SNAG_ARATH
ID SNAG_ARATH Reviewed; 291 AA.
AC Q9SPE5; Q9SUN8;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Gamma-soluble NSF attachment protein;
DE Short=Gamma-SNAP;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein gamma;
GN Name=GSNAP; OrderedLocusNames=At4g20410; ORFNames=F9F13.60;
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.
RC STRAIN=cv. Columbia;
RX PubMed=10727946; DOI=10.1046/j.1432-1327.2000.01212.x;
RA Weidenhaupt M., Bruckert F., Louwagie M., Garin J., Satre M.;
RT "Functional and molecular identification of novel members of the ubiquitous
RT membrane fusion proteins alpha- and gamma-SNAP (soluble N-ethylmaleimide-
RT sensitive factor-attachment proteins) families in Dictyostelium
RT discoideum.";
RL Eur. J. Biochem. 267:2062-2070(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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.
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus. Binds to SNARE complex and then
CC recruits NSF to disassemble it (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF177990; AAF01285.1; -; mRNA.
DR EMBL; AL080253; CAB45807.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161553; CAB79041.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84326.1; -; Genomic_DNA.
DR EMBL; AY086673; AAM63730.1; -; mRNA.
DR RefSeq; NP_567600.1; NM_118160.5.
DR AlphaFoldDB; Q9SPE5; -.
DR SMR; Q9SPE5; -.
DR BioGRID; 13080; 2.
DR STRING; 3702.AT4G20410.1; -.
DR PaxDb; Q9SPE5; -.
DR PRIDE; Q9SPE5; -.
DR ProteomicsDB; 245321; -.
DR DNASU; 827789; -.
DR EnsemblPlants; AT4G20410.1; AT4G20410.1; AT4G20410.
DR GeneID; 827789; -.
DR Gramene; AT4G20410.1; AT4G20410.1; AT4G20410.
DR KEGG; ath:AT4G20410; -.
DR Araport; AT4G20410; -.
DR TAIR; locus:2128669; AT4G20410.
DR eggNOG; KOG1585; Eukaryota.
DR HOGENOM; CLU_063974_2_0_1; -.
DR InParanoid; Q9SPE5; -.
DR OMA; MHKENGN; -.
DR PhylomeDB; Q9SPE5; -.
DR PRO; PR:Q9SPE5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SPE5; baseline and differential.
DR Genevisible; Q9SPE5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 2: Evidence at transcript level;
KW ER-Golgi transport; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..291
FT /note="Gamma-soluble NSF attachment protein"
FT /id="PRO_0000219070"
FT CONFLICT 45..46
FT /note="NK -> KN (in Ref. 4; AAM63730)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> S (in Ref. 4; AAM63730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32360 MW; 3EECE3B64D038BAD CRC64;
MSSDPDKMMS KADKMTKLTL TRWSADWRGA TELYEQAANG FRASNKYEKA KVALEKASKG
QEMQASPWDA AKHMESAAAL AQKLSIWNEV ADFYRKASEL YVECGRAQPA SDALGKAARA
LEDVKPDDAI QLYTDACEIL EEDGRDQMAF DLYRACANVY IKLEKFTDAA TFFLRLGVAA
DKCDATNSQC KAYLSAIILY LYAHDLQQAE KCYNDCSQID AFLKSDQSRS ASRLLTAYNE
GDIEEIKKVA SASTVSNLDH MIIKLARKLP TGDVTAIQMN TNDDLDEDDL T
