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SYP31_ARATH
ID   SYP31_ARATH             Reviewed;         336 AA.
AC   Q9FFK1; O65099;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Syntaxin-31;
DE            Short=AtSED5;
DE            Short=AtSYP31;
GN   Name=SYP31; OrderedLocusNames=At5g05760; ORFNames=MJJ3.17;
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. Columbia;
RX   PubMed=10888666; DOI=10.1091/mbc.11.7.2251;
RA   Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT   "AtVPS45 complex formation at the trans-Golgi network.";
RL   Mol. Biol. Cell 11:2251-2265(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   SUBCELLULAR LOCATION, AND INTERACTION WITH CDC48A.
RX   PubMed=12427991; DOI=10.1104/pp.011742;
RA   Rancour D.M., Dickey C.E., Park S., Bednarek S.Y.;
RT   "Characterization of AtCDC48. Evidence for multiple membrane fusion
RT   mechanisms at the plane of cell division in plants.";
RL   Plant Physiol. 130:1241-1253(2002).
CC   -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC       pathway. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the t-SNARE complex. Interacts with CDC48A, but not
CC       with VPS45. {ECO:0000269|PubMed:12427991}.
CC   -!- INTERACTION:
CC       Q9FFK1; Q8VZW1: NIP1-1; NbExp=2; IntAct=EBI-4434817, EBI-4424378;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
CC       Cytoplasm {ECO:0000269|PubMed:12427991}. Endosome
CC       {ECO:0000269|PubMed:12427991}. Note=During cytokinesis, also found in
CC       the division plane.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; AF051853; AAC06291.1; -; mRNA.
DR   EMBL; AB005237; BAB09670.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90921.1; -; Genomic_DNA.
DR   EMBL; AY054184; AAL06845.1; -; mRNA.
DR   EMBL; AY066041; AAL47408.1; -; mRNA.
DR   RefSeq; NP_196195.1; NM_120658.5.
DR   AlphaFoldDB; Q9FFK1; -.
DR   BioGRID; 15740; 47.
DR   IntAct; Q9FFK1; 38.
DR   STRING; 3702.AT5G05760.1; -.
DR   PaxDb; Q9FFK1; -.
DR   PRIDE; Q9FFK1; -.
DR   ProteomicsDB; 233056; -.
DR   EnsemblPlants; AT5G05760.1; AT5G05760.1; AT5G05760.
DR   GeneID; 830461; -.
DR   Gramene; AT5G05760.1; AT5G05760.1; AT5G05760.
DR   KEGG; ath:AT5G05760; -.
DR   Araport; AT5G05760; -.
DR   TAIR; locus:2166419; AT5G05760.
DR   eggNOG; KOG0812; Eukaryota.
DR   HOGENOM; CLU_044998_0_0_1; -.
DR   InParanoid; Q9FFK1; -.
DR   OMA; MGATKQL; -.
DR   OrthoDB; 1297427at2759; -.
DR   PhylomeDB; Q9FFK1; -.
DR   PRO; PR:Q9FFK1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FFK1; baseline and differential.
DR   Genevisible; Q9FFK1; AT.
DR   GO; GO:0009504; C:cell plate; IDA:TAIR.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA: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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; 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   InterPro; IPR010989; SNARE.
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   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Endosome; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..336
FT                   /note="Syntaxin-31"
FT                   /id="PRO_0000210256"
FT   TOPO_DOM        1..314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          244..306
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          23..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        136
FT                   /note="T -> A (in Ref. 1; AAC06291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  37311 MW;  64D40450D7ACF0F6 CRC64;
     MGSTFRDRTV ELHSLSQTLK KIGAIPSVHQ DEDDPASSKR SSPGSEFNKK ASRIGLGIKE
     TSQKITRLAK LAKQSTIFND RTVEIQELTV LIRNDITGLN MALSDLQTLQ NMELADGNYS
     QDQVGHYTAV CDDLKTRLMG ATKQLQDVLT TRSENMKAHE NRKQLFSTKN AVDSPPQNNA
     KSVPEPPPWS SSSNPFGNLQ QPLLPPLNTG APPGSQLRRR SAIENAPSQQ MEMSLLQQTV
     PKQENYSQSR AVALHSVESR ITELSGIFPQ LATMVTQQGE LAIRIDDNMD ESLVNVEGAR
     SALLQHLTRI SSNRWLMMKI FAVIILFLIV FLFFVA
 
 
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