SYP51_ARATH
ID SYP51_ARATH Reviewed; 232 AA.
AC Q9SA23;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Syntaxin-51;
DE Short=AtSYP51;
GN Name=SYP51; OrderedLocusNames=At1g16240; ORFNames=F3O9.4;
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 INTERACTION WITH SYP21; SYP22; SYP61; VTI11
RP AND VTI12.
RX PubMed=11739776; DOI=10.1091/mbc.12.12.3733;
RA Sanderfoot A.A., Kovaleva V., Bassham D.C., Raikhel N.V.;
RT "Interactions between syntaxins identify at least five SNARE complexes
RT within the Golgi/prevacuolar system of the Arabidopsis cell.";
RL Mol. Biol. Cell 12:3733-3743(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
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 [5]
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: Vesicle trafficking protein that functions in the secretory
CC pathway. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VTI11 and either SYP21, or SYP22, or SYP61 in
CC the prevacuolar compartment, or with VTI12 and SYP61 in the trans-Golgi
CC network to form t-SNARE complexes. {ECO:0000269|PubMed:11739776}.
CC -!- INTERACTION:
CC Q9SA23; Q946Y7: SYP61; NbExp=2; IntAct=EBI-4436558, EBI-4438441;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type IV membrane protein. Prevacuolar compartment membrane;
CC Single-pass type IV membrane protein.
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=Q9SA23-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in root, leaf, stem, flower and silique.
CC -!- MISCELLANEOUS: SYP51 and SYP52 may have redundant functions. The exact
CC location of the SYP51/SYP61 complex is unclear, but is probably on the
CC trans-Golgi network because of the likelihood of containing chiefly
CC VTI12.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF355755; AAK40223.1; -; mRNA.
DR EMBL; AC006341; AAD34675.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29423.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29424.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60981.1; -; Genomic_DNA.
DR EMBL; AY074863; AAL75885.1; -; mRNA.
DR EMBL; AY097382; AAM19898.1; -; mRNA.
DR EMBL; AY085320; AAM62551.1; -; mRNA.
DR PIR; C86297; C86297.
DR RefSeq; NP_001031054.1; NM_001035977.1. [Q9SA23-1]
DR RefSeq; NP_001323228.1; NM_001332216.1. [Q9SA23-1]
DR RefSeq; NP_563994.1; NM_101490.4. [Q9SA23-1]
DR AlphaFoldDB; Q9SA23; -.
DR SMR; Q9SA23; -.
DR BioGRID; 23433; 6.
DR IntAct; Q9SA23; 9.
DR STRING; 3702.AT1G16240.1; -.
DR SwissPalm; Q9SA23; -.
DR PaxDb; Q9SA23; -.
DR PRIDE; Q9SA23; -.
DR ProteomicsDB; 233064; -. [Q9SA23-1]
DR EnsemblPlants; AT1G16240.1; AT1G16240.1; AT1G16240. [Q9SA23-1]
DR EnsemblPlants; AT1G16240.2; AT1G16240.2; AT1G16240. [Q9SA23-1]
DR EnsemblPlants; AT1G16240.4; AT1G16240.4; AT1G16240. [Q9SA23-1]
DR GeneID; 838193; -.
DR Gramene; AT1G16240.1; AT1G16240.1; AT1G16240. [Q9SA23-1]
DR Gramene; AT1G16240.2; AT1G16240.2; AT1G16240. [Q9SA23-1]
DR Gramene; AT1G16240.4; AT1G16240.4; AT1G16240. [Q9SA23-1]
DR KEGG; ath:AT1G16240; -.
DR Araport; AT1G16240; -.
DR TAIR; locus:2032835; AT1G16240.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_074236_0_0_1; -.
DR InParanoid; Q9SA23; -.
DR OMA; RQSTACL; -.
DR PhylomeDB; Q9SA23; -.
DR PRO; PR:Q9SA23; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA23; baseline and differential.
DR Genevisible; Q9SA23; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; TAS:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
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 GO; GO:0016192; P:vesicle-mediated transport; TAS:TAIR.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..232
FT /note="Syntaxin-51"
FT /id="PRO_0000210261"
FT TOPO_DOM 1..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..232
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 136..198
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
SQ SEQUENCE 232 AA; 25889 MW; 8966A0232C856A8F CRC64;
MASSSDSWMR AYNEALKLSE EINGMISERS SSAVTGPDAQ RRASAIRRKI TIFGNKLDSL
QSLLAEIHGK PISEKEMNRR KDMVGNLRSK ANQMANALNM SNFANRDSLL GPDIKPDDSM
SRVTGMDNQG IVGYQRQVMR EQDEGLEQLE GTVMSTKHIA LAVSEELDLQ TRLIDDLDYH
VDVTDSRLRR VQKSLAVMNK NMRSGCSCMS MLLSVLGIVG LAVVIWMLVK YM
