SYNJ1_MOUSE
ID SYNJ1_MOUSE Reviewed; 1574 AA.
AC Q8CHC4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Synaptojanin-1;
DE EC=3.1.3.36;
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1;
GN Name=Synj1; Synonyms=Kiaa0910;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3.
RX PubMed=11082044; DOI=10.1242/jcs.113.24.4511;
RA Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT endocytosis.";
RL J. Cell Sci. 113:4511-4521(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-830; SER-1147;
RP SER-1350 AND THR-1354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Phosphatase that acts on various phosphoinositides, including
CC phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-
CC bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By
CC similarity). Has a role in clathrin-mediated endocytosis (By
CC similarity). Hydrolyzes PIP2 bound to actin regulatory proteins
CC resulting in the rearrangement of actin filaments downstream of
CC tyrosine kinase and ASH/GRB2 (By similarity).
CC {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426}.
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 -!- SUBUNIT: Interacts with ASH/GRB2. Interacts with PACSIN1, PACSIN2 and
CC PACSIN3 (PubMed:11082044). Binds AMPH, SH3GL1, SH3GL2 and SH3GL3.
CC Interacts with MYO1E (via SH3 domain). Interacts with BIN1 and DNM1 (By
CC similarity). {ECO:0000250|UniProtKB:Q62910,
CC ECO:0000269|PubMed:11082044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O18964}.
CC -!- DOMAIN: Binds to EPS15 (a clathrin coat-associated protein) via a C-
CC terminal domain containing three Asn-Pro-Phe (NPF) repeats.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal proline-rich region mediates binding to a
CC variety of SH3 domain-containing proteins including AMPH, SH3GL1,
CC SH3GL2, SH3GL3 and GRB2.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41456.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093272; BAC41456.2; ALT_INIT; Transcribed_RNA.
DR AlphaFoldDB; Q8CHC4; -.
DR SMR; Q8CHC4; -.
DR IntAct; Q8CHC4; 7.
DR MINT; Q8CHC4; -.
DR STRING; 10090.ENSMUSP00000113308; -.
DR iPTMnet; Q8CHC4; -.
DR PhosphoSitePlus; Q8CHC4; -.
DR SwissPalm; Q8CHC4; -.
DR EPD; Q8CHC4; -.
DR jPOST; Q8CHC4; -.
DR MaxQB; Q8CHC4; -.
DR PaxDb; Q8CHC4; -.
DR PeptideAtlas; Q8CHC4; -.
DR PRIDE; Q8CHC4; -.
DR ProteomicsDB; 263188; -.
DR UCSC; uc007zww.2; mouse.
DR MGI; MGI:1354961; Synj1.
DR eggNOG; KOG0566; Eukaryota.
DR InParanoid; Q8CHC4; -.
DR PhylomeDB; Q8CHC4; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR ChiTaRS; Synj1; mouse.
DR PRO; PR:Q8CHC4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CHC4; protein.
DR GO; GO:0030118; C:clathrin coat; TAS:MGI.
DR GO; GO:0030132; C:clathrin coat of coated pit; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030117; C:membrane coat; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0097060; C:synaptic membrane; ISS:BHF-UCL.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0012506; C:vesicle membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:1990175; F:EH domain binding; ISO:MGI.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; ISO:MGI.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; IMP:MGI.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:MGI.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IMP:MGI.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0006836; P:neurotransmitter transport; IMP:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IMP:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:MGI.
DR GO; GO:1904980; P:positive regulation of endosome organization; ISO:MGI.
DR GO; GO:0014015; P:positive regulation of gliogenesis; ISO:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; TAS:BHF-UCL.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IMP:SynGO.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; IMP:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IDA:SynGO.
DR CDD; cd12719; RRM_SYNJ1; 1.
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; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR034972; SYNJ1.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034971; SYNJ1_RRM.
DR PANTHER; PTHR11200:SF158; PTHR11200:SF158; 1.
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; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endocytosis; Hydrolase; Lipid metabolism; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1574
FT /note="Synaptojanin-1"
FT /id="PRO_0000209731"
FT DOMAIN 119..442
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 894..971
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1029..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62910"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62910"
FT MOD_RES 1198
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1354
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1574 AA; 172617 MW; F791EE3AD6A37B82 CRC64;
MAFSKGFRIY HKLDPPPFSL IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYAKVLDAY
GLLGVLRLNL GDTMLHYLVL VTGCMSVGKI QESEVFRVTS TEFISLRVDA SDEDRISEVR
KVLNSGNFYF AWSASGVSLD LSLNAHRSMQ EHTTDNRFFW NQSLHLHLKH YGVNCDDWLL
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVIYLD
DCVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFRTLK DLYGKQIVVN
LLGSKEGEHM LSKAFQSHLK ASEHASDIHM VSFDYHQMVK GGKAEKLHSI LKPQVQKFLD
YGFFYFDGSE VQRCQSGTVR TNCLDCLDRT NSVQAFLGLE MLAKQLEALG LAEKPQLVTR
FQEVFRSMWS VNGDSISKIY AGTGALEGKA KLKDGARSVT RTIQNNFFDS SKQEAIDVLL
LGNTLNSDLA DKARALLTTG SLRVSEQTLQ SASSKVLKNM CENFYKYSKP KKIRVCVGTW
NVNGGKQFRS IAFKNQTLTD WLLDAPKLAG IQEFQDKRSK PTDIFAIGFE EMVELNAGNI
VNASTTNQKL WAVELQKTIS RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT
GMGGATGNKG AVAIRMLFHT TSLCFVCSHF AAGQSQVKER NEDFVEIARK LSFPMGRMLF
SHDYVFWCGD FNYRIDLPNE EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF
APTYKYDLFS EDYDTSEKCR TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT
WTPGTLLHYG RAELKTSDHR PVVALIDIDI FEVEAEERQK IYKEVIAVQG PPDGTVLVSI
KSSAQESTFF DDALIDELLR QFAHFGEVIL IRFVEDKMWV TFLEGSSALN ALSLNGKELL
NRTITITLKS PDWIKHLEEE MSLEKISVTL PSSASSTLLG EDAEVAADFD MEGDVDDYSA
EVEELLPQHL QPSSSSGLGT SPSSSPRTSP CQSPTVPEYS APSLPIRPSR APSRTPGPPS
SQGSPVDTQP AAQKDSSQTL EPKRPPPPRP VAPPARPAPP QRPPPPSGAR SPAPARKEFG
GVGAPPSPGV ARREIEAPKS PGTARKDNIG RNQPSPQAGL AGPGPAGYGA ARPTIPARAG
VISAPQSQAR VCAGRPTPDS QSKPSETLKG PAVLPEPLKP QAAFPQQPSL PTPAQKLQDP
LVPIAAPTMP PSGPQPNLET PPQPPPRSRS SQSLPSDSSP QLQQEQPTGQ VKINGISGVK
QEPTLKSDPF EDLSLSVLAV SKAQPSVQIS PVLTPDPKML IQLPSASQSQ VNPLSSVSCM
PTRPPGPEES KSQESMGSSA NPFPSLPCRN PFTDRTAAPG NPFRVQSQES EATSWLSKEE
PVPNSPFPPL MPLSHDTSKA SSSLGGFEDN FDLQSQSTVK TSNPKGWVTF DEDDNFPTTG
KSKSVCPDLV GNAPASFDDD WSKGASVSFC VLPARRPPPP PPPVPLLPPG TTSSAGPSTT
LPSKAPSTLD FTER
