SAR1A_HUMAN
ID SAR1A_HUMAN Reviewed; 198 AA.
AC Q9NR31; B4DQ19;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=GTP-binding protein SAR1a;
DE AltName: Full=COPII-associated small GTPase;
GN Name=SAR1A; Synonyms=SAR1, SARA, SARA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10871277; DOI=10.1083/jcb.149.7.1345;
RA South S.T., Sacksteder K.A., Li X., Liu Y., Gould S.J.;
RT "Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome
RT synthesis.";
RL J. Cell Biol. 149:1345-1360(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Pietas A., Petersen I., Schluens K., Petersen S.;
RT "Identification of putative target genes involved in lung carcinogenesis.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=17005010; DOI=10.1111/j.1600-0854.2006.00493.x;
RA Watson P., Townley A.K., Koka P., Palmer K.J., Stephens D.J.;
RT "Sec16 defines endoplasmic reticulum exit sites and is required for
RT secretory cargo export in mammalian cells.";
RL Traffic 7:1678-1687(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP INTERACTION WITH B3GAT1.
RX PubMed=19181664; DOI=10.1074/jbc.m807517200;
RA Kizuka Y., Tonoyama Y., Oka S.;
RT "Distinct transport and intracellular activities of two GlcAT-P isoforms.";
RL J. Biol. Chem. 284:9247-9256(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP MUTAGENESIS OF HIS-79.
RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RT "STEEP mediates STING ER exit and activation of signaling.";
RL Nat. Immunol. 21:868-879(2020).
RN [16]
RP ERRATUM OF PUBMED:32690950.
RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5;
RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L.,
RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F.,
RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T.,
RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T.,
RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O.,
RA Thomsen M.K., Paludan S.R.;
RL Nat. Immunol. 21:1468-1469(2020).
CC -!- FUNCTION: Involved in transport from the endoplasmic reticulum to the
CC Golgi apparatus (By similarity). Required to maintain SEC16A
CC localization at discrete locations on the ER membrane perhaps by
CC preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on
CC the ER membrane forms an organized scaffold defining endoplasmic
CC reticulum exit sites (ERES). {ECO:0000250,
CC ECO:0000269|PubMed:17005010}.
CC -!- SUBUNIT: Interacts with B3GAT1. {ECO:0000269|PubMed:19181664}.
CC -!- INTERACTION:
CC Q9NR31; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-3920694, EBI-11277970;
CC Q9NR31; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-3920694, EBI-11957045;
CC Q9NR31; Q9BVK2: ALG8; NbExp=3; IntAct=EBI-3920694, EBI-3921603;
CC Q9NR31; P29972: AQP1; NbExp=3; IntAct=EBI-3920694, EBI-745213;
CC Q9NR31; Q96PS8: AQP10; NbExp=3; IntAct=EBI-3920694, EBI-12820279;
CC Q9NR31; Q92482: AQP3; NbExp=3; IntAct=EBI-3920694, EBI-2808854;
CC Q9NR31; P07306: ASGR1; NbExp=3; IntAct=EBI-3920694, EBI-1172335;
CC Q9NR31; P54253: ATXN1; NbExp=3; IntAct=EBI-3920694, EBI-930964;
CC Q9NR31; Q92843: BCL2L2; NbExp=3; IntAct=EBI-3920694, EBI-707714;
CC Q9NR31; P19397: CD53; NbExp=3; IntAct=EBI-3920694, EBI-6657396;
CC Q9NR31; P60033: CD81; NbExp=3; IntAct=EBI-3920694, EBI-712921;
CC Q9NR31; P23141-3: CES1; NbExp=3; IntAct=EBI-3920694, EBI-12360993;
CC Q9NR31; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3920694, EBI-12256978;
CC Q9NR31; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-3920694, EBI-11959453;
CC Q9NR31; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-3920694, EBI-11989440;
CC Q9NR31; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3920694, EBI-11522780;
CC Q9NR31; P29400-2: COL4A5; NbExp=3; IntAct=EBI-3920694, EBI-12211159;
CC Q9NR31; P54852: EMP3; NbExp=3; IntAct=EBI-3920694, EBI-3907816;
CC Q9NR31; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-3920694, EBI-711490;
CC Q9NR31; Q92520: FAM3C; NbExp=3; IntAct=EBI-3920694, EBI-2876774;
CC Q9NR31; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-3920694, EBI-11991950;
CC Q9NR31; P29033: GJB2; NbExp=3; IntAct=EBI-3920694, EBI-3905204;
CC Q9NR31; Q9Y3E0: GOLT1B; NbExp=3; IntAct=EBI-3920694, EBI-4402607;
CC Q9NR31; Q14416: GRM2; NbExp=3; IntAct=EBI-3920694, EBI-10232876;
CC Q9NR31; P02724: GYPA; NbExp=3; IntAct=EBI-3920694, EBI-702665;
CC Q9NR31; P30519: HMOX2; NbExp=3; IntAct=EBI-3920694, EBI-712096;
CC Q9NR31; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3920694, EBI-10266796;
CC Q9NR31; O43561-2: LAT; NbExp=3; IntAct=EBI-3920694, EBI-8070286;
CC Q9NR31; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3920694, EBI-2820517;
CC Q9NR31; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-3920694, EBI-2341610;
CC Q9NR31; P30301: MIP; NbExp=3; IntAct=EBI-3920694, EBI-8449636;
CC Q9NR31; O75425: MOSPD3; NbExp=3; IntAct=EBI-3920694, EBI-12179105;
CC Q9NR31; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-3920694, EBI-2863634;
CC Q9NR31; Q8N912: NRAC; NbExp=3; IntAct=EBI-3920694, EBI-12051377;
CC Q9NR31; Q8IXM6: NRM; NbExp=3; IntAct=EBI-3920694, EBI-10262547;
CC Q9NR31; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-3920694, EBI-1054848;
CC Q9NR31; Q9Y342: PLLP; NbExp=3; IntAct=EBI-3920694, EBI-3919291;
CC Q9NR31; P26678: PLN; NbExp=3; IntAct=EBI-3920694, EBI-692836;
CC Q9NR31; Q04941: PLP2; NbExp=3; IntAct=EBI-3920694, EBI-608347;
CC Q9NR31; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-3920694, EBI-10485931;
CC Q9NR31; Q59EV6: PPGB; NbExp=3; IntAct=EBI-3920694, EBI-14210385;
CC Q9NR31; Q8IXI1: RHOT2; NbExp=3; IntAct=EBI-3920694, EBI-1396563;
CC Q9NR31; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-3920694, EBI-2806908;
CC Q9NR31; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-3920694, EBI-8652744;
CC Q9NR31; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-3920694, EBI-10329948;
CC Q9NR31; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-3920694, EBI-10262251;
CC Q9NR31; P78382: SLC35A1; NbExp=3; IntAct=EBI-3920694, EBI-12870360;
CC Q9NR31; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-3920694, EBI-10314552;
CC Q9NR31; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-3920694, EBI-12188413;
CC Q9NR31; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-3920694, EBI-10244848;
CC Q9NR31; O15400: STX7; NbExp=3; IntAct=EBI-3920694, EBI-3221827;
CC Q9NR31; Q9UNK0: STX8; NbExp=3; IntAct=EBI-3920694, EBI-727240;
CC Q9NR31; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-3920694, EBI-12845616;
CC Q9NR31; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-3920694, EBI-1057733;
CC Q9NR31; Q14656: TMEM187; NbExp=3; IntAct=EBI-3920694, EBI-13046724;
CC Q9NR31; A2RU14: TMEM218; NbExp=3; IntAct=EBI-3920694, EBI-10173151;
CC Q9NR31; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-3920694, EBI-12887458;
CC Q9NR31; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-3920694, EBI-11956809;
CC Q9NR31; Q0VDI3: TMEM267; NbExp=3; IntAct=EBI-3920694, EBI-17555467;
CC Q9NR31; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-3920694, EBI-12038591;
CC Q9NR31; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-3920694, EBI-2852148;
CC Q9NR31; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-3920694, EBI-12111910;
CC Q9NR31; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-3920694, EBI-11996766;
CC Q9NR31; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-3920694, EBI-10243654;
CC Q9NR31; P49638: TTPA; NbExp=3; IntAct=EBI-3920694, EBI-10210710;
CC Q9NR31; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-3920694, EBI-2819725;
CC Q9NR31; Q53HI1: UNC50; NbExp=3; IntAct=EBI-3920694, EBI-7601760;
CC Q9NR31; O75841: UPK1B; NbExp=3; IntAct=EBI-3920694, EBI-12237619;
CC Q9NR31; Q15836: VAMP3; NbExp=3; IntAct=EBI-3920694, EBI-722343;
CC Q9NR31; O75379: VAMP4; NbExp=3; IntAct=EBI-3920694, EBI-744953;
CC Q9NR31; O95183: VAMP5; NbExp=3; IntAct=EBI-3920694, EBI-10191195;
CC Q9NR31; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-3920694, EBI-6256462;
CC Q9NR31; Q01405: Sec23a; Xeno; NbExp=2; IntAct=EBI-3920694, EBI-775901;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR31-2; Sequence=VSP_056220;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; AF261717; AAF81741.1; -; mRNA.
DR EMBL; AL136724; CAB66658.1; -; mRNA.
DR EMBL; AY008268; AAG16638.1; -; mRNA.
DR EMBL; AK298591; BAG60781.1; -; mRNA.
DR EMBL; AL731540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003658; AAH03658.1; -; mRNA.
DR CCDS; CCDS7298.1; -. [Q9NR31-1]
DR RefSeq; NP_001136120.1; NM_001142648.1. [Q9NR31-1]
DR RefSeq; NP_064535.1; NM_020150.4. [Q9NR31-1]
DR PDB; 2GAO; X-ray; 2.00 A; A/B=10-198.
DR PDBsum; 2GAO; -.
DR AlphaFoldDB; Q9NR31; -.
DR SMR; Q9NR31; -.
DR BioGRID; 121186; 187.
DR DIP; DIP-59790N; -.
DR IntAct; Q9NR31; 91.
DR MINT; Q9NR31; -.
DR STRING; 9606.ENSP00000362339; -.
DR ChEMBL; CHEMBL4295960; -.
DR GlyGen; Q9NR31; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR31; -.
DR PhosphoSitePlus; Q9NR31; -.
DR SwissPalm; Q9NR31; -.
DR BioMuta; SAR1A; -.
DR DMDM; 14548013; -.
DR OGP; Q9NR31; -.
DR EPD; Q9NR31; -.
DR jPOST; Q9NR31; -.
DR MassIVE; Q9NR31; -.
DR MaxQB; Q9NR31; -.
DR PaxDb; Q9NR31; -.
DR PeptideAtlas; Q9NR31; -.
DR PRIDE; Q9NR31; -.
DR ProteomicsDB; 4836; -.
DR ProteomicsDB; 82267; -. [Q9NR31-1]
DR TopDownProteomics; Q9NR31-1; -. [Q9NR31-1]
DR Antibodypedia; 1887; 212 antibodies from 36 providers.
DR DNASU; 56681; -.
DR Ensembl; ENST00000373238.5; ENSP00000362335.1; ENSG00000079332.15. [Q9NR31-1]
DR Ensembl; ENST00000373241.9; ENSP00000362338.4; ENSG00000079332.15. [Q9NR31-1]
DR Ensembl; ENST00000373242.6; ENSP00000362339.1; ENSG00000079332.15. [Q9NR31-1]
DR Ensembl; ENST00000431664.6; ENSP00000399698.2; ENSG00000079332.15. [Q9NR31-1]
DR GeneID; 56681; -.
DR KEGG; hsa:56681; -.
DR MANE-Select; ENST00000373241.9; ENSP00000362338.4; NM_020150.5; NP_064535.1.
DR UCSC; uc010qjh.3; human. [Q9NR31-1]
DR CTD; 56681; -.
DR DisGeNET; 56681; -.
DR GeneCards; SAR1A; -.
DR HGNC; HGNC:10534; SAR1A.
DR HPA; ENSG00000079332; Low tissue specificity.
DR MIM; 607691; gene.
DR neXtProt; NX_Q9NR31; -.
DR OpenTargets; ENSG00000079332; -.
DR PharmGKB; PA34942; -.
DR VEuPathDB; HostDB:ENSG00000079332; -.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000155276; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q9NR31; -.
DR OMA; DDRIAQH; -.
DR PhylomeDB; Q9NR31; -.
DR TreeFam; TF312890; -.
DR PathwayCommons; Q9NR31; -.
DR SignaLink; Q9NR31; -.
DR SIGNOR; Q9NR31; -.
DR BioGRID-ORCS; 56681; 62 hits in 1057 CRISPR screens.
DR ChiTaRS; SAR1A; human.
DR EvolutionaryTrace; Q9NR31; -.
DR GenomeRNAi; 56681; -.
DR Pharos; Q9NR31; Tbio.
DR PRO; PR:Q9NR31; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NR31; protein.
DR Bgee; ENSG00000079332; Expressed in calcaneal tendon and 218 other tissues.
DR ExpressionAtlas; Q9NR31; baseline and differential.
DR Genevisible; Q9NR31; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..198
FT /note="GTP-binding protein SAR1a"
FT /id="PRO_0000206258"
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:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056220"
FT MUTAGEN 79
FT /note="H->G: Decreases transport of STING1 from the
FT endoplasmic reticulum to the Golgi."
FT /evidence="ECO:0000269|PubMed:32690950"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:2GAO"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2GAO"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2GAO"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2GAO"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:2GAO"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:2GAO"
SQ 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
