O18964 (SYNJ1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synaptojanin-1
EC=3.1.3.36

Alternative name(s):
Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1
p150

Gene names

Name:

SYNJ1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1324 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
Subunit structure	Binds to AMPH and ASH/GRB2.
Subcellular location	Cytoplasm › perinuclear region. Note: Predominantly found in the perinuclear region.
Tissue specificity	Ubiquitously expressed with highest levels in brain.
Domain	The C-terminal proline-rich region mediates binding to a variety of SH3 domain-containing proteins including AMPH and ASH/GRB2.
Sequence similarities	Belongs to the synaptojanin family. In the central section; belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family. Contains 1 RRM (RNA recognition motif) domain. Contains 1 SAC domain.
Sequence caution	The sequence BAA21652.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›1324	›1324	Synaptojanin-1		PRO_0000209729
Regions
	Domain	119 – 442	324	SAC
	Domain	902 – 971	70	RRM
	Region	475 – 859	385	Catalytic
	Compositional bias	860 – 1212	353	Pro-rich
	Compositional bias	1033 – 1036	4	Poly-Ser
	Compositional bias	1108 – 1113	6	Poly-Pro
	Compositional bias	1126 – 1129	4	Poly-Pro
Amino acid modifications
	Modified residue	784	1	Phosphotyrosine By similarity
	Modified residue	786	1	Phosphotyrosine By similarity
	Modified residue	830	1	Phosphoserine By similarity
	Modified residue	1084	1	Phosphoserine By similarity
	Modified residue	1205	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	335	1	Y → YY AA sequence Ref.1
	Non-terminal residue	1324	1

Sequences

	Sequence		Length	Mass (Da)
	O18964 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: EDDC2DD9D6E3191C	FASTA	1,324	146,584
	10 20 30 40 50 60 MAFSKGFRIY HKLDPPPFSL IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYSKVLDAY 70 80 90 100 110 120 GLLGVLRLNL GDIMLHYLVL VTGCMSVGKI QESEVFRVTS TEFISLRVDS SDEDRISEVR 130 140 150 160 170 180 KVLNSGNFYF AWSASGVSLD LSLNAHRSLQ EHTTDNRFSW NQSLHLHLKH YGVNCADWLL 190 200 210 220 230 240 RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVVYLD 250 260 270 280 290 300 DSVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFRTLK NLYGKQIIVN 310 320 330 340 350 360 LLGSKEGEHM LSKAFQSHLK ASEHAADIQM VNFDYHQMVK GGKAEKLHSV LKPQVQKFLD 370 380 390 400 410 420 YGIFHFDGSE VQRCQSGTVR TNCLDCLDRT NSVQAFLGLE MLTKQLEALG LAEKPQLVTR 430 440 450 460 470 480 FQEVFRSMWS VNGDSISKIY AGTGALEGKA KLKDGARSVS RTIQNNFFDS SKQEAIDVLL 490 500 510 520 530 540 LGNTLNSDLA DKARALLTTG SLRVSEQTLQ SASSKVLKSM CENFYKYSKP KKIRVCVGTW 550 560 570 580 590 600 NVNGGKQFRS IAFKNQTLTD WLLDAPKLAG IQEFQDKRSK PMDIFPIGFE EMVELNAGNI 610 620 630 640 650 660 VNASTTNQKL WAAELQKTIS RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT 670 680 690 700 710 720 GMGGATGNKG AVAIRMLFHT TSLCFVCSHF AAGQSQVKER NDDFLEIARK LSFPMGRLLF 730 740 750 760 770 780 SHDYVFWCGD FNYRIDLPNE EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF 790 800 810 820 830 840 APTYKYDLFS DDYDTSEKCR TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT 850 860 870 880 890 900 WTPGTLLHYG RAELKTSDHR PVVALIDIDI FEVEAEERQN IYKEVIAVQG PPDGTVLVSI 910 920 930 940 950 960 KSSLPENNFF NDALIDELLQ QFTNFGEVIL IRFVEDKMWV TFLEGSSALN VLNLNGKELL 970 980 990 1000 1010 1020 GRTITITLKS PDWIKTLEEE MSLEKINVPL PSSTSSTLLG EDAEVTADFD MEGDVDDYSA 1030 1040 1050 1060 1070 1080 EVEEILPQHL QPSSSSALAR PPVLHPGPVP ASHLPYRRGP VPSLPVRPSR APSRTPGPPA 1090 1100 1110 1120 1130 1140 SQSSPVDTLP ATQLQQKDSS QTLEPKRPPP PRPVAPPARP APPQRPPPPS GARSPAPARE 1150 1160 1170 1180 1190 1200 RVWSTRKAQE RPRRDNLGGS QLPPQGGLPG PGLAGHSAAR PIIPPRAGVI SAPESHGRVS 1210 1220 1230 1240 1250 1260 AGRLTPESQR KTXEVLKGPA LLPEPLKPQA ALPVPPSLAP PSQEMQEPLI AVAAPLAQSA 1270 1280 1290 1300 1310 1320 LQPSLETPPQ PPPRSRSSHS LPSDAPAAAA GATIRVTGEK QTGVSAVRLD CPLKSDPFED LSLN

References

[1]	"Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments." Sakisaka T., Itoh T., Miura K., Takenawa T. Mol. Cell. Biol. 17:3841-3849(1997) [PubMed: 9199318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 321-339 AND 454-469. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85682 mRNA. Translation: BAA21652.1. Frameshift.
IPI	IPI00689523.
UniGene	Bt.103203.
3D structure databases
ProteinModelPortal	O18964.
SMR	O18964. Positions 895-971.
ModBase	Search...
Protein-protein interaction databases
STRING	O18964.
Proteomic databases
PRIDE	O18964.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG07677.
GeneTree	ENSGT00600000084387.
HOVERGEN	HBG079225.
InParanoid	O18964.
PhylomeDB	O18964.
Family and domain databases
InterPro	IPR015047. DUF1866. IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR002013. Syja_N. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
Pfam	PF08952. DUF1866. 1 hit. PF03372. Exo_endo_phos. 1 hit. PF02383. Syja_N. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
PROSITE	PS50102. RRM. 1 hit. PS50275. SAC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYNJ1_BOVIN

Accession

Primary (citable) accession number: O18964

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	November 16, 2011
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program