UniProt: G4VEX3

Database: UniProt
Entry: G4VEX3_SCHMA

LinkDB:  G4VEX3_SCHMA 
Original site:  G4VEX3_SCHMA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   G4VEX3_SCHMA            Unreviewed;      1562 AA.
AC   G4VEX3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE   AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_308600.1};
RN   [1] {ECO:0000313|Proteomes:UP000008854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN   [2] {ECO:0000313|WBParaSite:Smp_308600.1}
RP   IDENTIFICATION.
RC   STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_308600.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2019) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   RefSeq; XP_018651092.1; XM_018799289.1.
DR   AlphaFoldDB; G4VEX3; -.
DR   STRING; 6183.G4VEX3; -.
DR   EnsemblMetazoa; Smp_308600.1; Smp_308600.1; Smp_308600.
DR   GeneID; 8342922; -.
DR   KEGG; smm:Smp_012970; -.
DR   WBParaSite; Smp_308600.1; Smp_308600.1; Smp_308600.
DR   CTD; 8342922; -.
DR   eggNOG; KOG1729; Eukaryota.
DR   eggNOG; KOG4471; Eukaryota.
DR   HOGENOM; CLU_245887_0_0_1; -.
DR   InParanoid; G4VEX3; -.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd14533; PTP-MTMR3-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF75; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          135..517
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          1363..1422
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          541..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1532..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1219..1253
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        541..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        353
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         353..359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   1562 AA;  174569 MW;  D7486B932829DE47 CRC64;
     MNVISMHFLP GEEPINTKSI ADGIFTLTNY RLIFSTKRPQ SSWSIPTTLV WKAEAFEMIH
     IKIITKIGIS VTWSFVDEIA CDAGYAHITS LIDTPRDIDS LFACKFRSSL EANIPNHPFL
     LSACELLQIN DVDRTLDTAL VCFEFRRMNF DKTWKITDIN NEFKICSTYP RHHIVPRSIS
     DNDIINMASF RSHNRFLTVV WRSQVTGAVL LRCAQPCVGL MCSRNEYDEK FLRTVLACCP
     KKPFSDPNKD THRLMIVDAR SRSSAQFNRI RGGGFEYPEY YDQAEVVFMD LPNLHTVRSN
     FEALTNLFAG KCPNWFSSLE KSSWLNNIGQ LLKTASEIAI ALEENARPVM VHCTDGWDRT
     PQISSLAQLL ADPFYRTIQG FNILVEREWL QFGHKFSDRS GHVSPSLNIN EQSPIFLQWL
     DCVHQIRNQF PHCFEFNESF LLKLGLHICS NLFGTFLCNS EKERQKASVA SRTCSLWGLL
     SSKYNWTIVN YFYEPEAEHL LQPDCQVRSL SLWSAFYGIA LSTSKVNPTL DIPQDVIEAT
     PNNAHSVTNS TISSPTKHKS LSSIDPAPHK TDSTSNINYE ESSQPTTNLL GDDHPSDSIK
     IMVPNLKIGT SEELNSDGDL FIKGYASSRN SHRRSLDDIN NYMDSRFTKQ QSREFSLSNR
     VSPTIMKSSS QCFFENNICN EKNSPGPAIL RLSSLSDDTG ICSGLSKSYI RSLSSVNNGS
     YPFPKHSDKC ISPESDPAQL TASTCTYVNR FQQQECVLSP DENIDVFASD EQLEQNDFSF
     TNHNNNIDTM NSCSNNLMSS GRLYYSQFNQ PIQNCQFYGK CSPLSISPRQ FEFNDCDDSN
     HNDSVNVESH SKLPSNFNLD GVQCDNFTYN SPRWSVTTRG SNTSLYVLSD VKQSSIELLK
     PVSINSSQPV DIKISRRLDN PNSLIPIGSG SVYPNEFTVH SLPENDEVLV NGAVSLTSDS
     DDSPNECNDL NFSTPLGESV SGQVLSTNKT EISIFGHNGS EKSQDITSTI SRVNEESLDE
     AFVTKLSELL IPEDLLAWRN KYFRSEYFSN ILSQSSPSVS CGSRNPSSSQ MFDCSSNNNS
     KALKPGGSFD SKSYSVTVNP KISLPEFTRI TTNDDVYNRP TSAPISPTSA VSYFPSTLHK
     NSTLLHRAVH NPSIDQNISN DTNALEKIKK KPLSSTLMNT LSCFPDWDGL PMLVDRLTIH
     AHSQLCQERY NRKTQKQSML ALEAKLKYTQ LEVERLNSEA RRLKQLLELT KTQTCKQDKN
     TLASSDDHLS SLSSSLSSYE RKLTQNSHIN GQCKSKESSL LSSELFVSIS KDKNISEEAH
     NPSNIKSELN DPIESTFLNA SCKTTSFELI DTEDGQSVLL QPDCIAHQCT LCRIEFSALR
     PKHHCRNCGY IFCANCSDRR IVTTSQPSGP VRVCRHCFFQ LSRPSVKSSK QQSIEEYTPC
     VARHTMVKED NNGGGLVKNF TNPDFLNYMN NSIMLSTGSD SGCMPVSSFP DGAILRMSSS
     GVSHHFNGSF NSETTTNNAT TTATVNHRLD SIITNNPPLS RCHSAGGARP TSSAASDGIA
     QA
//

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