SYP21_ARATH
ID SYP21_ARATH Reviewed; 279 AA.
AC Q39233;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Syntaxin-21;
DE Short=AtSYP21;
DE AltName: Full=PEP12 homolog;
DE Short=AtPEP12;
DE AltName: Full=aPEP12;
GN Name=SYP21; OrderedLocusNames=At5g16830; ORFNames=F5E19_170;
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].
RC STRAIN=cv. RLD;
RX PubMed=7638178; DOI=10.1073/pnas.92.16.7262;
RA Bassham D.C., Gal S., da Silva Conceicao A., Raikhel N.V.;
RT "An Arabidopsis syntaxin homologue isolated by functional complementation
RT of a yeast pep12 mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7262-7266(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9144962; DOI=10.1105/tpc.9.4.571;
RA da Silva Conceicao A., Marty-Mazars D., Bassham D.C., Sanderfoot A.A.,
RA Marty F., Raikhel N.V.;
RT "The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in
RT plants.";
RL Plant Cell 9:571-582(1997).
RN [7]
RP INTERACTION WITH ALPHA-SNAP.
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).
RN [8]
RP INTERACTION WITH VTI11 AND SYP51.
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).
CC -!- FUNCTION: May function in the docking or fusion of transport vesicles
CC with the prevacuolar membrane.
CC -!- SUBUNIT: Interacts with VTI11 and SYP51 to form a t-SNARE complex and
CC with alpha-SNAP to form a 20S complex. {ECO:0000269|PubMed:10504581,
CC ECO:0000269|PubMed:11739776}.
CC -!- INTERACTION:
CC Q39233; Q9SEL6: VTI11; NbExp=4; IntAct=EBI-2352544, EBI-1162795;
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:9144962}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:9144962}.
CC -!- TISSUE SPECIFICITY: A high level expression is seen in the roots while
CC a low level expression is seen in the leaves.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; L41651; AAA87296.1; -; mRNA.
DR EMBL; AL391147; CAC01847.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92345.1; -; Genomic_DNA.
DR EMBL; AF411797; AAL06486.1; -; mRNA.
DR EMBL; AY088599; AAM66128.1; -; mRNA.
DR PIR; T51515; T51515.
DR RefSeq; NP_197185.1; NM_121689.4.
DR AlphaFoldDB; Q39233; -.
DR SMR; Q39233; -.
DR BioGRID; 16822; 54.
DR IntAct; Q39233; 52.
DR STRING; 3702.AT5G16830.1; -.
DR SwissPalm; Q39233; -.
DR PaxDb; Q39233; -.
DR PRIDE; Q39233; -.
DR ProteomicsDB; 228470; -.
DR EnsemblPlants; AT5G16830.1; AT5G16830.1; AT5G16830.
DR GeneID; 831546; -.
DR Gramene; AT5G16830.1; AT5G16830.1; AT5G16830.
DR KEGG; ath:AT5G16830; -.
DR Araport; AT5G16830; -.
DR TAIR; locus:2148960; AT5G16830.
DR eggNOG; KOG0811; Eukaryota.
DR HOGENOM; CLU_059257_3_0_1; -.
DR InParanoid; Q39233; -.
DR OMA; YNAPELD; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; Q39233; -.
DR PRO; PR:Q39233; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39233; baseline and differential.
DR Genevisible; Q39233; 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:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:TAIR.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:TAIR.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; TAS:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IDA:TAIR.
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; 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; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P93654"
FT CHAIN 2..279
FT /note="Syntaxin-21"
FT /id="PRO_0000210253"
FT TOPO_DOM 2..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 186..248
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..94
FT /evidence="ECO:0000255"
FT COMPBIAS 16..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 CONFLICT 14
FT /note="A -> T (in Ref. 5; AAM66128)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="I -> T (in Ref. 5; AAM66128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 31061 MW; EDAB4B07CC377CE3 CRC64;
MSFQDLEAGT RSPAPNRFTG GRQQRPSSRG DPSQEVAAGI FRISTAVNSF FRLVNSIGTP
KDTLELRDKL QKTRLQISEL VKNTSAKLKE ASEADLHGSA SQIKKIADAK LAKDFQSVLK
EFQKAQRLAA EREITYTPVV TKEIPTSYNA PELDTESLRI SQQQALLLQS RRQEVVFLDN
EITFNEAIIE EREQGIREIE DQIRDVNGMF KDLALMVNHQ GNIVDDISSN LDNSHAATTQ
ATVQLRKAAK TQRSNSSLTC LLILIFGIVL LIVIIVVLV
