ID M4AJL9_XIPMA Unreviewed; 901 AA.
AC M4AJL9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN Name=INPP5B {ECO:0000313|Ensembl:ENSXMAP00000014663.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014663.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000014663.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014663.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000256|ARBA:ARBA00005910}.
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DR AlphaFoldDB; M4AJL9; -.
DR STRING; 8083.ENSXMAP00000014663; -.
DR Ensembl; ENSXMAT00000014683.2; ENSXMAP00000014663.2; ENSXMAG00000014629.2.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156762; -.
DR HOGENOM; CLU_006779_2_0_1; -.
DR InParanoid; M4AJL9; -.
DR OMA; VREDAWC; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; IEA:InterPro.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09093; INPP5c_INPP5B; 1.
DR CDD; cd04380; RhoGAP_OCRL1; 1.
DR Gene3D; 2.30.29.110; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR031896; INPP5B_PH_dom.
DR InterPro; IPR046985; IP5.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR048869; OCRL-1_2_ASH.
DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR047078; RhoGAP_OCRL1.
DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR PANTHER; PTHR11200:SF163; TYPE II INOSITOL 1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; 1.
DR Pfam; PF16776; INPP5B_PH; 1.
DR Pfam; PF21310; OCRL-like_ASH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 723..901
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 168..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 103200 MW; EFD66FDCE89FAFB6 CRC64;
MDQSVAIQET LGKEENCIVA AQCDILLEDC SESRLLGLVE CAKEHAIFIY THRRMAITAD
DVSLEDIIPI TLDFAVVEVS SPEQLVVVGA DTRVRMSYKN EKLELRLPFG SHSRFFLGEV
NKAWSDVCRL PTQVPKFEWT KKYKKSIKRQ EATKQAIAPL EVLSTKNNQH QKIEKVSDKK
GSLEKVKSSN SISQKSKGNS SQDNQSISSR EERDDLVRSS SHTASNKAQI LAMPQFGLRD
NLIRCELLKS EDSYTYLENF RFFLGTYNVN GQTPKESLRP WLSCTPDPPD IYCLGFQELD
LSKEAFFFSD TPKELEWMKA VFEALHEEAN YALVKLIRLV GIMLIFYVKK EHAEFISDVE
AETVGTGIMG RMGNKGAVSI RFRFHNSDIC VVNSHLAAHV EEYERRNQDF KDICSRLQFR
QLDPTQPPLT ILKHNVVLWI GDLNYRISDL DVDSVKDLIS KNDFETLHSY DQLKRQIDVE
AVFVGFKEGE IDFQPTYKYD TGSDKWDTSE KCRIPAWCDR ILWKGKNIQQ NHYKSHMDVR
TSDHKPVSSL LIIGIKRVNP EAYKKTFEEI VRNIDKMENE CIPSLSLSKR EFHFKDVKFM
QHHAETLNLF NDGQVPCQFE FIQKPNESTY SKPWLTANPS KGFIAQGASM DIDLEVFVNR
TTAPDLNCGK QEIEDILVLH LERGKDYFIS VTGNYLPSCY GTSIYSLCHM KEPIQDMPKE
TLLELAEKSP NDDTATDEKP LDIPKELWMM VDHLFRNAVD QEDLFQQPGL RTEFAEIRDC
LDSGMPDSLP GSNHSVAEAL LLFLDALPEP VIPFPFYQQC LECSSSAGQC EKVISMLPQF
HKNVFNYLAA FLRELLKNSA NNRLEVAILA TIFASLLLRS PTKQDFAEKR KTQEFFQHFL
T
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