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SYT3_ARATH
ID   SYT3_ARATH              Reviewed;         540 AA.
AC   Q7XA06; B6ETT6; Q9FYD9;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Synaptotagmin-3;
DE   AltName: Full=NTMC2T1.3;
DE   AltName: Full=Synaptotagmin C;
GN   Name=SYT3; Synonyms=SYTC; OrderedLocusNames=At5g04220; ORFNames=F21E1.140;
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] (ISOFORM 1).
RX   PubMed=12801916; DOI=10.1093/jb/mvg082;
RA   Fukuda M.;
RT   "Molecular cloning, expression, and characterization of a novel class of
RT   synaptotagmin (Syt XIV) conserved from Drosophila to humans.";
RL   J. Biochem. 133:641-649(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=17672888; DOI=10.1186/1471-2164-8-259;
RA   Craxton M.;
RT   "Evolutionary genomics of plant genes encoding N-terminal-TM-C2 domain
RT   proteins and the similar FAM62 genes and synaptotagmin genes of
RT   metazoans.";
RL   BMC Genomics 8:259-259(2007).
RN   [3]
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   [4]
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).
CC   -!- FUNCTION: May be involved in membrane trafficking. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7XA06-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7XA06-2; Sequence=VSP_044138;
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC05504.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB102952; BAC76813.1; -; mRNA.
DR   EMBL; FM213367; CAR82572.1; -; mRNA.
DR   EMBL; FM213368; CAR82573.1; -; mRNA.
DR   EMBL; AL391716; CAC05504.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90712.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90713.1; -; Genomic_DNA.
DR   RefSeq; NP_568135.1; NM_120504.2. [Q7XA06-2]
DR   RefSeq; NP_974729.1; NM_203000.2. [Q7XA06-1]
DR   AlphaFoldDB; Q7XA06; -.
DR   SMR; Q7XA06; -.
DR   STRING; 3702.AT5G04220.2; -.
DR   iPTMnet; Q7XA06; -.
DR   PaxDb; Q7XA06; -.
DR   PRIDE; Q7XA06; -.
DR   ProteomicsDB; 234109; -. [Q7XA06-1]
DR   EnsemblPlants; AT5G04220.1; AT5G04220.1; AT5G04220. [Q7XA06-2]
DR   EnsemblPlants; AT5G04220.2; AT5G04220.2; AT5G04220. [Q7XA06-1]
DR   GeneID; 830301; -.
DR   Gramene; AT5G04220.1; AT5G04220.1; AT5G04220. [Q7XA06-2]
DR   Gramene; AT5G04220.2; AT5G04220.2; AT5G04220. [Q7XA06-1]
DR   KEGG; ath:AT5G04220; -.
DR   Araport; AT5G04220; -.
DR   TAIR; locus:2146688; AT5G04220.
DR   eggNOG; KOG1012; Eukaryota.
DR   HOGENOM; CLU_028927_1_0_1; -.
DR   InParanoid; Q7XA06; -.
DR   PhylomeDB; Q7XA06; -.
DR   PRO; PR:Q7XA06; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q7XA06; baseline and differential.
DR   Genevisible; Q7XA06; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.150; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR031468; SMP_LBD.
DR   InterPro; IPR045050; Synaptotagmin_plant.
DR   InterPro; IPR039010; Synaptotagmin_SMP.
DR   PANTHER; PTHR10774; PTHR10774; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF17047; SMP_LBD; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS51847; SMP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Lipid transport; Lipid-binding; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..540
FT                   /note="Synaptotagmin-3"
FT                   /id="PRO_0000419240"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          67..249
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT   DOMAIN          240..363
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          401..521
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          227..509
FT                   /note="Phospholipid binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         277
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         341
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   VAR_SEQ         1..227
FT                   /note="MGFFTSVLGIIGFVIGIPIGLILGFFVLIYSQPSHQEYPPARPLVETSISVL
FT                   LDLLPDIPLWMKNPDYERVDWFNKFISYMWPYLDKAVCGIIRSSVQPLFADYIGTFCIE
FT                   SIEFENLSLGTLPPTVHGVKFYETNEKELLFEPSIKWAGNPNIVLVLKVLSLRIRVQLV
FT                   DLQFFAIVRVALKPLLPTFPCFGMVVVSLMEKPHVDFGLKVLGGDLMSIPGLYRYVQ
FT                   -> MILLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17672888"
FT                   /id="VSP_044138"
SQ   SEQUENCE   540 AA;  61870 MW;  FC5FE33A40A6DB1E CRC64;
     MGFFTSVLGI IGFVIGIPIG LILGFFVLIY SQPSHQEYPP ARPLVETSIS VLLDLLPDIP
     LWMKNPDYER VDWFNKFISY MWPYLDKAVC GIIRSSVQPL FADYIGTFCI ESIEFENLSL
     GTLPPTVHGV KFYETNEKEL LFEPSIKWAG NPNIVLVLKV LSLRIRVQLV DLQFFAIVRV
     ALKPLLPTFP CFGMVVVSLM EKPHVDFGLK VLGGDLMSIP GLYRYVQETI KRQVSSMYHW
     PQVLEIPILD SSTASVKKPV GLLHVSILRA RNLLKKDLLG TSDPYVKLSL TGEKLPAKKT
     TIKKRNLNPE WNEHFKLIVK DPNSQVLQLE VFDWDKVGGH DRLGMQMIPL QKINPGERKE
     FNLDLIKNSN VVMDSGDKKK RGRLEVDLRY VPFREESIKR RKESREEKSS EDDDFLSQAG
     LLSVAVQSAK DVEGKKKHSN PYAVVLFRGE KKKTKMLKKT RDPRWNEEFQ FTLEEPPVKE
     SIRVEVMSKG TGFHFRSKEE LGHVDINLDD VVDNGRINQK YHLINSRNGI IHIEIRWTTS
 
 
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