SYP52_ARATH
ID SYP52_ARATH Reviewed; 233 AA.
AC Q94KK7; Q9MA16;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Syntaxin-52;
DE Short=AtSYP52;
GN Name=SYP52; OrderedLocusNames=At1g79590; ORFNames=F20B17.2;
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 either with VTI11 and SYP21, or with VTI11 and SYP22
CC in the prevacuolar compartment, or with VTI12 and SYP61 in the trans-
CC Golgi network to form t-SNARE complexes. {ECO:0000269|PubMed:11739776}.
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 -!- TISSUE SPECIFICITY: Expressed in root, leaf, stem, flower and silique.
CC -!- MISCELLANEOUS: SYP51 and SYP52 may have redundant functions.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF355756; AAK40224.1; -; mRNA.
DR EMBL; AC010793; AAF68106.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36269.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36270.1; -; Genomic_DNA.
DR EMBL; BT003941; AAO41986.1; -; mRNA.
DR EMBL; BT006106; AAP04091.1; -; mRNA.
DR EMBL; AY086285; AAM64357.1; -; mRNA.
DR PIR; C96827; C96827.
DR RefSeq; NP_001031301.1; NM_001036224.2.
DR RefSeq; NP_565213.1; NM_106607.5.
DR AlphaFoldDB; Q94KK7; -.
DR SMR; Q94KK7; -.
DR BioGRID; 29516; 3.
DR IntAct; Q94KK7; 1.
DR STRING; 3702.AT1G79590.2; -.
DR SwissPalm; Q94KK7; -.
DR PaxDb; Q94KK7; -.
DR PRIDE; Q94KK7; -.
DR ProteomicsDB; 233065; -.
DR EnsemblPlants; AT1G79590.1; AT1G79590.1; AT1G79590.
DR EnsemblPlants; AT1G79590.2; AT1G79590.2; AT1G79590.
DR GeneID; 844297; -.
DR Gramene; AT1G79590.1; AT1G79590.1; AT1G79590.
DR Gramene; AT1G79590.2; AT1G79590.2; AT1G79590.
DR KEGG; ath:AT1G79590; -.
DR Araport; AT1G79590; -.
DR TAIR; locus:2019858; AT1G79590.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_074236_0_0_1; -.
DR InParanoid; Q94KK7; -.
DR OMA; CGYWIVI; -.
DR PhylomeDB; Q94KK7; -.
DR PRO; PR:Q94KK7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94KK7; baseline and differential.
DR Genevisible; Q94KK7; 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:0000325; C:plant-type vacuole; HDA:TAIR.
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 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 Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..233
FT /note="Syntaxin-52"
FT /id="PRO_0000210262"
FT TOPO_DOM 1..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..233
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 137..199
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
SQ SEQUENCE 233 AA; 26108 MW; F58629FD64713BBE CRC64;
MASSSDPWMR EYNEALKLSE DINGMMSERN ASGLTGPDAQ RRASAIRRKI TILGTRLDSL
QSLLVKVPGK QHVSEKEMNR RKDMVGNLRS KTNQVASALN MSNFANRDSL FGTDLKPDDA
INRVSGMDNQ GIVVFQRQVM REQDEGLEKL EETVMSTKHI ALAVNEELTL QTRLIDDLDY
DVDITDSRLR RVQKSLALMN KSMKSGCSCM SMLLSVLGIV GLALVIWLLV KYL
