SNAA2_ARATH
ID SNAA2_ARATH Reviewed; 289 AA.
AC Q9SPE6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Alpha-soluble NSF attachment protein 2;
DE Short=Alpha-SNAP2;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha 2;
GN Name=ASNAP2; Synonyms=ASNAP; OrderedLocusNames=At3g56190;
GN ORFNames=F18O21_150;
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.
RC STRAIN=cv. Columbia;
RA Weidenhaupt M., Bruckert F.;
RT "Molecular characterization of Arabidopsis thaliana alpha-soluble
RT attachment protein (alpha-SNAP).";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP INTERACTION WITH SYP21.
RX PubMed=10504581; DOI=10.1046/j.1365-313x.1999.00552.x;
RA Bassham D.C., Raikhel N.V.;
RT "The pre-vacuolar t-SNARE AtPEP12p forms a 20S complex that dissociates in
RT the presence of ATP.";
RL Plant J. 19:599-603(1999).
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 -!- SUBUNIT: Binds to the syntaxin SYP21 and to NSF. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SPE6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR EMBL; AF177989; AAF01284.1; -; mRNA.
DR EMBL; AL163763; CAB87418.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79491.1; -; Genomic_DNA.
DR EMBL; AK118366; BAC42980.1; -; mRNA.
DR PIR; T47736; T47736.
DR RefSeq; NP_191178.1; NM_115477.3. [Q9SPE6-1]
DR AlphaFoldDB; Q9SPE6; -.
DR SMR; Q9SPE6; -.
DR BioGRID; 10101; 9.
DR IntAct; Q9SPE6; 3.
DR STRING; 3702.AT3G56190.1; -.
DR iPTMnet; Q9SPE6; -.
DR PaxDb; Q9SPE6; -.
DR PRIDE; Q9SPE6; -.
DR ProteomicsDB; 232642; -. [Q9SPE6-1]
DR EnsemblPlants; AT3G56190.1; AT3G56190.1; AT3G56190. [Q9SPE6-1]
DR GeneID; 824785; -.
DR Gramene; AT3G56190.1; AT3G56190.1; AT3G56190. [Q9SPE6-1]
DR KEGG; ath:AT3G56190; -.
DR Araport; AT3G56190; -.
DR TAIR; locus:2078366; AT3G56190.
DR eggNOG; KOG1586; Eukaryota.
DR HOGENOM; CLU_046329_0_2_1; -.
DR InParanoid; Q9SPE6; -.
DR OMA; WSVKEYL; -.
DR PhylomeDB; Q9SPE6; -.
DR PRO; PR:Q9SPE6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SPE6; baseline and differential.
DR Genevisible; Q9SPE6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
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:0035494; P:SNARE complex disassembly; IBA:GO_Central.
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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..289
FT /note="Alpha-soluble NSF attachment protein 2"
FT /id="PRO_0000219067"
FT REPEAT 112..145
FT /note="TPR 1"
FT REPEAT 152..185
FT /note="TPR 2"
FT CONFLICT 137
FT /note="K -> R (in Ref. 3; BAC42980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32755 MW; EE0A811FCE12E4D7 CRC64;
MGDHLVRAEE FEKKAEKKLN GWGIFGSKYE DAADLLEKAA NSYKLAKSWD QAGKAYLKLA
DCHLKSDSKH DAANAYAEAA KCYKKVDTNE AASCLERAVN IFCEIGRLNM AARYYKEIAE
YYESDQKFEQ AIAYFEKAAE FFQNEEVTTS ANQCNLKVAQ YAAQLEQYEK AIKIYEDIAR
HSLNNNLLKY GVKGHLLTAG MCHLCKADVV SITNALEKYQ DLDPTFTGTR ECKFLADLAS
AIDEEDIAKF TDVVKEFDSM TPLDSWKTTM LLRVKEKLKA KELEEDDLT