SYNJ_CAEEL
ID SYNJ_CAEEL Reviewed; 1119 AA.
AC G5ECL2; B3CJ53; G5EDR8; G5EEJ9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Synaptojanin {ECO:0000303|PubMed:10931870};
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q9D2G5};
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase {ECO:0000250|UniProtKB:Q9D2G5};
DE AltName: Full=Uncoordinated protein 26 {ECO:0000312|WormBase:JC8.10b};
GN Name=unc-26 {ECO:0000312|WormBase:JC8.10b};
GN ORFNames=JC8.10 {ECO:0000312|WormBase:JC8.10b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAG18574.1};
RN [1] {ECO:0000312|EMBL:AAG18574.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10931870; DOI=10.1083/jcb.150.3.589;
RA Harris T.W., Hartwieg E., Horvitz H.R., Jorgensen E.M.;
RT "Mutations in synaptojanin disrupt synaptic vesicle recycling.";
RL J. Cell Biol. 150:589-600(2000).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14622579; DOI=10.1016/s0896-6273(03)00667-6;
RA Schuske K.R., Richmond J.E., Matthies D.S., Davis W.S., Runz S., Rube D.A.,
RA van der Bliek A.M., Jorgensen E.M.;
RT "Endophilin is required for synaptic vesicle endocytosis by localizing
RT synaptojanin.";
RL Neuron 40:749-762(2003).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18094048; DOI=10.1091/mbc.e07-07-0719;
RA Marza E., Long T., Saiardi A., Sumakovic M., Eimer S., Hall D.H.,
RA Lesa G.M.;
RT "Polyunsaturated fatty acids influence synaptojanin localization to
RT regulate synaptic vesicle recycling.";
RL Mol. Biol. Cell 19:833-842(2008).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=21029864; DOI=10.1016/j.cell.2010.09.024;
RA Bai J., Hu Z., Dittman J.S., Pym E.C., Kaplan J.M.;
RT "Endophilin functions as a membrane-bending molecule and is delivered to
RT endocytic zones by exocytosis.";
RL Cell 143:430-441(2010).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-378; ASP-380
RP AND ASP-722.
RX PubMed=25918845; DOI=10.7554/elife.05660;
RA Dong Y., Gou Y., Li Y., Liu Y., Bai J.;
RT "Synaptojanin cooperates in vivo with endophilin through an unexpected
RT mechanism.";
RL Elife 4:E05660-E05660(2015).
CC -!- FUNCTION: Probable inositol 5-phosphatase which regulates synaptic
CC vesicle recycling in neurons by regulating clathrin-mediated
CC endocytosis. {ECO:0000269|PubMed:10931870, ECO:0000269|PubMed:18094048,
CC ECO:0000269|PubMed:25918845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000250|UniProtKB:Q9D2G5};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}.
CC Synapse {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048,
CC ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:25918845}.
CC Note=Localizes to puncta at neuromuscular junctions in the nerve cord.
CC {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:18094048}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:JC8.10b};
CC IsoId=G5ECL2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:JC8.10a};
CC IsoId=G5ECL2-2; Sequence=VSP_058630;
CC Name=c {ECO:0000312|WormBase:JC8.10c};
CC IsoId=G5ECL2-3; Sequence=VSP_058629, VSP_058631;
CC Name=d {ECO:0000312|WormBase:JC8.10d};
CC IsoId=G5ECL2-4; Sequence=VSP_058632, VSP_058633;
CC -!- DOMAIN: The Pro-rich domain is dispensable for endocytosis during the
CC synaptic vesicle recycling, locomotion and for endogenous and evoked
CC excitatory postsynaptic currents (EPSC) at neuromuscular junctions
CC (PubMed:21029864, PubMed:25918845). May play a role together with the
CC SAC domain in targeting unc-26 to synapses (PubMed:25918845).
CC {ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:25918845}.
CC -!- DOMAIN: The SAC domain, but not is catalytic activity, is required for
CC targeting unc-26 to synapses, for locomotion and for normal endogenous
CC and evoked excitatory postsynaptic currents (EPSC) at neuromuscular
CC junctions. {ECO:0000269|PubMed:25918845}.
CC -!- DISRUPTION PHENOTYPE: Viable but small with slow grow and uncoordinated
CC movements (PubMed:10931870, PubMed:21029864). Synaptic vesicles at
CC neuromuscular synapses are reduced, arranged linearly and are
CC dissociated from the synaptic active zone (PubMed:10931870). Several
CC defects in vesicle recycling including accumulation of endocytic pits
CC at the neuromuscular junctions and accumulation of coated vesicles
CC predominantly at synapses of neurons but also near the Golgi in cell
CC bodies of neurons, muscles, hypodermis and gonadal sheath cells
CC (PubMed:10931870). Accumulation of endosome-like compartments in
CC cholinergic and GABA neurons and diffused snb-1/synaptobrevin
CC distribution along the ventral nerve cord (PubMed:10931870).
CC Neurotransmission defects characterized by reduced endogenous frequency
CC of synaptic vesicle fusion, a reduced evoked current amplitude after
CC one stimulation and a faster decline in evoked response caused by
CC multiple responses (PubMed:14622579). Resistant to paralysis induced by
CC Aldicar, an acetylcholinesterase inhibitor which causes acetylcholine
CC accumulation (PubMed:14622579). {ECO:0000269|PubMed:10931870,
CC ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}.
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
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DR EMBL; AF283322; AAG18574.1; -; mRNA.
DR EMBL; AF283323; AAG18575.1; -; mRNA.
DR EMBL; AF283324; AAG18576.1; -; mRNA.
DR EMBL; BX284604; CAB05234.2; -; Genomic_DNA.
DR EMBL; BX284604; CAC70096.1; -; Genomic_DNA.
DR EMBL; BX284604; CAQ58127.1; -; Genomic_DNA.
DR EMBL; BX284604; CAN86614.1; -; Genomic_DNA.
DR PIR; C88883; C88883.
DR RefSeq; NP_001023265.1; NM_001028094.2. [G5ECL2-2]
DR RefSeq; NP_001023266.1; NM_001028095.3. [G5ECL2-1]
DR RefSeq; NP_001122785.1; NM_001129313.2. [G5ECL2-3]
DR RefSeq; NP_001129862.1; NM_001136390.2. [G5ECL2-4]
DR AlphaFoldDB; G5ECL2; -.
DR SMR; G5ECL2; -.
DR IntAct; G5ECL2; 11.
DR STRING; 6239.JC8.10b; -.
DR EPD; G5ECL2; -.
DR PaxDb; G5ECL2; -.
DR PeptideAtlas; G5ECL2; -.
DR EnsemblMetazoa; JC8.10a.1; JC8.10a.1; WBGene00006763. [G5ECL2-2]
DR EnsemblMetazoa; JC8.10b.1; JC8.10b.1; WBGene00006763. [G5ECL2-1]
DR EnsemblMetazoa; JC8.10c.1; JC8.10c.1; WBGene00006763. [G5ECL2-3]
DR EnsemblMetazoa; JC8.10d.1; JC8.10d.1; WBGene00006763. [G5ECL2-4]
DR GeneID; 178284; -.
DR KEGG; cel:CELE_JC8.10; -.
DR CTD; 178284; -.
DR WormBase; JC8.10a; CE28239; WBGene00006763; unc-26. [G5ECL2-2]
DR WormBase; JC8.10b; CE29050; WBGene00006763; unc-26. [G5ECL2-1]
DR WormBase; JC8.10c; CE40972; WBGene00006763; unc-26. [G5ECL2-3]
DR WormBase; JC8.10d; CE42707; WBGene00006763; unc-26. [G5ECL2-4]
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000170400; -.
DR InParanoid; G5ECL2; -.
DR OMA; EYVRPRM; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; G5ECL2; -.
DR Reactome; R-CEL-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-CEL-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR SignaLink; G5ECL2; -.
DR PRO; PR:G5ECL2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006763; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; ISS:WormBase.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; ISS:WormBase.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0015870; P:acetylcholine transport; IMP:WormBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:WormBase.
DR GO; GO:0007032; P:endosome organization; IMP:WormBase.
DR GO; GO:0015812; P:gamma-aminobutyric acid transport; IMP:WormBase.
DR GO; GO:0048212; P:Golgi vesicle uncoating; IMP:WormBase.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0006936; P:muscle contraction; IMP:WormBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0035418; P:protein localization to synapse; IGI:WormBase.
DR GO; GO:0043058; P:regulation of backward locomotion; IMP:WormBase.
DR GO; GO:0043059; P:regulation of forward locomotion; IMP:WormBase.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IMP:WormBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IMP:WormBase.
DR GO; GO:0016050; P:vesicle organization; IMP:WormBase.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endocytosis; Hydrolase;
KW Reference proteome; Synapse.
FT CHAIN 1..1119
FT /note="Synaptojanin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438241"
FT DOMAIN 119..438
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 532..826
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 986..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 500..502
FT /note="ESY -> GLF (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058629"
FT VAR_SEQ 501..506
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058630"
FT VAR_SEQ 503..1119
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058631"
FT VAR_SEQ 506..508
FT /note="EYA -> GKL (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058632"
FT VAR_SEQ 509..1119
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058633"
FT MUTAGEN 378
FT /note="C->S: Normal synapse localization, locomotion and,
FT endogenous and evoked excitatory postsynaptic currents;
FT when associated with N-380."
FT /evidence="ECO:0000269|PubMed:25918845"
FT MUTAGEN 380
FT /note="D->N: Normal synapse localization, locomotion and,
FT endogenous and evoked excitatory postsynaptic currents;
FT when associated with S-378."
FT /evidence="ECO:0000269|PubMed:25918845"
FT MUTAGEN 722
FT /note="D->A: Probable loss of catalytic activity. Reduced
FT locomotion and severe reduction in endogenous and evoked
FT excitatory postsynaptic currents."
FT /evidence="ECO:0000269|PubMed:25918845"
SQ SEQUENCE 1119 AA; 124209 MW; 37004D0B646EF394 CRC64;
MSVRGIRIWR RNDARFQPSI LVEKNGLDGS LLFQGGAIAT LDSDSTDVER RSYQKIVDAY
GILGVLAITK DEAVLVAVTG VLSVGQLYGA DILKITNVEF ISLRTFGSVE NVDSRIIDLQ
RLLSSQMFYF SSLQSYDLTR SAQHRDSHDC SDARFFWNRS LHFSFQRYGI DTDNWLLKCM
AGSVLVRVVY VGANTGRVAL ISRLSCERVG TRFNVRGANY LGNVANFVET EQLLLFDEKE
CSLLQIRGSI PLFWEQPGVN VGSHKVKLRA FETSLPAYHR HLSQLQHRYG EFAIVNLLGR
KEGERVLGDA FKTQHKSSHF APLVDFIDFD YHAQMKISKE AIVQLKKKMS PHMTKHGFFY
SMGKEIVKRQ TGVIRTNCLD CLDRTNAVQT AIGLQMSHDQ VAFLNLNAGK VNVEQRVEEI
LRDLWQKNGD QCSTIYAGTG ALDGKSKLKD ASRSLARTIQ NNLMDGAKQE SFDLFLTGAA
YDPRLFDRAC NILPPSLIQE SYYYHEYADA VSQLVERSPE IAEPQSIKIF VGTWNVNGGK
NIHNVAFRNE SSLSHWIFAN SMTRLVSVED EQLADIVAIG VEELVDLNAS NMVKASTTNQ
RMWCESIRKT LSEKAPFVLI GSEQLVGVCL FLFARPRVSP YLKDFAVASV KTGMGGATGN
KGSVAFRIVV FSTSICFICS HFAAGQNEIR DRNEDFATTL KKIRFPLGRE IDSHDVIFWL
GDFNYRINLS GDEVKNAVRN GDYAKLVEND QLTQQKALGQ TFVGFNEGQL TFAPTYKYDT
FSDDYDTSEK CRAPAWTDRI LWKDQRKKGK TQLLSYDRSE LKTSDHRPVG AVFKVETFKV
GGRKCVELIE DVVESMGPPD GTIIVSIAGK PRFPPQMFPP IHEKLKELGA QVQLSKFDDG
DLWIVLNSGE MALAALSMDG LKIGGTDQIN VKLKSPDWAY ALKPHLSDFD LESFEVTAEE
EALLGGTDGA VFEFADEDED AISVSSLTLT GSAPDRPRPP SARSEAISVA KLEWPTEQPN
VLSTSMPTRA SSASLANSSW YEHVPPLAPP QSNNNKSPPQ ACLFNPFTQS APSPAPPPST
IPLPPTRGAS VGPGPPAVPV RKAPPPPPRP VIPPRPKNM
