SYNJ2_RAT
ID SYNJ2_RAT Reviewed; 1496 AA.
AC O55207; Q91ZD8; Q91ZD9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Synaptojanin-2;
DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q9D2G5};
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2;
GN Name=Synj2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2A), AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=9388224; DOI=10.1074/jbc.272.49.30817;
RA Nemoto Y., Arribas M., Haffner C., de Camilli P.;
RT "Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting
RT domain and expression pattern.";
RL J. Biol. Chem. 272:30817-30821(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2B1 AND 2B2), SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ASP-388; GLY-435 AND ARG-466.
RC STRAIN=Sprague-Dawley;
RX PubMed=11498538; DOI=10.1074/jbc.m106404200;
RA Nemoto Y., Wenk M.R., Watanabe M., Daniell L., Murakami T., Ringstad N.,
RA Yamada H., Takei K., De Camilli P.;
RT "Identification and characterization of a synaptojanin 2 splice isoform
RT predominantly expressed in nerve terminals.";
RL J. Biol. Chem. 276:41133-41142(2001).
RN [3]
RP INTERACTION WITH SYNJ2BP, SUBCELLULAR LOCATION (ISOFORM 2A), AND
RP MUTAGENESIS.
RX PubMed=10357812; DOI=10.1093/emboj/18.11.2991;
RA Nemoto Y., De Camilli P.;
RT "Recruitment of an alternatively spliced form of synaptojanin 2 to
RT mitochondria by the interaction with the PDZ domain of a mitochondrial
RT outer membrane protein.";
RL EMBO J. 18:2991-3006(1999).
CC -!- FUNCTION: Inositol 5-phosphatase which may be involved in distinct
CC membrane trafficking and signal transduction pathways. May mediate the
CC inhibitory effect of Rac1 on endocytosis (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Binds to GRB2 (By similarity). Isoform 2A binds to
CC SYNJ2BP/OMP25. {ECO:0000250, ECO:0000269|PubMed:10357812}.
CC -!- INTERACTION:
CC O55207-3; Q9WVJ4: Synj2bp; NbExp=9; IntAct=EBI-7007476, EBI-7007454;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11498538}. Cell
CC membrane {ECO:0000269|PubMed:11498538}. Presynapse
CC {ECO:0000269|PubMed:11498538}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11498538}. Membrane raft. Note=Localizes at
CC presynapse terminals in brain and at bundles of microtubules
CC surrounding the nucleus in the elongating spermatids corresponding to
CC the manchette (PubMed:11498538). Translocates from the cytoplasm to
CC membrane ruffles in a RAC1-dependent manner (PubMed:11498538).
CC {ECO:0000269|PubMed:11498538}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2A]: Mitochondrion
CC {ECO:0000269|PubMed:10357812}. Note=Interaction of isoform 2A with
CC SYNJ2BP/OMP25 results in localization to the mitochondrion
CC (PubMed:10357812). {ECO:0000269|PubMed:10357812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist. Experimental confirmation
CC may be lacking for some isoforms.;
CC Name=2B2;
CC IsoId=O55207-1; Sequence=Displayed;
CC Name=2B1;
CC IsoId=O55207-2; Sequence=VSP_012914;
CC Name=2A; Synonyms=7.5kb;
CC IsoId=O55207-3; Sequence=VSP_012915, VSP_012916;
CC Name=7.2kb;
CC IsoId=O55207-4; Sequence=Not described;
CC Name=6.0kb;
CC IsoId=O55207-5; Sequence=Not described;
CC Name=5.2kb;
CC IsoId=O55207-6; Sequence=Not described;
CC Name=3.5kb;
CC IsoId=O55207-7; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoforms 2B1 and 2B2 are
CC concentrated at nerve terminals in brain and at spermatid manchette in
CC testis.
CC -!- MISCELLANEOUS: [Isoform 2A]: The PDZ domain of isoform 2A binds
CC SYNJ2BP/OMP25. Mutagenesis of Ser-1246 or Val-1248 to Ala abolishes
CC SYNJ2BP/OMP25 binding. {ECO:0000305}.
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; U90312; AAB92481.1; -; mRNA.
DR EMBL; AY034050; AAK61722.1; -; mRNA.
DR EMBL; AY034051; AAK61723.1; -; mRNA.
DR RefSeq; NP_001106842.1; NM_001113371.1.
DR RefSeq; NP_001106843.1; NM_001113372.1.
DR RefSeq; NP_114460.1; NM_032071.2.
DR AlphaFoldDB; O55207; -.
DR SMR; O55207; -.
DR ELM; O55207; -.
DR IntAct; O55207; 1.
DR MINT; O55207; -.
DR STRING; 10116.ENSRNOP00000062564; -.
DR iPTMnet; O55207; -.
DR PhosphoSitePlus; O55207; -.
DR PaxDb; O55207; -.
DR PRIDE; O55207; -.
DR GeneID; 84018; -.
DR KEGG; rno:84018; -.
DR CTD; 8871; -.
DR RGD; 69436; Synj2.
DR eggNOG; KOG0566; Eukaryota.
DR InParanoid; O55207; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; O55207; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O55207; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:RGD.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0052744; F:phosphatidylinositol monophosphate phosphatase activity; IDA:RGD.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:RGD.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IDA:RGD.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd12720; RRM_SYNJ2; 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; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034974; SYNJ2.
DR InterPro; IPR034973; SYNJ2_RRM.
DR PANTHER; PTHR11200:SF148; PTHR11200:SF148; 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 Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Hydrolase; Lipid metabolism; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; RNA-binding; Synapse.
FT CHAIN 1..1496
FT /note="Synaptojanin-2"
FT /id="PRO_0000209735"
FT DOMAIN 120..444
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 906..985
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 450..?
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 1047..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15056"
FT VAR_SEQ 1085..1129
FT /note="Missing (in isoform 2B1)"
FT /evidence="ECO:0000303|PubMed:11498538"
FT /id="VSP_012914"
FT VAR_SEQ 1254..1293
FT /note="PMLPEEQCEQQPVHFTMASQEMNLETPPPITAPIPPVPKP -> IVFCSSSQ
FT ASQPCSLLQRHEFVRTVAAQRLTPVDASGSSV (in isoform 2A)"
FT /evidence="ECO:0000303|PubMed:9388224"
FT /id="VSP_012915"
FT VAR_SEQ 1294..1496
FT /note="Missing (in isoform 2A)"
FT /evidence="ECO:0000303|PubMed:9388224"
FT /id="VSP_012916"
FT MUTAGEN 388
FT /note="D->N: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11498538"
FT MUTAGEN 435
FT /note="G->V: Reduced phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11498538"
FT MUTAGEN 466
FT /note="R->H: No effect."
FT /evidence="ECO:0000269|PubMed:11498538"
FT CONFLICT 1130
FT /note="T -> A (in Ref. 2; AAK61722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1496 AA; 165264 MW; CB15017BF7821648 CRC64;
MALSKGLRLL ARLDPTGPSS VLLEARGRGD CLLFEAGAVA TLAPEEKEVI KGLYGKPTDA
YGCLGELSLK SGGVPLSFLV LVTGCTSVGR IPDAEIYKIT GTEFYPLQEE AKEEDRLPAL
KKILSSGVFY FAWPNDGACF DLTIRAQKQG DDCSEWGTSF FWNQLLHVPL RQHQVNCHDW
LLKVICGVVT IRTVYASHKQ AKACLISRIS CERAGARFLT RGVNDDGHVS NFVETEQAIY
MDDGVSSFVQ IRGSVPLFWE QPGLQVGSHH LRLHRGLEAN APAFERHMVL LKEQYGQQVV
VNLLGSRGGE EVLNRAFKKL LWASCHAGDT PMINFDFHQF AKGRKLEKLE NLLRPQLKLH
WDDFGVFAKG ENVSPRFQKG TLRMNCLDCL DRTNTVQCFI ALEVLHLQLE SLGLNSKPIT
DRFVESFKAM WSLNGHGLSK VFTGSRALEG KAKVGKLKDG ARSMSRTIQS NFFDGVKQEA
IKLLLVGDVY NEESTDKGRM LLDNTALLGL GSNKQNSLSG MLDGKATPRI LKAMTERQSE
FTNFKRIQIA MGTWNVNGGK QFRSNLLGTT ELTDWLLDAP QLSGAVDSQD DGGPADIFAV
GFEEMVELSA GNIVNASTTN RKMWGEQLQK AISRSHRYIL LTSAQLVGVC LYIFVRPYHV
PFIRDVAIDT VKTGMGGKAG NKGAVGIRFQ FHSTSFCFIC SHLTAGQSQV KERNEDYREI
THKLSFPSGR NIFSHDYVFW CGDFNYRIDL TYEEVFYFVK RQDWKKLMEF DQLQLQKSSG
KIFKDFHEGT INFGPTYKYD VGSAAYDTSD KCRTPAWTDR VLWWRKKHPY DKTAGELNLL
DSDLDGDANI RHTWSPGTLK YYGRAELQAS DHRPVLAIVE VEVQEVDVGA RERVFQEVSS
VQGPLDATVI VNLQSPTLEE RNEFPEDLRT ELMQTLGNYG TIILVRINQG QMLVTFADSH
SALSVLDVDG MKVKGRAVKI RPKTKDWLEG LREELIRKRD SMAPVSPTAN SCLLEENFDF
TSLDYESEGD VLEDDEDYLA DEFGQPVVSD SELGGDDSSD TMSASTPASK SPALAKKKQH
PTYKDDADLM TLKLELEVAG NFRHRSPSRS LSVPNRPRPP HPPQRPPPPT GLMVKKSASD
ASISSGTHGQ YSILQTAKLL PGAPQQPPKA RTGISKPYNV KQIKTTNAQE AEAAIRCLLE
AGGGVPESAP GATPLRNQGS SKPEASLGPP VLPRRPVPRV PTMKKPTLRR TGKPMLPEEQ
CEQQPVHFTM ASQEMNLETP PPITAPIPPV PKPRTFQPGR GVERRPSGGK PEPDDAPPVT
GAVELSSPEA PEAPSLAPKV PPRRKKSAPA AFHLQVLQSN SQLLQGLTCS SSSPSPPKPD
TPLLYPQMAL GTSSAISPET DGPRVTEPEA ASFHGDYPDP FWSLLHHPKL LNNNTWLSKS
SEPLDLGSRT PERTHTDSAQ VNASVVERGL PPDHGGKDFS HWMAASNKDK RTTLGV
