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SY123_ARATH
ID   SY123_ARATH             Reviewed;         305 AA.
AC   Q9ZQZ8; A0A178V4Y6; Q0WPM4;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Syntaxin-123 {ECO:0000305};
DE            Short=AtSYP123 {ECO:0000305};
GN   Name=SYP123 {ECO:0000303|PubMed:19098073};
GN   OrderedLocusNames=At4g03330 {ECO:0000312|Araport:AT4G03330};
GN   ORFNames=F4C21.26 {ECO:0000312|EMBL:AAD14461.1};
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 [GENOMIC DNA].
RX   PubMed=21037570; DOI=10.1038/ng.704;
RA   Alcazar R., Garcia A.V., Kronholm I., de Meaux J., Koornneef M.,
RA   Parker J.E., Reymond M.;
RT   "Natural variation at strubbelig receptor kinase 3 drives immune-triggered
RT   incompatibilities between Arabidopsis thaliana accessions.";
RL   Nat. Genet. 42:1135-1139(2010).
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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=19098073; DOI=10.1093/pcp/pcn197;
RA   Enami K., Ichikawa M., Uemura T., Kutsuna N., Hasezawa S., Nakagawa T.,
RA   Nakano A., Sato M.H.;
RT   "Differential expression control and polarized distribution of plasma
RT   membrane-resident SYP1 SNAREs in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 50:280-289(2009).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24642714; DOI=10.1093/pcp/pcu048;
RA   Ichikawa M., Hirano T., Enami K., Fuselier T., Kato N., Kwon C., Voigt B.,
RA   Schulze-Lefert P., Baluska F., Sato M.H.;
RT   "Syntaxin of plant proteins SYP123 and SYP132 mediate root hair tip growth
RT   in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 55:790-800(2014).
CC   -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC       pathway (Probable). Acts in coordination with SYP132 to mediate tip-
CC       focused membrane trafficking for root hair tip growth
CC       (PubMed:24642714). Functions in root hair elongation by forming SNARE
CC       complexes with VAMP721,VAMP722 or VAMP724 (PubMed:24642714).
CC       {ECO:0000269|PubMed:24642714, ECO:0000305|PubMed:24642714}.
CC   -!- SUBUNIT: Part of the t-SNARE complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type IV
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in tips of root hairs.
CC       {ECO:0000269|PubMed:19098073}.
CC   -!- DISRUPTION PHENOTYPE: Reduced root hair length.
CC       {ECO:0000269|PubMed:24642714}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; GU571158; ADM21178.1; -; Genomic_DNA.
DR   EMBL; AC005275; AAD14461.1; -; Genomic_DNA.
DR   EMBL; AL161496; CAB77818.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82307.1; -; Genomic_DNA.
DR   EMBL; AK229042; BAF00925.1; -; mRNA.
DR   EMBL; BT044612; ACI31312.1; -; mRNA.
DR   EMBL; AY087693; AAM65230.1; -; mRNA.
DR   PIR; C85042; C85042.
DR   RefSeq; NP_192242.1; NM_116571.3.
DR   AlphaFoldDB; Q9ZQZ8; -.
DR   SMR; Q9ZQZ8; -.
DR   BioGRID; 13261; 39.
DR   IntAct; Q9ZQZ8; 38.
DR   STRING; 3702.AT4G03330.1; -.
DR   PaxDb; Q9ZQZ8; -.
DR   PRIDE; Q9ZQZ8; -.
DR   ProteomicsDB; 226773; -.
DR   EnsemblPlants; AT4G03330.1; AT4G03330.1; AT4G03330.
DR   GeneID; 827970; -.
DR   Gramene; AT4G03330.1; AT4G03330.1; AT4G03330.
DR   KEGG; ath:AT4G03330; -.
DR   Araport; AT4G03330; -.
DR   TAIR; locus:2125487; AT4G03330.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_1_1_1; -.
DR   InParanoid; Q9ZQZ8; -.
DR   OMA; SGRKWAC; -.
DR   OrthoDB; 1033833at2759; -.
DR   PhylomeDB; Q9ZQZ8; -.
DR   PRO; PR:Q9ZQZ8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9ZQZ8; baseline and differential.
DR   Genevisible; Q9ZQZ8; 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:0005886; C:plasma 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:0006887; P:exocytosis; 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; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 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   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Membrane; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..305
FT                   /note="Syntaxin-123"
FT                   /id="PRO_0000210248"
FT   TOPO_DOM        1..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..305
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..268
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          46..66
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZSD4"
SQ   SEQUENCE   305 AA;  34483 MW;  E8A7E49196708087 CRC64;
     MNDLISSSFK RYTDLNHQVQ LDDIESQNVS LDSGNLDEFF GYVESVKEDM KAVDEIHKRL
     QDANEESKTV HDSKAVKKLR ARMDSSVTEV LKRVKMIKTK LVALEKSNAA QRKVAGCGPG
     SSADRTRTSV VSGLGKKLKD MMDDFQRLRT KMATEYKETV ERRYFTVTGQ KADEETVEKL
     ISSGESERFL QKAIQEQGRG QVMDTLSEIQ ERHDTVKEIE RSLLELHQVF LDMAALVEAQ
     GNMLNDIESN VSKASSFVMR GTDQLHGAKV LQRNNRKWAC IATILAIVVV IVILFPILFN
     TLLRP
 
 
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