[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1074/jbc.273.22.13371; PubMed=9593663 [NCBI, ExPASy, EBI, Israel, Japan] Hosaka M., Suedhof T.C.; "Synapsin III, a novel synapsin with an unusual regulation by Ca2+."; J. Biol. Chem. 273:13371-13374(1998).
[2]	INTERACTION WITH CAPON. DOI=10.1073/pnas.261705799; PubMed=11867766 [NCBI, ExPASy, EBI, Israel, Japan] Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.; "Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON."; Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).

Comments

FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed.
SUBUNIT: Interacts with CAPON.
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles.
TISSUE SPECIFICITY: Expressed primarily in brain.
MISCELLANEOUS: Regulated by calcium.
SIMILARITY: Belongs to the synapsin family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF056704; AAC24521.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00390215; -.

NP_058805.1; -.

3D structure databases

HSSP

P17599; 1AUX. [HSSP ENTRY / PDB]

SMR

O70441; 90-395.

ModBase

O70441.

Protein-protein interaction databases

DIP

DIP:358N; -.

PTM databases

PhosphoSite

O70441; -.

Organism-specific databases

RGD

3799; Syn3.

Ontologies

GO:0030054;	Cellular component: cell junction (inferred from electronic annotation from UniProtKB-KW).
GO:0030141;	Cellular component: secretory granule (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030672;	Cellular component: synaptic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from direct assay from RGD).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003824;	Molecular function: catalytic activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007269;	Biological process: neurotransmitter secretion (traceable author statement from RGD).
QuickGo view.

Family and domain databases

InterPro

IPR013816; ATP_grasp_subdomain_2.
IPR001359; Synapsin.
IPR019735; Synapsin_CS.
IPR019569; Synapsin_N.
IPR019736; Synapsin_phosporylation.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.

Pfam

PF02078; Synapsin; 1.
PF02750; Synapsin_C; 1.
PF10581; Synapsin_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR01368; SYNAPSIN.

PROSITE

PS00415; SYNAPSIN_1; 1.
PS00416; SYNAPSIN_2; 1.

Genome annotation databases

Ensembl

ENSRNOG00000026866; Rattus norvegicus. [Contig view]

GeneID

29130; -.

KEGG

rno:29130; -.

Phylogenomic databases

HOVERGEN

O70441; -.

OMA

O70441; MQVVRNG.

Other

608075; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Calcium; Cell junction; Cytoplasmic vesicle; Membrane; Nucleotide-binding; Phosphoprotein; Synapse.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 579`	`579`	`Synapsin-3.`	`PRO_0000183026`
`REGION`	`1 28`	`28`	`A.`
`REGION`	`28 90`	`63`	`B; linker.`
`REGION`	`91 398`	`308`	`C; actin-binding and synaptic-vesicle binding.`
`REGION`	`399 530`	`132`	`J; Pro-rich linker.`
`REGION`	`531 579`	`49`	`E.`
`MOD_RES`	`461 461`		`Phosphoserine (By similarity).`
`MOD_RES`	`469 469`		`Phosphoserine (By similarity).`
`MOD_RES`	`483 483`		`Phosphoserine (By similarity).`

Sequence information

Length: 579 AA [This is the length of the unprocessed precursor]

Molecular weight: 63349 Da [This is the MW of the unprocessed precursor]

CRC64: EA69F25ED14A4722 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF 

        70         80         90        100        110        120 
SSFSSAMKQT PQAPTGLMEP PTPVTPVVQR PRILLVIDDA HTDWSKYFHG KKVNGDIEIR 

       130        140        150        160        170        180 
VEQAEFSELN LAAYVTGGCM VDMQVVRNGT KIVRSFKPDF ILVRQHAYSM ALAEDYRSLV 

       190        200        210        220        230        240 
IGLQYGGLPA VNSLYSVYNF CSKPWVFSQL IKIFHSLGPE KFPLVEQTFF PNHKPMLTAP 

       250        260        270        280        290        300 
NFPVVIKLGH AHAGMGKIKV ENQHDYQDIT SVVAMAKTYA TTEAFIDSKY DIRIQKIGSN 

       310        320        330        340        350        360 
YKAYMRTSIS GNWKANTGSA MLEQVAMTER YRLWVDSCSE MFGGLDICAV KAVHSKNGRD 

       370        380        390        400        410        420 
YIIEVMDSSM PLIGEHVEED KQLMADLVVS KMSQLLVPGA SVPSPLRPWG PQTKSAKSPG 

       430        440        450        460        470        480 
QGQLGPLLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQQPVSP QSGSPQQQRS 

       490        500        510        520        530        540 
PGSPQLSRAS GGSSPNQASK PTASLSSHTR PPVQGRSTSQ QGEEPQKTAS PHPHLNKSQS 

       550        560        570 
LTNSLSTSDT SHRGTPSEDE AKAETIRNLR KSFASLFSD

O70441 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools