I5P2_HUMAN
ID I5P2_HUMAN Reviewed; 993 AA.
AC P32019; C9J6U5; Q5VSG9; Q5VSH0; Q5VSH1; Q658Q5; Q6P6D4; Q6PD53; Q86YE1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Type II inositol 1,4,5-trisphosphate 5-phosphatase;
DE EC=3.1.3.36;
DE AltName: Full=75 kDa inositol polyphosphate-5-phosphatase;
DE AltName: Full=Phosphoinositide 5-phosphatase;
DE Short=5PTase;
DE Flags: Precursor;
GN Name=INPP5B; Synonyms=OCRL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-990, MUTAGENESIS OF CYS-990,
RP AND VARIANT THR-745.
RX PubMed=7721860; DOI=10.1074/jbc.270.16.9370;
RA Jefferson A.B., Majerus P.W.;
RT "Properties of type II inositol polyphosphate 5-phosphatase.";
RL J. Biol. Chem. 270:9370-9377(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT THR-745.
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339, AND
RP VARIANT THR-745.
RC TISSUE=Placenta;
RX PubMed=1718960; DOI=10.1016/s0021-9258(18)54920-6;
RA Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W.;
RT "Cloning and expression of human 75-kDa inositol polyphosphate-5-
RT phosphatase.";
RL J. Biol. Chem. 266:20283-20289(1991).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RAB GTPASES.
RX PubMed=17956944; DOI=10.1242/jcs.014423;
RA Williams C., Choudhury R., McKenzie E., Lowe M.;
RT "Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to
RT the early secretory pathway.";
RL J. Cell Sci. 120:3941-3951(2007).
RN [7]
RP INTERACTION WITH FAM109A.
RX PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT "Two closely related endocytic proteins that share a common OCRL-binding
RT motif with APPL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH FAM109A AND FAM109B.
RX PubMed=21233288; DOI=10.1091/mbc.e10-08-0730;
RA Noakes C.J., Lee G., Lowe M.;
RT "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in
RT the endocytic pathway.";
RL Mol. Biol. Cell 22:606-623(2011).
RN [10]
RP INTERACTION WITH INPP5F.
RX PubMed=25869668; DOI=10.1083/jcb.201409064;
RA Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M.,
RA De Camilli P.;
RT "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic
RT pathway.";
RL J. Cell Biol. 209:85-95(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB8A.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 339-646 IN COMPLEX WITH MAGNESIUM
RP AND PHOSPHATIDYLINOSITOL 4-PHOSPHATE.
RG Structural genomics consortium (SGC);
RT "Crystal structure of INPP5B in complex with phosphatidylinositol 4-
RT phosphate (CASP target).";
RL Submitted (JUL-2010) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate
CC (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-
CC trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular
CC signaling events. {ECO:0000269|PubMed:7721860}.
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 Evidence={ECO:0000269|PubMed:7721860};
CC -!- SUBUNIT: Interacts with APPL1, FAM109A and FAM109B (PubMed:20133602,
CC PubMed:21233288). Interacts with several Rab GTPases, at least RAB1A,
CC RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may
CC play a dual role in targeting INPP5B to the specific membranes and
CC stimulating its phosphatase activity (PubMed:17956944, PubMed:26824392,
CC Ref.12). Interacts preferentially with non-phosphorylated RAB8A;
CC phosphoryation of RAB8A on 'Thr-72' disrupts this interaction
CC (PubMed:26824392). Interacts with INPP5F (PubMed:25869668).
CC {ECO:0000269|PubMed:17956944, ECO:0000269|PubMed:20133602,
CC ECO:0000269|PubMed:21233288, ECO:0000269|PubMed:25869668,
CC ECO:0000269|PubMed:26824392, ECO:0000269|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7721860}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000269|PubMed:17956944}. Early endosome membrane
CC {ECO:0000269|PubMed:17956944}. Membrane {ECO:0000269|PubMed:7721860};
CC Peripheral membrane protein {ECO:0000305|PubMed:7721860}; Cytoplasmic
CC side {ECO:0000305|PubMed:7721860}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q8K337}. Golgi apparatus
CC {ECO:0000269|PubMed:17956944}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P32019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P32019-2; Sequence=VSP_012820;
CC Name=3;
CC IsoId=P32019-3; Sequence=VSP_012821;
CC Name=4;
CC IsoId=P32019-4; Sequence=VSP_013902, VSP_013903;
CC -!- TISSUE SPECIFICITY: Platelets.
CC -!- DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating)
CC domains form a single folding module. The ASH domain has an
CC immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic
CC arginine and is catalytically inactive. The ASH-RhoGAP module regulates
CC the majority of the protein-protein interactions currently described.
CC The ASH domain mediates association with membrane-targeting Rab
CC GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1,
CC which is then displaced by FAM109A and FAM109B as endosomes mature, all
CC three interactions rely on F&H motifs, an approximately 12-13 amino-
CC acid sequence centered around Phe and His residues essential for
CC binding (By similarity). {ECO:0000250}.
CC -!- PTM: Isoprenylation at Cys-990 may be required for localization at the
CC membrane. {ECO:0000269|PubMed:7721860}.
CC -!- PTM: May be proteolytically cleaved after Lys-320 as inferred from N-
CC terminal protein sequence of the 75 kda form.
CC {ECO:0000269|PubMed:1718960}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79207.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M74161; AAA79207.1; ALT_INIT; mRNA.
DR EMBL; AL603790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX296560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042529; AAH42529.2; -; mRNA.
DR EMBL; BC058932; AAH58932.1; -; mRNA.
DR EMBL; AL833055; CAH56301.1; -; mRNA.
DR CCDS; CCDS41306.1; -. [P32019-2]
DR CCDS; CCDS72760.1; -. [P32019-3]
DR RefSeq; NP_001284363.1; NM_001297434.1. [P32019-3]
DR RefSeq; NP_005531.2; NM_005540.2. [P32019-2]
DR PDB; 3MTC; X-ray; 2.40 A; A=339-643.
DR PDB; 3N9V; X-ray; 2.65 A; A/B=342-646.
DR PDB; 4CML; X-ray; 2.30 A; A=339-643.
DR PDB; 5A7I; X-ray; 2.89 A; A=339-643.
DR PDB; 5A7J; X-ray; 2.90 A; A/B=339-643.
DR PDBsum; 3MTC; -.
DR PDBsum; 3N9V; -.
DR PDBsum; 4CML; -.
DR PDBsum; 5A7I; -.
DR PDBsum; 5A7J; -.
DR AlphaFoldDB; P32019; -.
DR SMR; P32019; -.
DR BioGRID; 109845; 24.
DR IntAct; P32019; 21.
DR MINT; P32019; -.
DR STRING; 9606.ENSP00000362115; -.
DR BindingDB; P32019; -.
DR ChEMBL; CHEMBL2636; -.
DR DrugBank; DB03158; D-Myo-Inositol-1,4-Bisphosphate.
DR DEPOD; INPP5B; -.
DR GlyGen; P32019; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P32019; -.
DR PhosphoSitePlus; P32019; -.
DR BioMuta; INPP5B; -.
DR DMDM; 281185510; -.
DR EPD; P32019; -.
DR jPOST; P32019; -.
DR MassIVE; P32019; -.
DR MaxQB; P32019; -.
DR PaxDb; P32019; -.
DR PeptideAtlas; P32019; -.
DR PRIDE; P32019; -.
DR ProteomicsDB; 54832; -. [P32019-1]
DR ProteomicsDB; 54833; -. [P32019-2]
DR ProteomicsDB; 54834; -. [P32019-3]
DR ProteomicsDB; 54835; -. [P32019-4]
DR ABCD; P32019; 1 sequenced antibody.
DR Antibodypedia; 31808; 172 antibodies from 25 providers.
DR DNASU; 3633; -.
DR Ensembl; ENST00000373023.6; ENSP00000362114.2; ENSG00000204084.13. [P32019-1]
DR Ensembl; ENST00000373024.8; ENSP00000362115.3; ENSG00000204084.13. [P32019-2]
DR Ensembl; ENST00000373026.5; ENSP00000362117.1; ENSG00000204084.13. [P32019-1]
DR Ensembl; ENST00000373027.5; ENSP00000362118.1; ENSG00000204084.13. [P32019-3]
DR GeneID; 3633; -.
DR KEGG; hsa:3633; -.
DR MANE-Select; ENST00000373024.8; ENSP00000362115.3; NM_005540.3; NP_005531.2. [P32019-2]
DR UCSC; uc001ccf.1; human. [P32019-1]
DR CTD; 3633; -.
DR DisGeNET; 3633; -.
DR GeneCards; INPP5B; -.
DR HGNC; HGNC:6077; INPP5B.
DR HPA; ENSG00000204084; Low tissue specificity.
DR MIM; 147264; gene.
DR neXtProt; NX_P32019; -.
DR OpenTargets; ENSG00000204084; -.
DR PharmGKB; PA29885; -.
DR VEuPathDB; HostDB:ENSG00000204084; -.
DR eggNOG; KOG0565; Eukaryota.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000156762; -.
DR HOGENOM; CLU_006779_2_0_1; -.
DR InParanoid; P32019; -.
DR OMA; ECANNYL; -.
DR OrthoDB; 1399831at2759; -.
DR PhylomeDB; P32019; -.
DR TreeFam; TF317034; -.
DR BioCyc; MetaCyc:HS05898-MON; -.
DR BRENDA; 3.1.3.36; 2681.
DR PathwayCommons; P32019; -.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SABIO-RK; P32019; -.
DR SignaLink; P32019; -.
DR BioGRID-ORCS; 3633; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; INPP5B; human.
DR EvolutionaryTrace; P32019; -.
DR GeneWiki; INPP5B; -.
DR GenomeRNAi; 3633; -.
DR Pharos; P32019; Tbio.
DR PRO; PR:P32019; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P32019; protein.
DR Bgee; ENSG00000204084; Expressed in left ovary and 148 other tissues.
DR ExpressionAtlas; P32019; baseline and differential.
DR Genevisible; P32019; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; TAS:Reactome.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd09093; INPP5c_INPP5B; 1.
DR CDD; cd13383; PH_OCRL2; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR031896; INPP5B_PH_dom.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR037793; OCRL1/INPP5B_INPP5c.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF16776; INPP5B_PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; Golgi apparatus; Hydrolase;
KW Lipid metabolism; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Methylation; Prenylation; Reference proteome.
FT CHAIN 1..990
FT /note="Type II inositol 1,4,5-trisphosphate 5-phosphatase"
FT /id="PRO_0000015640"
FT PROPEP 991..993
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422293"
FT DOMAIN 22..148
FT /note="PH"
FT DOMAIN 821..993
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 224..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..668
FT /note="5-phosphatase"
FT /evidence="ECO:0000250"
FT REGION 669..782
FT /note="ASH"
FT /evidence="ECO:0000250"
FT COMPBIAS 228..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 383
FT /ligand="substrate"
FT BINDING 459..460
FT /ligand="substrate"
FT BINDING 582..583
FT /ligand="substrate"
FT BINDING 596..598
FT /ligand="substrate"
FT MOD_RES 990
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 990
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_012821"
FT VAR_SEQ 178..257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7721860"
FT /id="VSP_012820"
FT VAR_SEQ 810..828
FT /note="TLMPVWTGDDGSQLDSPME -> LAYLAAYCFETQLVTKSLI (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013902"
FT VAR_SEQ 829..993
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013903"
FT VARIANT 46
FT /note="G -> S (in dbSNP:rs56993041)"
FT /id="VAR_061270"
FT VARIANT 745
FT /note="M -> T (in dbSNP:rs11488569)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1718960, ECO:0000269|PubMed:7721860"
FT /id="VAR_028002"
FT MUTAGEN 990
FT /note="C->S: Loss of prenylation and membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:7721860"
FT CONFLICT 587..606
FT /note="GSDDWDTSEKCRAPAWCDRI -> RALTTGIPVRSAVLLPGVIGF (in
FT Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="G -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 340..353
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 435..440
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 488..501
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:3MTC"
FT STRAND 518..527
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:4CML"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:5A7J"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:5A7J"
FT STRAND 604..620
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:4CML"
FT STRAND 632..643
FT /evidence="ECO:0007829|PDB:4CML"
SQ SEQUENCE 993 AA; 112852 MW; ABD3581CC6CD29D6 CRC64;
MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM
AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM
FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY
PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE
AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD
MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK
ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK
LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH
LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV
KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD
KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN
ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL
PSCFGSPIHT LCYMREPILD LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL
YRNAVQQEDL FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY
STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG
SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL
