SYT4_ARATH
ID SYT4_ARATH Reviewed; 569 AA.
AC A0JJX5; Q9FY55;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Synaptotagmin-4;
DE AltName: Full=NTMC2T2.2;
DE AltName: Full=Synaptotagmin D;
GN Name=SYT4; Synonyms=SYTD; OrderedLocusNames=At5g11100; ORFNames=T5K6.90;
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].
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 [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).
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 -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC03458.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM410051; CAL64988.1; -; mRNA.
DR EMBL; AL391222; CAC03458.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91635.1; -; Genomic_DNA.
DR PIR; T51799; T51799.
DR RefSeq; NP_196671.2; NM_121148.3.
DR AlphaFoldDB; A0JJX5; -.
DR SMR; A0JJX5; -.
DR STRING; 3702.AT5G11100.1; -.
DR PaxDb; A0JJX5; -.
DR PRIDE; A0JJX5; -.
DR ProteomicsDB; 234179; -.
DR GeneID; 830978; -.
DR KEGG; ath:AT5G11100; -.
DR Araport; AT5G11100; -.
DR TAIR; locus:2184931; AT5G11100.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_479515_0_0_1; -.
DR InParanoid; A0JJX5; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; A0JJX5; -.
DR PRO; PR:A0JJX5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A0JJX5; baseline and differential.
DR Genevisible; A0JJX5; 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 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 Calcium; Lipid transport; Lipid-binding; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..569
FT /note="Synaptotagmin-4"
FT /id="PRO_0000419241"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 67..251
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 245..366
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 426..543
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 229..531
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 569 AA; 63609 MW; 396D0ED18C4A4454 CRC64;
MGFLFGLFIG IAVSFGLVVA FARYSSVRST RRADLAKTIA AFARMTVQDS RKLLPGDFYP
SWVVFSQRQK LNWLNLELEK IWPYVNEAAS ELIKSSVEPV LEQYTPAMLA SLKFSKFTLG
TVAPQFTGVS ILESESGPNG ITMELEMQWD GNPKIVLDVK TLLGVSLPIE VKNIGFTGVF
RLIFKPLVDE FPCFGALSYS LREKKGLDFT LKVIGGELTS IPGISDAIEE TIRDAIEDSI
TWPVRKIIPI LPGDYSDLEL KPVGKLDVKV VQAKDLANKD MIGKSDPYAI VFIRPLPDRT
KKTKTISNSL NPIWNEHFEF IVEDVSTQHL TVRVFDDEGV GSSQLIGAAQ VPLNELVPGK
VKDIWLKLVK DLEIQRDTKN RGQVQLELLY CPLGKEGGLK NPFNPDYSLT ILEKVLKPES
EDSDATDMKK LVTSKKKDVI VRGVLSVTVV AAEDLPAVDF MGKADAFVVI TLKKSETKSK
TRVVPDSLNP VWNQTFDFVV EDALHDLLTL EVWDHDKFGK DKIGRVIMTL TRVMLEGEFQ
EWFELDGAKS GKLCVHLKWT PRLKLRDAS
