Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10040107 |
Family | AA2 |
Protein Properties | Length: 894 Molecular Weight: 100818 Isoelectric Point: 7.4676 |
Chromosome | Chromosome/Scaffold: 86 Start: 177960 End: 184041 |
Description | myo-inositol polyphosphate 5-phosphatase 2 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA2 | 617 | 873 | 0 |
KHPRIAASLIRLHFHDCFVMGCDGSLLLDRKGGMQSEKDAKPNANSVHGFELVDKIKSEVEQACPSTVSCADILAIAARDAVALRGGKGWEVMLGRKDSL NASIDAANDLLPSPNSTVKELVDNFKQQGLDIKDLVALSGAHTLGKARCSSINGRIHDLFESRKNDEYERHTTFLKILRSTCLGNQRQLAPLDLQTPFRF DNKYYLNILQGRGLLGSDDVLVSERNTTVMSLVWAYASNEELFFRDFAKSMIEMGNI |
Full Sequence |
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Protein Sequence Length: 894 Download |
MRARRAKRSE AFWPSLVMKK WLNIKPQVHD FSEDELTENE SEDDACSVRD ERVNVREDHG 60 QMKHYQSHQS PPSKGYSLKH RRGKSETLRI QYINTKDVRV TIGTWNVAGK TPDDDLEIES 120 WLCTEEPADV YIIGFQEVVP LSAGNVLGAE SNRPISKWEG IIRKTLNKSS QPAKKHKCFS 180 APPSPVLRTS SVADDLADEV HDALPLDLTN EEYLEPMDNN REPEGNEPRR EVGIGKDLHL 240 KTIFGMDCEN KLDWPEHSLD AAPQVISSGS KLRRVFSARM SSSWENSLGS TPSFAANPCG 300 LRRTHHSSGD LGSLLVDQPK EIVSVWVRKG VRRHVNNLKV SPVGVGLMGY MGNKGSVSVS 360 MSIFQSRMCF VCSHLTSGQK EGQEQRRNAD VYEILKRTRF SSILDTDQPQ TIPSHDQIFW 420 FGDLNYRLNK SDSEVRKLVS LKQWNELTNS DQLIRELRSG HVFDGWREGA IHFPPTYKYE 480 INSDRYVGEF PREGEKKRSP AWCDRILWLG KGIKQLFYKR ADIRISDHRP VSSMFVVEVE 540 VFDHRKLKKA LNVNSAAVHP DIFLFDDEEP ETSQITQRII MACSICQGQN LVQHYYKGTC 600 PSAEAIVRYN VEDAVIKHPR IAASLIRLHF HDCFVMGCDG SLLLDRKGGM QSEKDAKPNA 660 NSVHGFELVD KIKSEVEQAC PSTVSCADIL AIAARDAVAL RGGKGWEVML GRKDSLNASI 720 DAANDLLPSP NSTVKELVDN FKQQGLDIKD LVALSGAHTL GKARCSSING RIHDLFESRK 780 NDEYERHTTF LKILRSTCLG NQRQLAPLDL QTPFRFDNKY YLNILQGRGL LGSDDVLVSE 840 RNTTVMSLVW AYASNEELFF RDFAKSMIEM GNINVLTGNQ GEIRKNCRVV NSS* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd09093 | INPP5c_INPP5B | 5.0e-12 | 99 | 168 | 71 | + Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins. This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain. | ||
cd09093 | INPP5c_INPP5B | 4.0e-64 | 325 | 530 | 208 | + Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins. This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain. | ||
PLN03030 | PLN03030 | 6.0e-68 | 579 | 891 | 320 | + cationic peroxidase; Provisional | ||
cd00693 | secretory_peroxidase | 4.0e-151 | 590 | 890 | 303 | + Horseradish peroxidase and related secretory plant peroxidases. Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites. | ||
PLN03191 | PLN03191 | 0 | 1 | 564 | 622 | + Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0004601 | peroxidase activity |
GO:0006979 | response to oxidative stress |
GO:0020037 | heme binding |
GO:0055114 | oxidation-reduction process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABV90875.1 | 0 | 1 | 564 | 3 | 625 | inositol-1,4,5-triphosphate-5-phosphatase [Solanum lycopersicum] |
EMBL | CAB59428.1 | 0 | 1 | 561 | 1 | 610 | inositol-1,4,5-trisphosphate 5-Phosphatase [Arabidopsis thaliana] |
EMBL | CBI33949.1 | 0 | 1 | 564 | 1 | 626 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002279188.1 | 0 | 1 | 564 | 1 | 628 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002326505.1 | 0 | 1 | 561 | 1 | 618 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1qo4_A | 0 | 595 | 893 | 7 | 306 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1pa2_A | 0 | 595 | 893 | 7 | 306 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 1gx2_B | 0 | 591 | 893 | 3 | 308 | A Chain A, Recombinant Horseradish Peroxidase Phe209ser Complex With Benzhydroxamic Acid |
PDB | 1gx2_A | 0 | 591 | 893 | 3 | 308 | A Chain A, Recombinant Horseradish Peroxidase Phe209ser Complex With Benzhydroxamic Acid |
PDB | 3atj_B | 0 | 591 | 893 | 3 | 308 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795711 | 530 | 40 | 499 | 0 |
HO795711 | 76 | 496 | 571 | 0 |
CV478229 | 243 | 45 | 287 | 0 |
ES829939 | 249 | 323 | 571 | 0 |
DV135454 | 234 | 327 | 560 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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