMBL; AY008268; AAG16638.1; -; mRNA.
EMBL; AK298591; BAG60781.1; -; mRNA.
EMBL; AL731540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003658; AAH03658.1; -; mRNA.
CCDS; CCDS7298.1; -. [Q9NR31-1]
RefSeq; NP_001136120.1; NM_001142648.1. [Q9NR31-1]
RefSeq; NP_064535.1; NM_020150.4. [Q9NR31-1]
UniGene; Hs.499960; -.
PDB; 2GAO; X-ray; 2.00 A; A/B=10-198.
PDBsum; 2GAO; -.
ProteinModelPortal; Q9NR31; -.
SMR; Q9NR31; -.
BioGrid; 121186; 21.
DIP; DIP-59790N; -.
IntAct; Q9NR31; 72.
MINT; Q9NR31; -.
STRING; 9606.ENSP00000362335; -.
iPTMnet; Q9NR31; -.
PhosphoSitePlus; Q9NR31; -.
SwissPalm; Q9NR31; -.
BioMuta; SAR1A; -.
DMDM; 14548013; -.
OGP; Q9NR31; -.
EPD; Q9NR31; -.
MaxQB; Q9NR31; -.
PaxDb; Q9NR31; -.
PeptideAtlas; Q9NR31; -.
PRIDE; Q9NR31; -.
ProteomicsDB; 82267; -.
TopDownProteomics; Q9NR31-1; -. [Q9NR31-1]
DNASU; 56681; -.
Ensembl; ENST00000373238; ENSP00000362335; ENSG00000079332. [Q9NR31-1]
Ensembl; ENST00000373241; ENSP00000362338; ENSG00000079332. [Q9NR31-1]
Ensembl; ENST00000373242; ENSP00000362339; ENSG00000079332. [Q9NR31-1]
Ensembl; ENST00000431664; ENSP00000399698; ENSG00000079332. [Q9NR31-1]
GeneID; 56681; -.
KEGG; hsa:56681; -.
UCSC; uc010qjh.3; human. [Q9NR31-1]
CTD; 56681; -.
DisGeNET; 56681; -.
EuPathDB; HostDB:ENSG00000079332.14; -.
GeneCards; SAR1A; -.
HGNC; HGNC:10534; SAR1A.
HPA; CAB022545; -.
HPA; HPA006923; -.
HPA; HPA048368; -.
MIM; 607691; gene.
neXtProt; NX_Q9NR31; -.
OpenTargets; ENSG00000079332; -.
PharmGKB; PA34942; -.
eggNOG; KOG0077; Eukaryota.
eggNOG; ENOG410YIKI; LUCA.
GeneTree; ENSGT00550000074696; -.
HOGENOM; HOG000163690; -.
HOVERGEN; HBG104997; -.
InParanoid; Q9NR31; -.
KO; K07953; -.
OMA; KDDRLAQ; -.
OrthoDB; EOG091G0KFV; -.
PhylomeDB; Q9NR31; -.
TreeFam; TF312890; -.
ChiTaRS; SAR1A; human.
EvolutionaryTrace; Q9NR31; -.
GenomeRNAi; 56681; -.
PRO; PR:Q9NR31; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000079332; Expressed in 242 organ(s), highest expression level in female gonad.
CleanEx; HS_SAR1A; -.
ExpressionAtlas; Q9NR31; baseline and differential.
Genevisible; Q9NR31; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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;
3D-structure; Alternative splicing; Complete proteome;
Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
GTP-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 198 GTP-binding protein SAR1a.
/FTId=PRO_0000206258.
NP_BIND 32 39 GTP. {ECO:0000250}.
NP_BIND 75 78 GTP. {ECO:0000250}.
NP_BIND 134 137 GTP. {ECO:0000250}.
MOD_RES 139 139 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 43 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056220.
HELIX 14 19 {ECO:0000244|PDB:2GAO}.
STRAND 26 31 {ECO:0000244|PDB:2GAO}.
HELIX 38 44 {ECO:0000244|PDB:2GAO}.
STRAND 61 66 {ECO:0000244|PDB:2GAO}.
STRAND 69 73 {ECO:0000244|PDB:2GAO}.
HELIX 86 89 {ECO:0000244|PDB:2GAO}.
HELIX 90 92 {ECO:0000244|PDB:2GAO}.
STRAND 95 101 {ECO:0000244|PDB:2GAO}.
HELIX 105 107 {ECO:0000244|PDB:2GAO}.
HELIX 108 120 {ECO:0000244|PDB:2GAO}.
HELIX 122 124 {ECO:0000244|PDB:2GAO}.
STRAND 129 134 {ECO:0000244|PDB:2GAO}.
HELIX 144 150 {ECO:0000244|PDB:2GAO}.
TURN 154 156 {ECO:0000244|PDB:2GAO}.
TURN 165 167 {ECO:0000244|PDB:2GAO}.
STRAND 173 177 {ECO:0000244|PDB:2GAO}.
TURN 180 183 {ECO:0000244|PDB:2GAO}.
HELIX 186 194 {ECO:0000244|PDB:2GAO}.
SEQUENCE 198 AA; 22367 MW; 38A869175CBA54F3 CRC64;
MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT
SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT
DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV
LKRQGYGEGF RWLSQYID


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