SYT5_RAT
ID SYT5_RAT Reviewed; 386 AA.
AC P47861; Q56A28;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Synaptotagmin-5;
DE AltName: Full=Synaptotagmin IX;
DE AltName: Full=Synaptotagmin V;
DE Short=SytV;
GN Name=Syt5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7698322; DOI=10.1016/0014-5793(95)00176-a;
RA Craxton M.A., Goedert M.;
RT "Synaptotagmin V: a novel synaptotagmin isoform expressed in rat brain.";
RL FEBS Lett. 361:196-200(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7597049; DOI=10.1073/pnas.92.13.5895;
RA Hudson A.W., Birnbaum M.J.;
RT "Identification of a nonneuronal isoform of synaptotagmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5895-5899(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TUBULIN.
RX PubMed=12966166; DOI=10.1242/jcs.00719;
RA Haberman Y., Grimberg E., Fukuda M., Sagi-Eisenberg R.;
RT "Synaptotagmin IX, a possible linker between the perinuclear endocytic
RT recycling compartment and the microtubules.";
RL J. Cell Sci. 116:4307-4318(2003).
CC -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory
CC vesicles through Ca(2+) and phospholipid binding to the C2 domain or
CC may serve as Ca(2+) sensors in the process of vesicular trafficking and
CC exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine
CC in PC12 cells. Required for export from the endocytic recycling
CC compartment to the cell surface. {ECO:0000269|PubMed:12966166}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250|UniProtKB:O00445};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with both alpha- and
CC beta-tubulin (PubMed:12966166). {ECO:0000250,
CC ECO:0000269|PubMed:12966166}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:12966166}; Single-pass membrane
CC protein {ECO:0000269|PubMed:12966166}. Recycling endosome membrane
CC {ECO:0000269|PubMed:12966166}; Single-pass membrane protein
CC {ECO:0000269|PubMed:12966166}. Note=In mast cells, localizes to the
CC endocytic recycling compartment.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, adipose tissue, lung and
CC heart, as well as at higher levels in brain.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; X84884; CAA59311.1; -; mRNA.
DR EMBL; U26402; AAA81382.1; -; mRNA.
DR EMBL; BC092198; AAH92198.1; -; mRNA.
DR PIR; I59387; I59387.
DR RefSeq; NP_062223.1; NM_019350.2.
DR RefSeq; XP_017445103.1; XM_017589614.1.
DR RefSeq; XP_017445104.1; XM_017589615.1.
DR AlphaFoldDB; P47861; -.
DR SMR; P47861; -.
DR BioGRID; 248527; 1.
DR STRING; 10116.ENSRNOP00000024547; -.
DR iPTMnet; P47861; -.
DR PhosphoSitePlus; P47861; -.
DR jPOST; P47861; -.
DR PaxDb; P47861; -.
DR PRIDE; P47861; -.
DR Ensembl; ENSRNOT00000024547; ENSRNOP00000024547; ENSRNOG00000018217.
DR GeneID; 54309; -.
DR KEGG; rno:54309; -.
DR UCSC; RGD:3806; rat.
DR CTD; 6861; -.
DR RGD; 3806; Syt5.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000161816; -.
DR HOGENOM; CLU_023008_0_1_1; -.
DR InParanoid; P47861; -.
DR OMA; CLCRKRC; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; P47861; -.
DR TreeFam; TF315600; -.
DR PRO; PR:P47861; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018217; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; P47861; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; ISO:RGD.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0099066; C:integral component of neuronal dense core vesicle membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990769; C:proximal neuron projection; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IDA:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0019905; F:syntaxin binding; IDA:BHF-UCL.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR028689; SYT5.
DR PANTHER; PTHR10024:SF282; PTHR10024:SF282; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Endosome; Membrane; Metal-binding;
KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Synaptotagmin-5"
FT /id="PRO_0000183953"
FT TOPO_DOM 1..24
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 108..227
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 239..372
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VARIANT 182
FT /note="P -> S"
FT VARIANT 237
FT /note="Missing"
SQ SEQUENCE 386 AA; 43127 MW; 51B881ADD46E3FD6 CRC64;
MFPEPPTPGS PAPETPPDSS RIRQGAVPAW VLATILLGSG LLVFSSCFCL YRKRCRRRMG
KKSQAQAQVH LQEVKELGRS YIDKVQPEIE ELDPSPSMPG QQVLDKHQLG RLQYSLDYDF
QTGQLLVGIL QAEGLAALDL GGSSDPYVSV YLLPDKRRRH ETKVHRQTLN PHFGETFAFK
VPYVELGGRV LVMAVYDFDR FSRNDAIGEV RVPMSSVNLG RPVQAWRELQ VAPKEEQEKL
GDICFSLRYV PTAGKLTVIV LEAKNLKKMD VGGLSDPYVK VHLLQGGKKV RKKKTTIKKN
TLNPYYNEAF SFEVPCDQVQ KVQVELTVLD YDKLGKNEAI GRVAVGTAVG GAGLRHWADM
LANPRRPIAQ WHSLRPPDRA RPIPAP
