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72 kDa inositol polyphosphate 5-phosphatase (EC 3.1.3.36) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (Phosphatidylinositol polyphosphate 5-phosphatase type IV)

 INP5E_HUMAN             Reviewed;         644 AA.
Q9NRR6; Q15734; Q6PIV5;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
27-SEP-2017, entry version 137.
RecName: Full=72 kDa inositol polyphosphate 5-phosphatase;
EC=3.1.3.36 {ECO:0000269|PubMed:10764818};
AltName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase;
AltName: Full=Phosphatidylinositol polyphosphate 5-phosphatase type IV;
Flags: Precursor;
Name=INPP5E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
ACTIVITY, ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10764818; DOI=10.1074/jbc.M910119199;
Kisseleva M.V., Wilson M.P., Majerus P.W.;
"The isolation and characterization of a cDNA encoding phospholipid-
specific inositol polyphosphate 5-phosphatase.";
J. Biol. Chem. 275:20110-20116(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 469-644 (ISOFORM 1).
Nussbaum R.L.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
SUBCELLULAR LOCATION, AND INVOLVEMENT IN MORMS.
PubMed=19668215; DOI=10.1038/ng.427;
Jacoby M., Cox J.J., Gayral S., Hampshire D.J., Ayub M., Blockmans M.,
Pernot E., Kisseleva M.V., Compere P., Schiffmann S.N., Gergely F.,
Riley J.H., Perez-Morga D., Woods C.G., Schurmans S.;
"INPP5E mutations cause primary cilium signaling defects, ciliary
instability and ciliopathies in human and mouse.";
Nat. Genet. 41:1027-1031(2009).
[8]
SUBCELLULAR LOCATION, VARIANTS JBTS1 CYS-378; GLN-435; TRP-512;
TRP-515; HIS-563 AND GLU-580, AND CHARACTERIZATION OF VARIANTS JBTS1
CYS-378; GLN-435; TRP-512; TRP-515; HIS-563 AND GLU-580.
PubMed=19668216; DOI=10.1038/ng.423;
Bielas S.L., Silhavy J.L., Brancati F., Kisseleva M.V., Al-Gazali L.,
Sztriha L., Bayoumi R.A., Zaki M.S., Abdel-Aleem A., Rosti R.O.,
Kayserili H., Swistun D., Scott L.C., Bertini E., Boltshauser E.,
Fazzi E., Travaglini L., Field S.J., Gayral S., Jacoby M.,
Schurmans S., Dallapiccola B., Majerus P.W., Valente E.M.,
Gleeson J.G.;
"Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E,
link phosphatidyl inositol signaling to the ciliopathies.";
Nat. Genet. 41:1032-1036(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
INTERACTION WITH PDE6D, SUBCELLULAR LOCATION, ISOPRENYLATION AT
CYS-641, METHYLATION AT CYS-641, AND MUTAGENESIS OF CYS-641.
PubMed=24166846; DOI=10.1002/humu.22470;
Thomas S., Wright K.J., Le Corre S., Micalizzi A., Romani M.,
Abhyankar A., Saada J., Perrault I., Amiel J., Litzler J., Filhol E.,
Elkhartoufi N., Kwong M., Casanova J.L., Boddaert N., Baehr W.,
Lyonnet S., Munnich A., Burglen L., Chassaing N., Encha-Ravazi F.,
Vekemans M., Gleeson J.G., Valente E.M., Jackson P.K., Drummond I.A.,
Saunier S., Attie-Bitach T.;
"A homozygous PDE6D mutation in Joubert syndrome impairs targeting of
farnesylated INPP5E protein to the primary cilium.";
Hum. Mutat. 35:137-146(2014).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 275-623.
Structural genomics consortium (SGC);
"Crystal structure of human INPP5E.";
Submitted (NOV-2010) to the PDB data bank.
[12]
VARIANTS JBTS1 ARG-286; MET-303; SER-345; ASN-426; GLN-435; ARG-474;
ASP-534; HIS-563; CYS-585; GLN-621 AND ARG-641.
PubMed=23386033; DOI=10.1038/ejhg.2012.305;
International JSRD Study Group;
Travaglini L., Brancati F., Silhavy J., Iannicelli M., Nickerson E.,
Elkhartoufi N., Scott E., Spencer E., Gabriel S., Thomas S.,
Ben-Zeev B., Bertini E., Boltshauser E., Chaouch M., Cilio M.R.,
de Jong M.M., Kayserili H., Ogur G., Poretti A., Signorini S.,
Uziel G., Zaki M.S., Johnson C., Attie-Bitach T., Gleeson J.G.,
Valente E.M.;
"Phenotypic spectrum and prevalence of INPP5E mutations in Joubert
syndrome and related disorders.";
Eur. J. Hum. Genet. 21:1074-1078(2013).
[13]
VARIANT JBTS1 GLN-621, AND INVOLVEMENT IN JBTS1.
PubMed=23034536; DOI=10.1038/jhg.2012.117;
Tsurusaki Y., Kobayashi Y., Hisano M., Ito S., Doi H., Nakashima M.,
Saitsu H., Matsumoto N., Miyake N.;
"The diagnostic utility of exome sequencing in Joubert syndrome and
related disorders.";
J. Hum. Genet. 58:113-115(2013).
-!- FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate
(PtdIns 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5-
bisphosphate to phosphatidylinositol 4-phosphate. Specific for
lipid substrates, inactive towards water soluble inositol
phosphates. {ECO:0000269|PubMed:10764818}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate
+ phosphate. {ECO:0000269|PubMed:10764818}.
-!- ENZYME REGULATION: Active in the presence of octyl-glucoside or
Triton X-100, but completely inhibited by CTAB.
{ECO:0000269|PubMed:10764818}.
-!- SUBUNIT: Interacts (when prenylated) with PDE6D; this is important
for normal location in cilia. {ECO:0000269|PubMed:24166846}.
-!- INTERACTION:
P62258:YWHAE; NbExp=3; IntAct=EBI-11900149, EBI-356498;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
{ECO:0000269|PubMed:19668215, ECO:0000269|PubMed:19668216,
ECO:0000269|PubMed:24166846}. Golgi apparatus, Golgi stack
membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q9JII1}. Cell membrane
{ECO:0000250|UniProtKB:Q9WVR1}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9WVR1}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q9WVR1}. Cell projection, ruffle
{ECO:0000250|UniProtKB:Q9WVR1}. Cytoplasm
{ECO:0000250|UniProtKB:Q9WVR1}. Note=Peripheral membrane protein
associated with Golgi stacks. {ECO:0000250|UniProtKB:Q9JII1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NRR6-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRR6-2; Sequence=VSP_009799;
-!- TISSUE SPECIFICITY: Detected in brain, heart, pancreas, testis and
spleen. {ECO:0000269|PubMed:10764818}.
-!- DISEASE: Joubert syndrome 1 (JBTS1) [MIM:213300]: A disorder
presenting with cerebellar ataxia, oculomotor apraxia, hypotonia,
neonatal breathing abnormalities and psychomotor delay.
Neuroradiologically, it is characterized by cerebellar vermian
hypoplasia/aplasia, thickened and reoriented superior cerebellar
peduncles, and an abnormally large interpeduncular fossa, giving
the appearance of a molar tooth on transaxial slices (molar tooth
sign). Additional variable features include retinal dystrophy and
renal disease. {ECO:0000269|PubMed:19668216,
ECO:0000269|PubMed:23034536, ECO:0000269|PubMed:23386033}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Mental retardation, truncal obesity, retinal dystrophy,
and micropenis (MORMS) [MIM:610156]: An autosomal recessive
disorder characterized by moderate mental retardation, truncal
obesity, congenital non-progressive retinal dystrophy, and
micropenis in males. The phenotype is similar to Bardet-Biedl
syndrome and Cohen syndrome Distinguishing features are the age of
onset, the non-progressive nature of the visual impairment, lack
of dysmorphic facies, skin or gingival infection, microcephaly,
mottled retina, polydactyly, and testicular anomalies.
{ECO:0000269|PubMed:19668215}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
phosphatase type IV family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB03215.1; Type=Miscellaneous discrepancy; Note=Several sequencing problems.; Evidence={ECO:0000305};
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EMBL; AF187891; AAF81404.1; -; mRNA.
EMBL; AL592301; CAI13947.1; -; Genomic_DNA.
EMBL; CH471090; EAW88234.1; -; Genomic_DNA.
EMBL; BC028032; AAH28032.1; -; mRNA.
EMBL; U45974; AAB03215.1; ALT_SEQ; mRNA.
CCDS; CCDS7000.1; -. [Q9NRR6-1]
RefSeq; NP_001305431.1; NM_001318502.1.
RefSeq; NP_063945.2; NM_019892.5. [Q9NRR6-1]
UniGene; Hs.120998; -.
PDB; 2XSW; X-ray; 1.90 A; A/B=275-623.
PDBsum; 2XSW; -.
ProteinModelPortal; Q9NRR6; -.
SMR; Q9NRR6; -.
CORUM; Q9NRR6; -.
IntAct; Q9NRR6; 55.
STRING; 9606.ENSP00000360777; -.
SwissLipids; SLP:000001180; -.
DEPOD; Q9NRR6; -.
iPTMnet; Q9NRR6; -.
PhosphoSitePlus; Q9NRR6; -.
BioMuta; INPP5E; -.
DMDM; 212276439; -.
MaxQB; Q9NRR6; -.
PaxDb; Q9NRR6; -.
PeptideAtlas; Q9NRR6; -.
PRIDE; Q9NRR6; -.
Ensembl; ENST00000371712; ENSP00000360777; ENSG00000148384. [Q9NRR6-1]
GeneID; 56623; -.
KEGG; hsa:56623; -.
UCSC; uc004cho.4; human. [Q9NRR6-1]
CTD; 56623; -.
DisGeNET; 56623; -.
EuPathDB; HostDB:ENSG00000148384.11; -.
GeneCards; INPP5E; -.
GeneReviews; INPP5E; -.
H-InvDB; HIX0125641; -.
HGNC; HGNC:21474; INPP5E.
HPA; HPA065758; -.
MalaCards; INPP5E; -.
MIM; 213300; phenotype.
MIM; 610156; phenotype.
MIM; 613037; gene.
neXtProt; NX_Q9NRR6; -.
OpenTargets; ENSG00000148384; -.
Orphanet; 475; Joubert syndrome.
Orphanet; 1454; Joubert syndrome with hepatic defect.
Orphanet; 220493; Joubert syndrome with ocular defect.
Orphanet; 75858; MORM syndrome.
PharmGKB; PA164741785; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000231541; -.
HOVERGEN; HBG052132; -.
InParanoid; Q9NRR6; -.
KO; K20278; -.
OMA; EMRKGSI; -.
OrthoDB; EOG091G05DT; -.
PhylomeDB; Q9NRR6; -.
TreeFam; TF323475; -.
BioCyc; MetaCyc:HS09270-MONOMER; -.
BRENDA; 3.1.3.36; 2681.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
ChiTaRS; INPP5E; human.
GenomeRNAi; 56623; -.
PRO; PR:Q9NRR6; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148384; -.
CleanEx; HS_INPP5E; -.
Genevisible; Q9NRR6; HS.
GO; GO:0005930; C:axoneme; IDA:UniProtKB.
GO; GO:0005929; C:cilium; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; TAS:UniProtKB.
GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; TAS:Reactome.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Ensembl.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
Pfam; PF03372; Exo_endo_phos; 1.
SMART; SM00128; IPPc; 1.
SUPFAM; SSF56219; SSF56219; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Ciliopathy; Cilium; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Golgi apparatus; Hydrolase; Joubert syndrome;
Lipid metabolism; Lipoprotein; Membrane; Mental retardation;
Methylation; Obesity; Phosphoprotein; Polymorphism; Prenylation;
Reference proteome; Repeat.
CHAIN 1 641 72 kDa inositol polyphosphate 5-
phosphatase.
{ECO:0000305|PubMed:24166846}.
/FTId=PRO_0000209747.
PROPEP 642 644 Removed in mature form.
{ECO:0000305|PubMed:24166846}.
/FTId=PRO_0000431688.
REPEAT 10 13 1.
REPEAT 15 18 2.
REPEAT 28 31 3.
REPEAT 39 42 4.
REPEAT 55 58 5.
REPEAT 69 71 6.
REPEAT 72 74 7.
REPEAT 75 78 8.
REPEAT 121 124 9.
REPEAT 169 172 10.
REPEAT 183 185 11.
REPEAT 190 193 12.
REPEAT 236 239 13.
REGION 10 242 13 X 4 AA repeats of P-X-X-P.
COMPBIAS 92 97 Poly-Arg.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WVR1}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JII1}.
MOD_RES 641 641 Cysteine methyl ester.
{ECO:0000305|PubMed:24166846}.
LIPID 641 641 S-farnesyl cysteine.
{ECO:0000305|PubMed:24166846}.
VAR_SEQ 346 379 Missing (in isoform 2).
{ECO:0000303|PubMed:10764818}.
/FTId=VSP_009799.
VARIANT 201 201 I -> M (in dbSNP:rs36064831).
/FTId=VAR_047078.
VARIANT 286 286 G -> R (in JBTS1; dbSNP:rs757936530).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077247.
VARIANT 303 303 V -> M (in JBTS1; dbSNP:rs746212325).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077248.
VARIANT 345 345 R -> S (in JBTS1).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077249.
VARIANT 378 378 R -> C (in JBTS1; slightly reduced
activity; dbSNP:rs121918130).
{ECO:0000269|PubMed:19668216}.
/FTId=VAR_063012.
VARIANT 426 426 T -> N (in JBTS1).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077250.
VARIANT 435 435 R -> Q (in JBTS1; severe reduction of
activity; dbSNP:rs121918129).
{ECO:0000269|PubMed:19668216,
ECO:0000269|PubMed:23386033}.
/FTId=VAR_063013.
VARIANT 474 474 W -> R (in JBTS1; unknown pathological
significance).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077251.
VARIANT 512 512 R -> W (in JBTS1; associated with W-515;
severe reduction of activity;
dbSNP:rs374152018).
{ECO:0000269|PubMed:19668216}.
/FTId=VAR_063014.
VARIANT 515 515 R -> W (in JBTS1; associated with W-512;
severe reduction of activity;
dbSNP:rs13297509).
{ECO:0000269|PubMed:19668216}.
/FTId=VAR_063015.
VARIANT 534 534 Y -> D (in JBTS1).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077252.
VARIANT 563 563 R -> H (in JBTS1; slightly reduced
activity; dbSNP:rs121918128).
{ECO:0000269|PubMed:19668216,
ECO:0000269|PubMed:23386033}.
/FTId=VAR_063016.
VARIANT 580 580 K -> E (in JBTS1; severe reduction of
activity). {ECO:0000269|PubMed:19668216}.
/FTId=VAR_063017.
VARIANT 585 585 R -> C (in JBTS1; dbSNP:rs763992407).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077253.
VARIANT 621 621 R -> Q (in JBTS1).
{ECO:0000269|PubMed:23034536,
ECO:0000269|PubMed:23386033}.
/FTId=VAR_076892.
VARIANT 641 641 C -> R (in JBTS1).
{ECO:0000269|PubMed:23386033}.
/FTId=VAR_077254.
MUTAGEN 641 641 C->A: Abolishes farnesylation-dependent
interaction with PDE6D.
{ECO:0000269|PubMed:24166846}.
CONFLICT 345 345 R -> T (in Ref. 1; AAF81404).
{ECO:0000305}.
HELIX 287 293 {ECO:0000244|PDB:2XSW}.
STRAND 298 307 {ECO:0000244|PDB:2XSW}.
HELIX 319 322 {ECO:0000244|PDB:2XSW}.
STRAND 332 340 {ECO:0000244|PDB:2XSW}.
HELIX 345 356 {ECO:0000244|PDB:2XSW}.
STRAND 360 368 {ECO:0000244|PDB:2XSW}.
STRAND 371 378 {ECO:0000244|PDB:2XSW}.
HELIX 379 384 {ECO:0000244|PDB:2XSW}.
STRAND 389 399 {ECO:0000244|PDB:2XSW}.
STRAND 402 413 {ECO:0000244|PDB:2XSW}.
STRAND 416 424 {ECO:0000244|PDB:2XSW}.
HELIX 432 445 {ECO:0000244|PDB:2XSW}.
STRAND 450 452 {ECO:0000244|PDB:2XSW}.
HELIX 457 459 {ECO:0000244|PDB:2XSW}.
HELIX 465 467 {ECO:0000244|PDB:2XSW}.
STRAND 468 477 {ECO:0000244|PDB:2XSW}.
STRAND 482 484 {ECO:0000244|PDB:2XSW}.
HELIX 486 493 {ECO:0000244|PDB:2XSW}.
HELIX 501 505 {ECO:0000244|PDB:2XSW}.
HELIX 509 515 {ECO:0000244|PDB:2XSW}.
STRAND 518 520 {ECO:0000244|PDB:2XSW}.
STRAND 540 543 {ECO:0000244|PDB:2XSW}.
STRAND 556 564 {ECO:0000244|PDB:2XSW}.
STRAND 567 575 {ECO:0000244|PDB:2XSW}.
STRAND 581 584 {ECO:0000244|PDB:2XSW}.
STRAND 587 594 {ECO:0000244|PDB:2XSW}.
HELIX 611 623 {ECO:0000244|PDB:2XSW}.
SEQUENCE 644 AA; 70205 MW; 5B6CFB75CD0ADC9A CRC64;
MPSKAENLRP SEPAPQPPEG RTLQGQLPGA PPAQRAGSPP DAPGSESPAL ACSTPATPSG
EDPPARAAPI APRPPARPRL ERALSLDDKG WRRRRFRGSQ EDLEARNGTS PSRGSVQSEG
PGAPAHSCSP PCLSTSLQEI PKSRGVLSSE RGSPSSGGNP LSGVASSSPN LPHRDAAVAG
SSPRLPSLLP PRPPPALSLD IASDSLRTAN KVDSDLADYK LRAQPLLVRA HSSLGPGRPR
SPLACDDCSL RSAKSSFSLL APIRSKDVRS RSYLEGSLLA SGALLGADEL ARYFPDRNVA
LFVATWNMQG QKELPPSLDE FLLPAEADYA QDLYVIGVQE GCSDRREWET RLQETLGPHY
VLLSSAAHGV LYMSLFIRRD LIWFCSEVEC STVTTRIVSQ IKTKGALGIS FTFFGTSFLF
ITSHFTSGDG KVAERLLDYT RTVQALVLPR NVPDTNPYRS SAADVTTRFD EVFWFGDFNF
RLSGGRTVVD ALLCQGLVVD VPALLQHDQL IREMRKGSIF KGFQEPDIHF LPSYKFDIGK
DTYDSTSKQR TPSYTDRVLY RSRHKGDICP VSYSSCPGIK TSDHRPVYGL FRVKVRPGRD
NIPLAAGKFD RELYLLGIKR RISKEIQRQQ ALQSQNSSTI CSVS


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