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O00445 (SYT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-5
Alternative name(s):
Synaptotagmin V
Short name=SytV
Gene names
Name:SYT5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may serve as Ca2+ sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca2+-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface By similarity.

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.

Subunit structure

Homodimer. Can also form heterodimers with SYT6. Interacts with both alpha- and beta-tubulin By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass membrane protein By similarity. Recycling endosome membrane; Single-pass membrane protein By similarity. Note: In mast cells, localizes to the endocytic recycling compartment By similarity.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasmic vesicle
Endosome
Membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion-dependent exocytosis

Inferred from electronic annotation. Source: InterPro

energy reserve metabolic process

Traceable author statement. Source: Reactome

regulation of insulin secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dense core granule

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium-dependent phospholipid binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Synaptotagmin-5
PRO_0000183951

Regions

Topological domain1 – 2424Vesicular Potential
Transmembrane25 – 4521Helical; Potential
Topological domain46 – 386341Cytoplasmic Potential
Domain124 – 21188C2 1
Domain253 – 34492C2 2

Sites

Metal binding1381Calcium 2; via carbonyl oxygen By similarity
Metal binding1391Calcium 1 By similarity
Metal binding1391Calcium 2 By similarity
Metal binding1451Calcium 1 By similarity
Metal binding1971Calcium 1 By similarity
Metal binding1971Calcium 2 By similarity
Metal binding1981Calcium 1; via carbonyl oxygen By similarity
Metal binding1991Calcium 1 By similarity
Metal binding1991Calcium 2 By similarity
Metal binding1991Calcium 3 By similarity
Metal binding2021Calcium 3 By similarity
Metal binding2051Calcium 2 By similarity
Metal binding2051Calcium 3 By similarity

Natural variations

Natural variant41E → D.
Corresponds to variant rs2301279 [ dbSNP | Ensembl ].
VAR_052240
Natural variant1111R → Q. Ref.4
Corresponds to variant rs11542503 [ dbSNP | Ensembl ].
VAR_034528

Experimental info

Sequence conflict241H → R in BAG54160. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O00445 [UniParc].

Last modified July 11, 2003. Version 2.
Checksum: 96A36792D177FD55

FASTA38642,900
        10         20         30         40         50         60 
MFPEPPTPGP PSPDTPPDSS RISHGPVPPW ALATIVLVSG LLIFSCCFCL YRKSCRRRTG 

        70         80         90        100        110        120 
KKSQAQAQVH LQEVKGLGQS YIDKVQPEVE ELEPAPSGPG QQVADKHELG RLQYSLDYDF 

       130        140        150        160        170        180 
QSGQLLVGIL QAMGLAALDL GGSSDPYVRV YLLPDKRRRY ETKVHRQTLN PHFGETFAFK 

       190        200        210        220        230        240 
VPYVELGGRV LVMAVYDFDR FSRNDAIGEV RVPMSSVDLG RPVQAWRELQ AAPREEQEKL 

       250        260        270        280        290        300 
GDICFSLRYV PTAGKLTVIV LEAKNLKKMD VGGLSDPYVK VHLLQGGKKV RKKKTTIKKN 

       310        320        330        340        350        360 
TLNPYYNEAF SFEVPCDQVQ KVQVELTVLD YDKLGKNEAI GRVAVGAAAG GAGLRHWADM 

       370        380 
LANPRRPIAQ WHSLRPPDRV RLLPAP 

« Hide

References

« Hide 'large scale' references
[1]"Human synaptotagmin V (SYT5): sequence, genomic structure, and chromosomal location."
Craxton M.A., Olsen A., Goedert M.
Genomics 42:165-169(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-111.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96783 Genomic DNA. Translation: CAA65579.1.
AK125182 mRNA. Translation: BAG54160.1.
AC010327 Genomic DNA. No translation available.
BC046157 mRNA. Translation: AAH46157.1.
CCDSCCDS12919.1.
RefSeqNP_003171.2. NM_003180.2.
XP_006723401.1. XM_006723338.1.
XP_006723402.1. XM_006723339.1.
UniGeneHs.631566.

3D structure databases

ProteinModelPortalO00445.
SMRO00445. Positions 108-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112725. 2 interactions.
IntActO00445. 2 interactions.
MINTMINT-1388417.
STRING9606.ENSP00000346265.

PTM databases

PhosphoSiteO00445.

Proteomic databases

MaxQBO00445.
PaxDbO00445.
PRIDEO00445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354308; ENSP00000346265; ENSG00000129990.
ENST00000537500; ENSP00000442896; ENSG00000129990.
GeneID6861.
KEGGhsa:6861.
UCSCuc002qjm.1. human.

Organism-specific databases

CTD6861.
GeneCardsGC19M055684.
HGNCHGNC:11513. SYT5.
HPAHPA010688.
MIM600782. gene.
neXtProtNX_O00445.
PharmGKBPA36294.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292488.
HOGENOMHOG000232127.
HOVERGENHBG005010.
InParanoidO00445.
OMANFAFKVP.
PhylomeDBO00445.
TreeFamTF315600.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO00445.
BgeeO00445.
CleanExHS_SYT5.
GenevestigatorO00445.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028689. SYT5.
[Graphical view]
PANTHERPTHR10024:SF37. PTHR10024:SF37. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSYT5.
GenomeRNAi6861.
NextBio26775.
PROO00445.
SOURCESearch...

Entry information

Entry nameSYT5_HUMAN
AccessionPrimary (citable) accession number: O00445
Secondary accession number(s): B3KWJ8, Q86X72
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2003
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM