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Protein

Synaptotagmin-7

Gene

Syt7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ca2+ sensor involved in Ca2+-dependent exocytosis of secretory and synaptic vesicles through Ca2+ and phospholipid binding to the C2 domain (PubMed:11395007, PubMed:10725327, PubMed:11511344). Ca2+ induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (PubMed:11395007). SYT7 binds Ca2+ with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca2+-triggered lysosomal exocytosis, a major component of the plasma membrane repair (PubMed:10725327, PubMed:11511344). Ca2+-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages. Ca2+-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts. Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes. Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca2+ into the axon terminal after spike generation, increasing the release probability of neurotransmitters. Probably mediates synaptic facilitation by directly increasing the probability of release. May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca2+ and by forming a complex with calmodulin. Also acts as a regulator of Ca2+-dependent insulin and glucagon secretion in beta-cells. Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (By similarity). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (PubMed:15456748).By similarity4 Publications

Cofactori

Ca2+1 Publication1 PublicationNote: Binds 3 Ca2+ ions per C2 domain. The ions are bound to the C2 domains.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi166 – 1661Calcium 1By similarity
Metal bindingi166 – 1661Calcium 2By similarity
Metal bindingi172 – 1721Calcium 11 Publication
Metal bindingi225 – 2251Calcium 11 Publication
Metal bindingi225 – 2251Calcium 21 Publication
Metal bindingi227 – 2271Calcium 1By similarity
Metal bindingi227 – 2271Calcium 2By similarity
Metal bindingi227 – 2271Calcium 3By similarity
Metal bindingi230 – 2301Calcium 3By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi297 – 2971Calcium 4By similarity
Metal bindingi297 – 2971Calcium 5By similarity
Metal bindingi303 – 3031Calcium 5By similarity
Metal bindingi357 – 3571Calcium 4By similarity
Metal bindingi357 – 3571Calcium 5By similarity
Metal bindingi359 – 3591Calcium 4By similarity
Metal bindingi359 – 3591Calcium 5By similarity
Metal bindingi359 – 3591Calcium 6By similarity
Metal bindingi362 – 3621Calcium 6By similarity
Metal bindingi365 – 3651Calcium 4By similarity
Metal bindingi365 – 3651Calcium 6By similarity

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: RGD
  • calmodulin binding Source: UniProtKB
  • clathrin binding Source: BHF-UCL
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • syntaxin binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

Calcium, Calmodulin-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-7Curated
Alternative name(s):
Protein Syt7Imported
Synaptotagmin VII1 Publication
Short name:
SytVII1 Publication
Gene namesi
Name:Syt7Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi62013. Syt7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616VesicularSequence analysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence analysisAdd
BLAST
Topological domaini38 – 403366CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • dense core granule Source: RGD
  • early phagosome Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • lysosome Source: UniProtKB
  • peroxisome Source: UniProtKB
  • plasma membrane Source: RGD
  • synaptic vesicle Source: UniProtKB
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane, Peroxisome, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721D → N: Loss of Ca(2+)-binding in the first C2 domain; when associated with N-225. 1 Publication
Mutagenesisi225 – 2251D → N: Loss of Ca(2+)-binding in the first C2 domain; when associated with N-172. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Synaptotagmin-7PRO_0000436055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei58 – 581PhosphothreonineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei122 – 1221PhosphoserineBy similarity

Post-translational modificationi

Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Expressioni

Gene expression databases

ExpressionAtlasiQ62747. baseline and differential.

Interactioni

Subunit structurei

Homodimer. Can also form heterodimers with SYT6, SYT9 and SYT10. Interacts with calmodulin (CALM1, CALM2 or CALM3). Interacts with CD63; required for localization to lysosomes.By similarity

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • clathrin binding Source: BHF-UCL
  • syntaxin binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-61710N.
STRINGi10116.ENSRNOP00000031195.

Structurei

3D structure databases

SMRiQ62747. Positions 133-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini150 – 23990C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini280 – 37192C2 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The C2 domains bind Ca2+ and membranes (PubMed:11823420). Binding to membranes involves Ca2+-dependent phospholipid binding (PubMed:11823420). Compared to other members of the family, the C2 domains of SYT7 dock and insert into cellular membranes in response to intracellular Ca2+ concentrations that are lower than those required for other synaptotagmins. The two C2 domains bind independently to planar membranes, without interdomain cooperativity. Moreover, SYT7 C2 domains insert more deeply into membranes compared to other synaptotagmins (By similarity).By similarity1 Publication

Sequence similaritiesi

Belongs to the synaptotagmin family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDM6. Eukaryota.
ENOG410XS7N. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
KOiK19907.
OMAiARGRWHT.
OrthoDBiEOG78PV8W.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62747-1) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIs1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK
60 70 80 90 100
NSLETVGTPD SGRGRGEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTEP
110 120 130 140 150
RSSVSDLVNS LTSEMLMLSP GSEEDEAHEG CSRENLGRIQ FSVGYNFQES
160 170 180 190 200
TLTVKVMKAQ ELPAKDFSGT SDPFVKIYLL PDKKHKLETK VKRKNLNPHW
210 220 230 240 250
NETFLFEGFP YEKVVQRILY LQVLDYDRFS RNDPIGEVSI PLNKVDLTQM
260 270 280 290 300
QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG
310 320 330 340 350
TSDPYVKVWL MYKDKRVEKK KTVTKKRNLN PIFNESFAFD IPTEKLRETT
360 370 380 390 400
IIITVMDKDK LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ

LKA
Note: Major isoform.1 Publication
Length:403
Mass (Da):45,482
Last modified:November 1, 1996 - v1
Checksum:i3153FD7FC1DEEEFB
GO
Isoform 2 (identifier: Q62747-2) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIL1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NDLDRDFWNN...QNQNAQGDKR

Show »
Length:687
Mass (Da):75,816
Checksum:i9D085A6E7B3794A1
GO
Isoform 3 (identifier: Q62747-3) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIId1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NDLDRDFWNN...QNQNAQGDKR

Show »
Length:611
Mass (Da):68,335
Checksum:i3BDC3B272C47F56F
GO
Isoform 4 (identifier: Q62747-4) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIe1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NGTLLSGAKV...QNQNAQGDKR

Show »
Length:643
Mass (Da):70,617
Checksum:i5507974FFE5AFDDE
GO
Isoform 5 (identifier: Q62747-5) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIb1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NDLDRDFWNN...LAAGKLNLSK

Show »
Length:523
Mass (Da):58,162
Checksum:i78E6D8BE0CBD2DC3
GO
Isoform 6 (identifier: Q62747-6) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIc1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NFEDSTLSTA...QNQNAQGDKR

Show »
Length:567
Mass (Da):63,137
Checksum:i4BAF44D0ED872FE1
GO
Isoform 7 (identifier: Q62747-7) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIa1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: K → NGTLLSGAKV...QNQNAQGDKR

Show »
Length:520
Mass (Da):57,442
Checksum:i409B9696CD46B502
GO
Isoform 8 (identifier: Q62747-8) [UniParc]FASTAAdd to basket

Also known as: Synaptotagmin VIIT11 Publication

, Synaptotagmin VIIT21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     72-122: KLPAGGKAVN...SEMLMLSPGS → NDLDRDFWNN...LSLNPLFLRR
     123-403: Missing.

Show »
Length:122
Mass (Da):13,768
Checksum:i8AC5E757E3F4E417
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei72 – 12251KLPAG…LSPGS → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNPLFLRR in isoform 8. VSP_058238Add
BLAST
Alternative sequencei72 – 721K → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNGTLLSGAKVATAAAG LAVEREGRLGEKPAPVPPPG EDALRSGGAAPSEPGSSGKA GRGRWRMVQSHLAAGKLNLS NFEDSTLSTATTLESIPSSA GEPKCQRPRTLMRQQSLQQP LSQNQRGRQPSQPTTSQSLG QLQAHAASAPGSNPRAYGRG QARQGTSAGSKYRAAGGRSR SNPGSWDHVVGQIRNRGLDM KSFLEGRMVVLSLVLGLSEQ DDFANIPDLQNPGTQQNQNA QGDKR in isoform 2. VSP_058239
Alternative sequencei72 – 721K → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNFEDSTLSTATTLESI PSSAGEPKCQRPRTLMRQQS LQQPLSQNQRGRQPSQPTTS QSLGQLQAHAASAPGSNPRA YGRGQARQGTSAGSKYRAAG GRSRSNPGSWDHVVGQIRNR GLDMKSFLEGRMVVLSLVLG LSEQDDFANIPDLQNPGTQQ NQNAQGDKR in isoform 3. VSP_058240
Alternative sequencei72 – 721K → NGTLLSGAKVATAAAGLAVE REGRLGEKPAPVPPPGEDAL RSGGAAPSEPGSSGKAGRGR WRMVQSHLAAGKLNLSNFED STLSTATTLESIPSSAGEPK CQRPRTLMRQQSLQQPLSQN QRGRQPSQPTTSQSLGQLQA HAASAPGSNPRAYGRGQARQ GTSAGSKYRAAGGRSRSNPG SWDHVVGQIRNRGLDMKSFL EGRMVVLSLVLGLSEQDDFA NIPDLQNPGTQQNQNAQGDK R in isoform 4. VSP_058241
Alternative sequencei72 – 721K → NDLDRDFWNNNESTVQQKWS SYPPKEFILNISPYAPYGDP RLSLNGTLLSGAKVATAAAG LAVEREGRLGEKPAPVPPPG EDALRSGGAAPSEPGSSGKA GRGRWRMVQSHLAAGKLNLS K in isoform 5. VSP_058242
Alternative sequencei72 – 721K → NFEDSTLSTATTLESIPSSA GEPKCQRPRTLMRQQSLQQP LSQNQRGRQPSQPTTSQSLG QLQAHAASAPGSNPRAYGRG QARQGTSAGSKYRAAGGRSR SNPGSWDHVVGQIRNRGLDM KSFLEGRMVVLSLVLGLSEQ DDFANIPDLQNPGTQQNQNA QGDKR in isoform 6. VSP_058243
Alternative sequencei72 – 721K → NGTLLSGAKVATAAAGLAVE REGRLGEKPAPVPPPGEDAL RSGGAAPSEPGSSGKAGRGR WRMVQSHLAAGKLNLSKEGR MVVLSLVLGLSEQDDFANIP DLQNPGTQQNQNAQGDKR in isoform 7. VSP_058244
Alternative sequencei123 – 403281Missing in isoform 8. VSP_058245Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20106 mRNA. Translation: AAA87725.1.
AF336852 mRNA. Translation: AAK01447.1.
AF336853 mRNA. Translation: AAK01448.1.
AF336854 mRNA. Translation: AAK01449.1.
AF336855 mRNA. Translation: AAK01450.1.
AF336856 mRNA. Translation: AAK01451.1.
AF336857 mRNA. Translation: AAK01452.1.
AF336858 mRNA. Translation: AAK01453.1.
AF336859 mRNA. Translation: AAK01454.1.
AF336860 mRNA. Translation: AAK01455.1.
AC095662 Genomic DNA. No translation available.
AC130565 Genomic DNA. No translation available.
CH473953 Genomic DNA. Translation: EDM12801.1.
CH473953 Genomic DNA. Translation: EDM12802.1.
CH473953 Genomic DNA. Translation: EDM12803.1.
CH473953 Genomic DNA. Translation: EDM12804.1.
CH473953 Genomic DNA. Translation: EDM12805.1.
CH473953 Genomic DNA. Translation: EDM12806.1.
CH473953 Genomic DNA. Translation: EDM12807.1.
PIRiS58400.
RefSeqiNP_067691.1. NM_021659.1.
XP_006231127.1. XM_006231065.2.
XP_006231129.1. XM_006231067.2.
XP_006231130.1. XM_006231068.2.
UniGeneiRn.91884.

Genome annotation databases

EnsembliENSRNOT00000007429; ENSRNOP00000007429; ENSRNOG00000026432. [Q62747-8]
ENSRNOT00000035576; ENSRNOP00000031890; ENSRNOG00000026432. [Q62747-4]
ENSRNOT00000036168; ENSRNOP00000031944; ENSRNOG00000026432. [Q62747-6]
ENSRNOT00000036180; ENSRNOP00000032388; ENSRNOG00000026432. [Q62747-3]
ENSRNOT00000036232; ENSRNOP00000031195; ENSRNOG00000026432. [Q62747-2]
ENSRNOT00000036283; ENSRNOP00000031816; ENSRNOG00000026432. [Q62747-7]
ENSRNOT00000047964; ENSRNOP00000049360; ENSRNOG00000026432. [Q62747-5]
ENSRNOT00000048704; ENSRNOP00000040667; ENSRNOG00000026432. [Q62747-1]
GeneIDi59267.
KEGGirno:59267.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20106 mRNA. Translation: AAA87725.1.
AF336852 mRNA. Translation: AAK01447.1.
AF336853 mRNA. Translation: AAK01448.1.
AF336854 mRNA. Translation: AAK01449.1.
AF336855 mRNA. Translation: AAK01450.1.
AF336856 mRNA. Translation: AAK01451.1.
AF336857 mRNA. Translation: AAK01452.1.
AF336858 mRNA. Translation: AAK01453.1.
AF336859 mRNA. Translation: AAK01454.1.
AF336860 mRNA. Translation: AAK01455.1.
AC095662 Genomic DNA. No translation available.
AC130565 Genomic DNA. No translation available.
CH473953 Genomic DNA. Translation: EDM12801.1.
CH473953 Genomic DNA. Translation: EDM12802.1.
CH473953 Genomic DNA. Translation: EDM12803.1.
CH473953 Genomic DNA. Translation: EDM12804.1.
CH473953 Genomic DNA. Translation: EDM12805.1.
CH473953 Genomic DNA. Translation: EDM12806.1.
CH473953 Genomic DNA. Translation: EDM12807.1.
PIRiS58400.
RefSeqiNP_067691.1. NM_021659.1.
XP_006231127.1. XM_006231065.2.
XP_006231129.1. XM_006231067.2.
XP_006231130.1. XM_006231068.2.
UniGeneiRn.91884.

3D structure databases

SMRiQ62747. Positions 133-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61710N.
STRINGi10116.ENSRNOP00000031195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007429; ENSRNOP00000007429; ENSRNOG00000026432. [Q62747-8]
ENSRNOT00000035576; ENSRNOP00000031890; ENSRNOG00000026432. [Q62747-4]
ENSRNOT00000036168; ENSRNOP00000031944; ENSRNOG00000026432. [Q62747-6]
ENSRNOT00000036180; ENSRNOP00000032388; ENSRNOG00000026432. [Q62747-3]
ENSRNOT00000036232; ENSRNOP00000031195; ENSRNOG00000026432. [Q62747-2]
ENSRNOT00000036283; ENSRNOP00000031816; ENSRNOG00000026432. [Q62747-7]
ENSRNOT00000047964; ENSRNOP00000049360; ENSRNOG00000026432. [Q62747-5]
ENSRNOT00000048704; ENSRNOP00000040667; ENSRNOG00000026432. [Q62747-1]
GeneIDi59267.
KEGGirno:59267.

Organism-specific databases

CTDi9066.
RGDi62013. Syt7.

Phylogenomic databases

eggNOGiENOG410KDM6. Eukaryota.
ENOG410XS7N. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
KOiK19907.
OMAiARGRWHT.
OrthoDBiEOG78PV8W.
TreeFamiTF315600.

Miscellaneous databases

NextBioi35580421.

Gene expression databases

ExpressionAtlasiQ62747. baseline and differential.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015427. Synaptotagmin7.
[Graphical view]
PANTHERiPTHR10024:SF230. PTHR10024:SF230. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins."
    Li C., Ullrich B., Zhang J.Z., Anderson R.G.W., Brose N., Suedhof T.C.
    Nature 375:594-599(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Intestine.
  2. "Synaptotagmin VII as a plasma membrane Ca(2+) sensor in exocytosis."
    Sugita S., Han W., Butz S., Liu X., Fernandez-Chacon R., Lao Y., Sudhof T.C.
    Neuron 30:459-473(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, COFACTOR, MUTAGENESIS OF ASP-172 AND ASP-225.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  5. "Synaptotagmin VII regulates Ca(2+)-dependent exocytosis of lysosomes in fibroblasts."
    Martinez I., Chakrabarti S., Hellevik T., Morehead J., Fowler K., Andrews N.W.
    J. Cell Biol. 148:1141-1149(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes."
    Reddy A., Caler E.V., Andrews N.W.
    Cell 106:157-169(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human."
    Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.
    Biochem. J. 365:173-180(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  8. "Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities."
    Sugita S., Shin O.H., Han W., Lao Y., Suedhof T.C.
    EMBO J. 21:270-280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, DOMAIN, SUBCELLULAR LOCATION.
  9. "Synaptotagmin VII is targeted to dense-core vesicles and regulates their Ca2+ -dependent exocytosis in PC12 cells."
    Fukuda M., Kanno E., Satoh M., Saegusa C., Yamamoto A.
    J. Biol. Chem. 279:52677-52684(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms."
    Bhalla A., Chicka M.C., Chapman E.R.
    J. Biol. Chem. 283:21799-21807(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYT7_RAT
AccessioniPrimary (citable) accession number: Q62747
Secondary accession number(s): F1M262
, Q99J98, Q99P33, Q99P34, Q99P35, Q99P36, Q99P37, Q99P38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2016
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.