SYP23_ARATH
ID SYP23_ARATH Reviewed; 255 AA.
AC O04378; O23613;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 167.
DE RecName: Full=Syntaxin-23;
DE Short=AtPLP;
DE Short=AtSYP23;
DE AltName: Full=AtPEP12-like protein;
GN Name=SYP23; OrderedLocusNames=At4g17730; ORFNames=dl4901w, FCAALL.117;
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], AND POLYMORPHISM.
RC STRAIN=cv. Columbia, and cv. RLD;
RA Zheng H., Bassham D.C., da Silva Conceicao A., Raikhel N.V.;
RT "The syntaxin family of proteins in Arabidopsis: a new syntaxin homologue
RT shows polymorphism between two ecotypes.";
RL J. Exp. Bot. 50:915-924(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [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=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 [6]
RP INTERACTION WITH RGS1.
RX PubMed=21952135; DOI=10.1038/msb.2011.66;
RA Klopffleisch K., Phan N., Augustin K., Bayne R.S., Booker K.S.,
RA Botella J.R., Carpita N.C., Carr T., Chen J.G., Cooke T.R., Frick-Cheng A.,
RA Friedman E.J., Fulk B., Hahn M.G., Jiang K., Jorda L., Kruppe L., Liu C.,
RA Lorek J., McCann M.C., Molina A., Moriyama E.N., Mukhtar M.S., Mudgil Y.,
RA Pattathil S., Schwarz J., Seta S., Tan M., Temp U., Trusov Y., Urano D.,
RA Welter B., Yang J., Panstruga R., Uhrig J.F., Jones A.M.;
RT "Arabidopsis G-protein interactome reveals connections to cell wall
RT carbohydrates and morphogenesis.";
RL Mol. Syst. Biol. 7:532-532(2011).
CC -!- FUNCTION: May function in the docking or fusion of transport vesicles
CC with the prevacuolar membrane.
CC -!- SUBUNIT: Part of the t-SNARE complex (By similarity). Interacts with
CC RGS1. {ECO:0000250, ECO:0000269|PubMed:21952135}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.
CC Membrane. Note=In cv. RLD, probably a type IV membrane protein. In cv.
CC Columbia, probably associated with membranes by a post-translational
CC modification or through protein-protein interactions.
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=O04378-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in leaves, flowers and
CC stems than in roots.
CC -!- POLYMORPHISM: Addition of one nucleotide in cv. RLD induces a
CC frameshift in position 245 leading to a protein 22 amino acids longer
CC than the one shown here. {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: In cv. RLD, the 22 amino acids extension regenerates a
CC typical syntaxin transmembrane domain. In cv. Columbia it encodes a
CC protein that has no terminal transmembrane domain, but that is however
CC not detected in cytosolic fractions.
CC -!- SIMILARITY: Belongs to the syntaxin 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; U85036; AAB58544.1; -; mRNA.
DR EMBL; Z97344; CAB10553.2; -; Genomic_DNA.
DR EMBL; AL161547; CAB78776.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83941.1; -; Genomic_DNA.
DR EMBL; AY074294; AAL66991.1; -; mRNA.
DR EMBL; BT000708; AAN31851.1; -; mRNA.
DR EMBL; BT008517; AAP40344.1; -; mRNA.
DR PIR; H85198; H85198.
DR RefSeq; NP_567537.1; NM_117882.3. [O04378-1]
DR AlphaFoldDB; O04378; -.
DR SMR; O04378; -.
DR BioGRID; 12787; 56.
DR STRING; 3702.AT4G17730.2; -.
DR PaxDb; O04378; -.
DR ProteomicsDB; 233054; -. [O04378-1]
DR EnsemblPlants; AT4G17730.1; AT4G17730.1; AT4G17730. [O04378-1]
DR GeneID; 827494; -.
DR Gramene; AT4G17730.1; AT4G17730.1; AT4G17730. [O04378-1]
DR KEGG; ath:AT4G17730; -.
DR Araport; AT4G17730; -.
DR eggNOG; KOG0811; Eukaryota.
DR HOGENOM; CLU_059257_3_0_1; -.
DR InParanoid; O04378; -.
DR OMA; HNINSET; -.
DR PhylomeDB; O04378; -.
DR PRO; PR:O04378; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O04378; baseline and differential.
DR Genevisible; O04378; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR Pfam; PF14523; Syntaxin_2; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P93654"
FT CHAIN 2..255
FT /note="Syntaxin-23"
FT /id="PRO_0000210255"
FT DOMAIN 184..246
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P93654"
FT VARIANT 245..255
FT /note="RHQRHKDQILL -> KASKTQRSNSSLTCLLLVIFGIVLMIVIIVLAV (in
FT strain: cv. RLD)"
SQ SEQUENCE 255 AA; 28604 MW; 73A12C5098363E7E CRC64;
MSFQDLEAGR GRSLASSRNI NGGGSRQDTT QDVASGIFQI NTSVSTFHRL VNTLGTPKDT
PELREKLHKT RLYIGQLVKD TSAKLKEASE TDHQRGVNQK KKIVDAKLAK DFQAVLKEFQ
KAQRLAAERE TVYAPLVHKP SLPSSYTSSE IDVNGDKHPE QRALLVESKR QELVLLDNEI
AFNEAVIEER EQGIQEIQQQ IGEVHEIFKD LAVLVHDQGN MIDDIGTHID NSYAATAQGK
SHLVRHQRHK DQILL
