SNAA1_ARATH
ID SNAA1_ARATH Reviewed; 381 AA.
AC Q9LXZ5;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alpha-soluble NSF attachment protein 1;
DE Short=Alpha-SNAP1;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha 1;
GN Name=ASNAP1; OrderedLocusNames=At3g56450; ORFNames=T5P19_100;
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 [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 [2]
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 [3]
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 -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL163972; CAB88048.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79523.1; -; Genomic_DNA.
DR PIR; T49046; T49046.
DR RefSeq; NP_191204.1; NM_115503.1.
DR AlphaFoldDB; Q9LXZ5; -.
DR SMR; Q9LXZ5; -.
DR BioGRID; 10128; 6.
DR STRING; 3702.AT3G56450.1; -.
DR PaxDb; Q9LXZ5; -.
DR PRIDE; Q9LXZ5; -.
DR EnsemblPlants; AT3G56450.1; AT3G56450.1; AT3G56450.
DR GeneID; 824812; -.
DR Gramene; AT3G56450.1; AT3G56450.1; AT3G56450.
DR KEGG; ath:AT3G56450; -.
DR Araport; AT3G56450; -.
DR TAIR; locus:2102494; AT3G56450.
DR eggNOG; KOG1586; Eukaryota.
DR HOGENOM; CLU_726372_0_0_1; -.
DR InParanoid; Q9LXZ5; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; Q9LXZ5; -.
DR PRO; PR:Q9LXZ5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXZ5; baseline and differential.
DR Genevisible; Q9LXZ5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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:0035494; P:SNARE complex disassembly; IBA:GO_Central.
DR CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW ER-Golgi transport; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..381
FT /note="Alpha-soluble NSF attachment protein 1"
FT /id="PRO_0000219066"
SQ SEQUENCE 381 AA; 43881 MW; C1B218DFD81D0FC9 CRC64;
MFFVKGEGFF YPLFIELRNL IRYQTTRVSN SSRDFNLSQQ HCSCFRPKRR HEAHLSFIGT
LQYSKQRTIT RAASATIARR QLLLLFDITF SSSSSCYYFQ KKAEKKLNRR RRFDTKYEDA
ADLLEKARDS YKLAKSWDQA GIAYLKLADC HLKANSLANT YMIMDECMDH EIAEYYESDE
MFEQAIAYYE TAAEFFQIEE VTTSANQCNL KVAQYASQLE QQSRFMKTQA RHSLNNKLLK
YGVKGHLLTA GMCHLCKADV VSITNALEKY QDLDPTFSGT RECKFLADLA SAIDEEDIAK
FTDVSKEIDS VSPLVWAVNH MQLFGCKLCL VLDHDNNVVE GKREVQGQGA GGGCKLYLIE
GKCILDWNNV YTKRIYNYTN F
