SYNJ1_BOVIN
ID SYNJ1_BOVIN Reviewed; 1324 AA.
AC O18964;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 23-FEB-2022, entry version 142.
DE RecName: Full=Synaptojanin-1;
DE EC=3.1.3.36;
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1;
DE AltName: Full=p150;
DE Flags: Fragment;
GN Name=SYNJ1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 321-339 AND 454-469,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9199318; DOI=10.1128/mcb.17.7.3841;
RA Sakisaka T., Itoh T., Miura K., Takenawa T.;
RT "Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the
RT rearrangement of actin filaments.";
RL Mol. Cell. Biol. 17:3841-3849(1997).
CC -!- FUNCTION: Phosphatase that acts on various phosphoinositides, including
CC phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-
CC bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate. Has a role
CC in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound
CC to actin regulatory proteins resulting in the rearrangement of actin
CC filaments downstream of tyrosine kinase and ASH/GRB2 (PubMed:9199318).
CC {ECO:0000250|UniProtKB:O43426, ECO:0000269|PubMed:9199318}.
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. Binds AMPH, SH3GL1, SH3GL2 and SH3GL3. Interacts with MYO1E
CC (via SH3 domain). Interacts with BIN1 and DNM1.
CC {ECO:0000250|UniProtKB:Q62910}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:9199318}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC brain.
CC -!- DOMAIN: The C-terminal proline-rich region mediates binding to a
CC variety of SH3 domain-containing proteins including AMPH and ASH/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=BAA21652.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D85682; BAA21652.1; ALT_FRAME; mRNA.
DR STRING; 9913.ENSBTAP00000003985; -.
DR PaxDb; O18964; -.
DR PRIDE; O18964; -.
DR eggNOG; KOG0566; Eukaryota.
DR InParanoid; O18964; -.
DR OrthoDB; 359616at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
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; Direct protein sequencing; Endocytosis; Hydrolase;
KW Lipid metabolism; Methylation; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..>1324
FT /note="Synaptojanin-1"
FT /id="PRO_0000209729"
FT DOMAIN 119..442
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 902..971
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 475..859
FT /note="Catalytic"
FT REGION 1006..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1021
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1079
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHC4"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1186
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHC4"
FT MOD_RES 1205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT CONFLICT 335
FT /note="Y -> YY (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1324
SQ SEQUENCE 1324 AA; 146584 MW; EDDC2DD9D6E3191C CRC64;
MAFSKGFRIY HKLDPPPFSL IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYSKVLDAY
GLLGVLRLNL GDIMLHYLVL VTGCMSVGKI QESEVFRVTS TEFISLRVDS SDEDRISEVR
KVLNSGNFYF AWSASGVSLD LSLNAHRSLQ EHTTDNRFSW NQSLHLHLKH YGVNCADWLL
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVVYLD
DSVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFRTLK NLYGKQIIVN
LLGSKEGEHM LSKAFQSHLK ASEHAADIQM VNFDYHQMVK GGKAEKLHSV LKPQVQKFLD
YGIFHFDGSE VQRCQSGTVR TNCLDCLDRT NSVQAFLGLE MLTKQLEALG LAEKPQLVTR
FQEVFRSMWS VNGDSISKIY AGTGALEGKA KLKDGARSVS RTIQNNFFDS SKQEAIDVLL
LGNTLNSDLA DKARALLTTG SLRVSEQTLQ SASSKVLKSM CENFYKYSKP KKIRVCVGTW
NVNGGKQFRS IAFKNQTLTD WLLDAPKLAG IQEFQDKRSK PMDIFPIGFE EMVELNAGNI
VNASTTNQKL WAAELQKTIS RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT
GMGGATGNKG AVAIRMLFHT TSLCFVCSHF AAGQSQVKER NDDFLEIARK LSFPMGRLLF
SHDYVFWCGD FNYRIDLPNE EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF
APTYKYDLFS DDYDTSEKCR TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT
WTPGTLLHYG RAELKTSDHR PVVALIDIDI FEVEAEERQN IYKEVIAVQG PPDGTVLVSI
KSSLPENNFF NDALIDELLQ QFTNFGEVIL IRFVEDKMWV TFLEGSSALN VLNLNGKELL
GRTITITLKS PDWIKTLEEE MSLEKINVPL PSSTSSTLLG EDAEVTADFD MEGDVDDYSA
EVEEILPQHL QPSSSSALAR PPVLHPGPVP ASHLPYRRGP VPSLPVRPSR APSRTPGPPA
SQSSPVDTLP ATQLQQKDSS QTLEPKRPPP PRPVAPPARP APPQRPPPPS GARSPAPARE
RVWSTRKAQE RPRRDNLGGS QLPPQGGLPG PGLAGHSAAR PIIPPRAGVI SAPESHGRVS
AGRLTPESQR KTXEVLKGPA LLPEPLKPQA ALPVPPSLAP PSQEMQEPLI AVAAPLAQSA
LQPSLETPPQ PPPRSRSSHS LPSDAPAAAA GATIRVTGEK QTGVSAVRLD CPLKSDPFED
LSLN
