SAR1B_ARATH
ID SAR1B_ARATH Reviewed; 193 AA.
AC Q01474;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=GTP-binding protein SAR1B;
GN Name=SAR1B; Synonyms=SAR1; OrderedLocusNames=At1g56330; ORFNames=F14G9.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1396601; DOI=10.1002/j.1460-2075.1992.tb05514.x;
RA d'Enfert C., Gensse M., Gaillardin C.;
RT "Fission yeast and a plant have functional homologues of the Sar1 and Sec12
RT proteins involved in ER to Golgi traffic in budding yeast.";
RL EMBO J. 11:4205-4211(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH BZIP28.
RX PubMed=22335396; DOI=10.1111/j.1365-313x.2012.04943.x;
RA Srivastava R., Chen Y., Deng Y., Brandizzi F., Howell S.H.;
RT "Elements proximal to and within the transmembrane domain mediate the
RT organelle-to-organelle movement of bZIP28 under ER stress conditions.";
RL Plant J. 70:1033-1042(2012).
CC -!- FUNCTION: Involved in transport from the endoplasmic reticulum to the
CC Golgi apparatus. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BZIP28. {ECO:0000269|PubMed:22335396}.
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; M95795; AAA32807.1; -; mRNA.
DR EMBL; AC069159; AAG50911.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33378.1; -; Genomic_DNA.
DR EMBL; AY072220; AAL60041.1; -; mRNA.
DR EMBL; AY096599; AAM20249.1; -; mRNA.
DR EMBL; AY085815; AAM63031.1; -; mRNA.
DR PIR; S28603; S28603.
DR RefSeq; NP_176029.1; NM_104512.3.
DR AlphaFoldDB; Q01474; -.
DR SMR; Q01474; -.
DR BioGRID; 27311; 20.
DR IntAct; Q01474; 18.
DR STRING; 3702.AT1G56330.1; -.
DR iPTMnet; Q01474; -.
DR PaxDb; Q01474; -.
DR PRIDE; Q01474; -.
DR ProteomicsDB; 226584; -.
DR EnsemblPlants; AT1G56330.1; AT1G56330.1; AT1G56330.
DR GeneID; 842086; -.
DR Gramene; AT1G56330.1; AT1G56330.1; AT1G56330.
DR KEGG; ath:AT1G56330; -.
DR Araport; AT1G56330; -.
DR TAIR; locus:2011796; AT1G56330.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q01474; -.
DR OMA; EYWPAIS; -.
DR OrthoDB; 1168548at2759; -.
DR PhylomeDB; Q01474; -.
DR PRO; PR:Q01474; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q01474; baseline and differential.
DR Genevisible; Q01474; AT.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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 Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT CHAIN 1..193
FT /note="GTP-binding protein SAR1B"
FT /id="PRO_0000206266"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 193 AA; 21986 MW; 9D9AE86B3E868878 CRC64;
MFLFDWFYGI LASLGLWQKE AKILFLGLDN AGKTTLLHML KDERLVQHQP TQHPTSEELS
IGKIKFKAFD LGGHQIARRV WKDYYAKVDA VVYLVDAYDK ERFAESKREL DALLSDEALA
TVPFLILGNK IDIPYAASED ELRYHLGLTN FTTGKGKVTL GDSGVRPLEV FMCSIVRKMG
YGEGFKWLSQ YIN
