SYT6_RAT
ID SYT6_RAT Reviewed; 511 AA.
AC Q62746; Q4KLI6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Synaptotagmin-6;
DE AltName: Full=Synaptotagmin VI;
DE Short=SytVI;
GN Name=Syt6;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7791877; DOI=10.1038/375594a0;
RA Li C., Ullrich B., Zhang J.Z., Anderson R.G.W., Brose N., Suedhof T.C.;
RT "Ca(2+)-dependent and -independent activities of neural and non-neural
RT synaptotagmins.";
RL Nature 375:594-599(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. May mediate Ca(2+)-regulation of exocytosis in acrosomal
CC reaction in sperm (By similarity). {ECO:0000250|UniProtKB:Q9R0N8}.
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:P40748};
CC -!- SUBUNIT: Isoform 1: Homodimer; disulfide-linked via the cysteine motif.
CC Isoform 1: Can also form heterodimers with SYT3, SYT7, SYT9 and SYT10.
CC Isoform 1: Interacts with STX1A, STX1B and STX2; the interaction is
CC Ca(2+)-dependent. Isoform 2: Is not able to form homodimer and
CC heterodimers. {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane
CC {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane protein
CC {ECO:0000250}. Note=Localized predominantly to endoplasmic reticulum
CC (ER) and/or Golgi-like perinuclear compartment (By similarity).
CC {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9R0N8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9R0N8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62746-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62746-2; Sequence=VSP_041730;
CC -!- DOMAIN: The cysteine motif mediates homo- or heterodimer formation via
CC formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; U20105; AAA87724.1; -; mRNA.
DR EMBL; BC099185; AAH99185.1; -; mRNA.
DR PIR; S58399; S58399.
DR RefSeq; NP_071527.1; NM_022191.1. [Q62746-1]
DR AlphaFoldDB; Q62746; -.
DR SMR; Q62746; -.
DR STRING; 10116.ENSRNOP00000025953; -.
DR PhosphoSitePlus; Q62746; -.
DR PaxDb; Q62746; -.
DR PRIDE; Q62746; -.
DR Ensembl; ENSRNOT00000077739; ENSRNOP00000069764; ENSRNOG00000019163. [Q62746-2]
DR GeneID; 60565; -.
DR KEGG; rno:60565; -.
DR UCSC; RGD:62012; rat. [Q62746-1]
DR CTD; 148281; -.
DR RGD; 62012; Syt6.
DR VEuPathDB; HostDB:ENSRNOG00000019163; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000157665; -.
DR InParanoid; Q62746; -.
DR OMA; VMRVGCN; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q62746; -.
DR PRO; PR:Q62746; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019163; Expressed in thymus and 7 other tissues.
DR ExpressionAtlas; Q62746; baseline and differential.
DR Genevisible; Q62746; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0099699; C:integral component of synaptic membrane; IDA:SynGO.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0030276; F:clathrin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein 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:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:RGD.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; ISO:RGD.
DR GO; GO:0007340; P:acrosome reaction; ISO:RGD.
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:0099525; P:presynaptic dense core vesicle exocytosis; IDA:SynGO.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; 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; IPR028701; SYT6.
DR PANTHER; PTHR10024:SF45; PTHR10024:SF45; 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 Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Disulfide bond; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..511
FT /note="Synaptotagmin-6"
FT /id="PRO_0000183956"
FT TOPO_DOM 1..59
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 230..351
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 362..495
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 12..38
FT /note="Cysteine motif"
FT /evidence="ECO:0000250|UniProtKB:O35681"
FT REGION 93..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..511
FT /note="Necessary for cell membrane association (isoform 2)"
FT /evidence="ECO:0000250|UniProtKB:Q9R0N8"
FT COMPBIAS 93..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T7P8"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041730"
SQ SEQUENCE 511 AA; 57179 MW; 17773C73BEC0FAF8 CRC64;
MSGVWGAGGP RCQAALAVLA SLCRARPPPL GLDVETCQSF ELQPPEQSPS AADSGTSVSL
LAVVVIVCGV ALVAVFFFLF WKLCWMPWRN KEASSPSSAN PASEILQSPS SRGNMADKLK
DPSALGFLEA AVKISHTSPD IPAEVQMSVK EHIMRHTKLQ RQTTEPASST RHTSFKRHLP
RQMHVSSVDY GNELPPAAAE QPTSIGRIKP ELYKQKSVDG DEAKSEAAKS CGKINFSLRY
DYESETLIVR ILKAFDLPAK DFCGSSDPYV KIYLLPDRKC KLQTRVHRKT LNPTFDENFH
FPVPYEELAD RKLHLSVFDF DRFSRHDMIG EVILDNLFEA SDLSRETSIW KDIQYATSES
VDLGEIMFSL CYLPTAGRLT LTVIKCRNLK AMDITGYSDP YVKVSLLCDG RRLKKKKTTI
KKNTLNPVYN EAIIFDIPPE NMDQVSLLIS VMDYDRVGHN EIIGVCRVGI SAEGLGRDHW
NEMLAYPRKP IAHWHCLAEV KKSFKEGTPR L
