SYN3_HUMAN
ID SYN3_HUMAN Reviewed; 580 AA.
AC O14994; B1B1F9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Synapsin-3;
DE AltName: Full=Synapsin III;
GN Name=SYN3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9539796; DOI=10.1073/pnas.95.8.4667;
RA Kao H.-T., Porton B., Czernik A.J., Feng J., Yiu G., Haering M.,
RA Benfenati F., Greengard P.;
RT "A third member of the synapsin gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4667-4672(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP PHOSPHORYLATION AT SER-470, AND VARIANT ASN-470.
RX PubMed=14732590; DOI=10.1016/j.biopsych.2003.07.002;
RA Porton B., Ferreira A., DeLisi L.E., Kao H.T.;
RT "A rare polymorphism affects a mitogen-activated protein kinase site in
RT synapsin III: possible relationship to schizophrenia.";
RL Biol. Psychiatry 55:118-125(2004).
CC -!- FUNCTION: May be involved in the regulation of neurotransmitter release
CC and synaptogenesis.
CC -!- SUBUNIT: Interacts with CAPON. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Peripheral membrane protein localized to the cytoplasmic surface
CC of synaptic vesicles.
CC -!- TISSUE SPECIFICITY: Neuron specific. Detected predominantly in brain.
CC -!- DOMAIN: The A region binds phospholipids with a preference for
CC negatively charged species. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC vesicles. {ECO:0000250}.
CC -!- MISCELLANEOUS: Regulated by calcium. Calcium inhibits ATP binding to
CC the C-domain.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR EMBL; AF046873; AAC15101.1; -; mRNA.
DR EMBL; CR456589; CAG30475.1; -; mRNA.
DR EMBL; Z83846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z71183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z80902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60034.1; -; Genomic_DNA.
DR EMBL; BC075065; AAH75065.1; -; mRNA.
DR EMBL; BC075066; AAH75066.1; -; mRNA.
DR EMBL; BC143874; AAI43875.1; -; mRNA.
DR CCDS; CCDS13908.1; -.
DR RefSeq; NP_003481.3; NM_003490.3.
DR RefSeq; NP_598344.2; NM_133633.2.
DR RefSeq; XP_011528707.1; XM_011530405.2.
DR RefSeq; XP_011528708.1; XM_011530406.2.
DR RefSeq; XP_011528709.1; XM_011530407.2.
DR RefSeq; XP_011528710.1; XM_011530408.1.
DR RefSeq; XP_016884449.1; XM_017028960.1.
DR RefSeq; XP_016884450.1; XM_017028961.1.
DR RefSeq; XP_016884451.1; XM_017028962.1.
DR RefSeq; XP_016884452.1; XM_017028963.1.
DR PDB; 2P0A; X-ray; 1.90 A; A/B=76-417.
DR PDBsum; 2P0A; -.
DR AlphaFoldDB; O14994; -.
DR SMR; O14994; -.
DR BioGRID; 113857; 13.
DR STRING; 9606.ENSP00000351614; -.
DR iPTMnet; O14994; -.
DR PhosphoSitePlus; O14994; -.
DR BioMuta; SYN3; -.
DR EPD; O14994; -.
DR jPOST; O14994; -.
DR MassIVE; O14994; -.
DR PaxDb; O14994; -.
DR PeptideAtlas; O14994; -.
DR PRIDE; O14994; -.
DR ProteomicsDB; 48363; -.
DR ABCD; O14994; 2 sequenced antibodies.
DR Antibodypedia; 25287; 129 antibodies from 22 providers.
DR DNASU; 8224; -.
DR Ensembl; ENST00000358763.7; ENSP00000351614.2; ENSG00000185666.15.
DR GeneID; 8224; -.
DR KEGG; hsa:8224; -.
DR MANE-Select; ENST00000358763.7; ENSP00000351614.2; NM_003490.4; NP_003481.3.
DR UCSC; uc003amx.4; human.
DR CTD; 8224; -.
DR DisGeNET; 8224; -.
DR GeneCards; SYN3; -.
DR HGNC; HGNC:11496; SYN3.
DR HPA; ENSG00000185666; Tissue enriched (brain).
DR MalaCards; SYN3; -.
DR MIM; 602705; gene.
DR neXtProt; NX_O14994; -.
DR OpenTargets; ENSG00000185666; -.
DR PharmGKB; PA36278; -.
DR VEuPathDB; HostDB:ENSG00000185666; -.
DR eggNOG; KOG3895; Eukaryota.
DR GeneTree; ENSGT00940000155415; -.
DR HOGENOM; CLU_010582_3_0_1; -.
DR InParanoid; O14994; -.
DR OMA; FFPNHTQ; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; O14994; -.
DR TreeFam; TF319919; -.
DR PathwayCommons; O14994; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR SignaLink; O14994; -.
DR SIGNOR; O14994; -.
DR BioGRID-ORCS; 8224; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; SYN3; human.
DR EvolutionaryTrace; O14994; -.
DR GeneWiki; SYN3; -.
DR GenomeRNAi; 8224; -.
DR Pharos; O14994; Tbio.
DR PRO; PR:O14994; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O14994; protein.
DR Bgee; ENSG00000185666; Expressed in cortical plate and 117 other tissues.
DR ExpressionAtlas; O14994; baseline and differential.
DR Genevisible; O14994; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; TAS:ProtInc.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; TAS:ParkinsonsUK-UCL.
DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR028712; SYN2/3.
DR InterPro; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR InterPro; IPR019735; Synapsin_CS.
DR InterPro; IPR019736; Synapsin_P_site.
DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR PANTHER; PTHR10841:SF20; PTHR10841:SF20; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR Pfam; PF10581; Synapsin_N; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS00415; SYNAPSIN_1; 1.
DR PROSITE; PS00416; SYNAPSIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Cytoplasmic vesicle; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..580
FT /note="Synapsin-3"
FT /id="PRO_0000183024"
FT REGION 1..28
FT /note="A"
FT REGION 19..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..90
FT /note="B; linker"
FT REGION 91..399
FT /note="C; actin-binding and synaptic-vesicle binding"
FT REGION 395..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..531
FT /note="J; Pro-rich linker"
FT REGION 532..580
FT /note="E"
FT COMPBIAS 19..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine; by PKA and CaMK1"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 470
FT /note="Phosphoserine; by CDK1 and MAPK"
FT /evidence="ECO:0000269|PubMed:14732590"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70441"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP2"
FT VARIANT 470
FT /note="S -> N (in patients affected by schizophrenia;
FT dbSNP:rs5998526)"
FT /evidence="ECO:0000269|PubMed:14732590"
FT /id="VAR_068906"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2P0A"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:2P0A"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:2P0A"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 289..298
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 301..312
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 340..344
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 347..356
FT /evidence="ECO:0007829|PDB:2P0A"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2P0A"
FT HELIX 378..394
FT /evidence="ECO:0007829|PDB:2P0A"
SQ SEQUENCE 580 AA; 63303 MW; 4F61DE236DE8F3C5 CRC64;
MNFLRRRLSD SSFMANLPNG YMTDLQRPDS STSSPASPAM ERRHPQPLAA SFSSPGSSLF
SSLSSAMKQA PQATSGLMEP PGPSTPIVQR PRILLVIDDA HTDWSKYFHG KKVNGEIEIR
VEQAEFSELN LAAYVTGGCM VDMQVVRNGT KVVSRSFKPD FILVRQHAYS MALGEDYRSL
VIGLQYGGLP AVNSLYSVYN FCSKPWVFSQ LIKIFHSLGP EKFPLVEQTF FPNHKPMVTA
PHFPVVVKLG HAHAGMGKIK VENQLDFQDI TSVVAMAKTY ATTEAFIDSK YDIRIQKIGS
NYKAYMRTSI SGNWKANTGS AMLEQVAMTE RYRLWVDSCS EMFGGLDICA VKAVHSKDGR
DYIIEVMDSS MPLIGEHVEE DRQLMADLVV SKMSQLPMPG GTAPSPLRPW APQIKSAKSP
GQAQLGPQLG QPQPRPPPQG GPRQAQSPQP QRSGSPSQQR LSPQGQQPLS PQSGSPQQQR
SPGSPQLSRA SSGSSPNQAS KPGATLASQP RPPVQGRSTS QQGEESKKPA PPHPHLNKSQ
SLTNSLSTSD TSQRGTPSED EAKAETIRNL RKSFASLFSD
