SAC2_MOUSE
ID SAC2_MOUSE Reviewed; 1132 AA.
AC Q8CDA1; Q3UCS0; Q6NX83; Q6ZQ16; Q8C8G7; Q8CBW2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphatidylinositide phosphatase SAC2;
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:Q9Y2H2, ECO:0000269|PubMed:25869669};
DE AltName: Full=Inositol polyphosphate 5-phosphatase F {ECO:0000312|MGI:MGI:2141867};
DE AltName: Full=Sac domain-containing inositol phosphatase 2;
DE AltName: Full=Sac domain-containing phosphoinositide 4-phosphatase 2 {ECO:0000305|PubMed:25869669};
DE Short=hSAC2;
GN Name=Inpp5f {ECO:0000312|MGI:MGI:2141867}; Synonyms=Kiaa0966, Sac2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Diencephalon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, AND INDUCTION.
RX PubMed=17322895; DOI=10.1038/nm1552;
RA Trivedi C.M., Luo Y., Yin Z., Zhang M., Zhu W., Wang T., Floss T.,
RA Goettlicher M., Noppinger P.R., Wurst W., Ferrari V.A., Abrams C.S.,
RA Gruber P.J., Epstein J.A.;
RT "Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3 beta
RT activity.";
RL Nat. Med. 13:324-331(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19875726; DOI=10.1161/circresaha.109.208785;
RA Zhu W., Trivedi C.M., Zhou D., Yuan L., Lu M.M., Epstein J.A.;
RT "Inpp5f is a polyphosphoinositide phosphatase that regulates cardiac
RT hypertrophic responsiveness.";
RL Circ. Res. 105:1240-1247(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; SER-827; SER-830;
RP SER-879; SER-882; SER-908; SER-911 AND SER-1103, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INPP4A; INPP5B; OCRL AND
RP RAB5A, AND MUTAGENESIS OF ASP-460.
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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25869669; DOI=10.1083/jcb.201408027;
RA Hsu F., Hu F., Mao Y.;
RT "Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2
RT regulates endocytic recycling.";
RL J. Cell Biol. 209:97-110(2015).
RN [10]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26203138; DOI=10.1523/jneurosci.1718-15.2015;
RA Zou Y., Stagi M., Wang X., Yigitkanli K., Siegel C.S., Nakatsu F.,
RA Cafferty W.B., Strittmatter S.M.;
RT "Gene-silencing screen for mammalian axon regeneration identifies Inpp5f
RT (Sac2) as an endogenous suppressor of repair after spinal cord injury.";
RL J. Neurosci. 35:10429-10439(2015).
CC -!- FUNCTION: Inositol 4-phosphatase which mainly acts on
CC phosphatidylinositol 4-phosphate. May be functionally linked to OCRL,
CC which converts phosphatidylinositol 4,5-bisphosphate to
CC phosphatidylinositol, for a sequential dephosphorylation of
CC phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of
CC inositol, thus playing an important role in the endocytic recycling
CC (PubMed:25869668, PubMed:25869669). Regulator of TF:TFRC and integrins
CC recycling pathway, is also involved in cell migration mechanisms (By
CC similarity). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B
CC phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling
CC pathway through inhibition of STAT3 phosphorylation and translocation
CC to the nucleus (By similarity). Functionally important modulator of
CC cardiac myocyte size and of the cardiac response to stress
CC (PubMed:19875726). May play a role as negative regulator of axon
CC regeneration after central nervous system injuries (PubMed:26203138).
CC {ECO:0000250|UniProtKB:Q9Y2H2, ECO:0000269|PubMed:17322895,
CC ECO:0000269|PubMed:19875726, ECO:0000269|PubMed:25869668,
CC ECO:0000269|PubMed:25869669, ECO:0000269|PubMed:26203138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2H2};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with OCRL and RAB5.
CC Interacts with INPP5B and INPP4A (PubMed:25869668). Interacts with
CC STAT3; the interaction is independent of STAT3 'TYR-705'
CC phosphorylation status (By similarity). {ECO:0000250|UniProtKB:Q9Y2H2,
CC ECO:0000269|PubMed:25869668}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:25869668}. Early endosome
CC {ECO:0000269|PubMed:25869668}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9Y2H2}. Note=Also found on macropinosomes.
CC {ECO:0000269|PubMed:25869668}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CDA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDA1-2; Sequence=VSP_033271, VSP_033274;
CC Name=3;
CC IsoId=Q8CDA1-3; Sequence=VSP_033270;
CC Name=4;
CC IsoId=Q8CDA1-4; Sequence=VSP_033272, VSP_033273;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and hypothalamus,
CC expressed in lung and pancreas, and detected at low levels in liver and
CC heart (at protein level). {ECO:0000269|PubMed:25869669,
CC ECO:0000269|PubMed:26203138}.
CC -!- INDUCTION: Up-regulated in the absence of histone deacetylase 2/HDAC2
CC in the heart from HDAC2-null mice. {ECO:0000269|PubMed:17322895}.
CC -!- DISRUPTION PHENOTYPE: Animals develop normal corticospinal tract and
CC raphespinal tract. Mutants show greater axonal growth and functional
CC recovery after central nervous system trauma (PubMed:26203138).
CC Knockout mice have normal cardiac form and function but show augmented
CC hypertrophy and reactivation of the fetal gene program in response to
CC stress compared to wild-type littermates (PubMed:19875726).
CC {ECO:0000269|PubMed:19875726, ECO:0000269|PubMed:26203138}.
CC -!- CAUTION: INPP5F has been initially described as an inositol
CC polyphosphate 5-phosphatase. {ECO:0000250|UniProtKB:Q9Y2H2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28723.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK129249; BAC98059.1; -; mRNA.
DR EMBL; AK030870; BAC27166.1; -; mRNA.
DR EMBL; AK034482; BAC28723.1; ALT_FRAME; mRNA.
DR EMBL; AK047166; BAC32978.1; -; mRNA.
DR EMBL; AK150418; BAE29542.1; -; mRNA.
DR EMBL; BC067200; AAH67200.1; -; mRNA.
DR EMBL; BC125437; AAI25438.1; -; mRNA.
DR CCDS; CCDS21899.1; -. [Q8CDA1-1]
DR CCDS; CCDS85430.1; -. [Q8CDA1-2]
DR RefSeq; NP_001333446.1; NM_001346517.1. [Q8CDA1-2]
DR RefSeq; NP_848756.2; NM_178641.5. [Q8CDA1-1]
DR AlphaFoldDB; Q8CDA1; -.
DR SMR; Q8CDA1; -.
DR STRING; 10090.ENSMUSP00000045910; -.
DR iPTMnet; Q8CDA1; -.
DR PhosphoSitePlus; Q8CDA1; -.
DR EPD; Q8CDA1; -.
DR jPOST; Q8CDA1; -.
DR MaxQB; Q8CDA1; -.
DR PaxDb; Q8CDA1; -.
DR PeptideAtlas; Q8CDA1; -.
DR PRIDE; Q8CDA1; -.
DR ProteomicsDB; 260812; -. [Q8CDA1-1]
DR ProteomicsDB; 260813; -. [Q8CDA1-2]
DR ProteomicsDB; 260814; -. [Q8CDA1-3]
DR ProteomicsDB; 260815; -. [Q8CDA1-4]
DR Antibodypedia; 32161; 99 antibodies from 18 providers.
DR DNASU; 101490; -.
DR Ensembl; ENSMUST00000043138; ENSMUSP00000045910; ENSMUSG00000042105. [Q8CDA1-1]
DR Ensembl; ENSMUST00000118605; ENSMUSP00000113700; ENSMUSG00000042105. [Q8CDA1-2]
DR Ensembl; ENSMUST00000151237; ENSMUSP00000146197; ENSMUSG00000042105. [Q8CDA1-3]
DR GeneID; 101490; -.
DR KEGG; mmu:101490; -.
DR UCSC; uc009jzc.1; mouse. [Q8CDA1-1]
DR UCSC; uc009jzf.1; mouse. [Q8CDA1-3]
DR UCSC; uc009jzg.1; mouse. [Q8CDA1-2]
DR CTD; 22876; -.
DR MGI; MGI:2141867; Inpp5f.
DR VEuPathDB; HostDB:ENSMUSG00000042105; -.
DR eggNOG; KOG1890; Eukaryota.
DR GeneTree; ENSGT00940000155996; -.
DR HOGENOM; CLU_044255_0_0_1; -.
DR InParanoid; Q8CDA1; -.
DR OMA; CWRDKQG; -.
DR PhylomeDB; Q8CDA1; -.
DR TreeFam; TF313543; -.
DR BRENDA; 3.1.3.25; 3474.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR BioGRID-ORCS; 101490; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Inpp5f; mouse.
DR PRO; PR:Q8CDA1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CDA1; protein.
DR Bgee; ENSMUSG00000042105; Expressed in cortical plate and 230 other tissues.
DR ExpressionAtlas; Q8CDA1; baseline and differential.
DR Genevisible; Q8CDA1; MM.
DR GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0034596; F:phosphatidylinositol phosphate 4-phosphatase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; IEA:Ensembl.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:ParkinsonsUK-UCL.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:ParkinsonsUK-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IMP:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:MGI.
DR InterPro; IPR034753; hSac2.
DR InterPro; IPR022158; Inositol_phosphatase.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF12456; hSac2; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS51791; HSAC2; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Endosome; Hydrolase; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1132
FT /note="Phosphatidylinositide phosphatase SAC2"
FT /id="PRO_0000331622"
FT DOMAIN 167..518
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 593..760
FT /note="hSac2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01127"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..691
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033270"
FT VAR_SEQ 1..627
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033271"
FT VAR_SEQ 373..414
FT /note="VIVNLVDQAGREKIIGDAYLKQVLLFNNPKLTYVSFDFHEHC -> RIWVWS
FT QHPLTQREEKRREEKRREEKRREEKRREEKRREEVT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033272"
FT VAR_SEQ 415..1132
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033273"
FT VAR_SEQ 628..629
FT /note="PS -> MH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033274"
FT MUTAGEN 460
FT /note="D->A: Has a diffuse cytosolic localization."
FT /evidence="ECO:0000269|PubMed:25869668"
FT MUTAGEN 460
FT /note="D->N: Loss of inositol 4-phosphatase activity. No
FT effect on subcellular localization. No effect on
FT interaction with OCRL, INPP5B and IPP4A."
FT /evidence="ECO:0000269|PubMed:25869668"
FT CONFLICT 728
FT /note="E -> D (in Ref. 3; AAH67200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 127608 MW; 4EDEA936E95D486C CRC64;
MELFQAKDHY ILQQGERALW CSRRDGGLQL RPATDLLLAW NPICLGLVEG VIGKIQLHSD
LPWWLILIRQ KALVGKLPGD HEVCKVTKIA VLSLSEMEPQ ELELELCKKH HFGINKPEKI
IPSPDDSKFL LKTFTNIKSN VSAPNKKKVK ESKEKEKLER RLLEELLKMF MDSESFYYSL
TYDLTNSVQR QSTGERDGRP LWQKVDDRFF WNKYMIQALT EIGTPDVDFW IIPIIQGFVQ
IEELVVNYNE SSDDDKSSPE TPPQDSTCVD DIHPRFLVAL ISRRSRHRAG MRYKRRGVDK
NGNVANYVET EQLIHVHHHT LSFIQTRGSV PVFWSQVGYR YNPRPRLDKS EKETVDCFCA
HFEEQLKIYK KQVIVNLVDQ AGREKIIGDA YLKQVLLFNN PKLTYVSFDF HEHCRGMKFE
NVQTLTDAIH DIIIDMKWCW VDQAGVICKQ EGIFRVNCMD CLDRTNVVQA AIARVVMEQQ
LKKLGVMPPE QPLPVKCNRT YQIMWANNGD SISRQYAGTA ALKGDFTRTG ERKLAGVMKD
GVNSANRYYL SRFKDAYRQA VIDLMQGVPV TEDLYSIFTK EKEHEALHKE SQRSHQELIS
QLLQSYMQLL LPGDEKFHGG WALVDCDPSL TDAAHRDVEV LLLLSNAAYY VAYYDDEVDK
VNQYQRLGLE DLERIEIGPE PTLFGKPKFS CMRLHYRCKE AGGYFHTLRA VPRSPEEDGK
DTLQCIAEML QITKQAMGLD VPIIEKKLER KSSKPHEDII GIRSQNQGSL AQGKSFLMSK
FSSLNQKVKQ TKSNVNIGNL RKLGNFTKPE MKVNFLKPNL KVNLWKSDSS LETMENPGVM
GNKVQGESDG DISSDNDSYH SDEFLTNSKS EEDKQLANSL ESVGPIDYIL PSCGIIVSAP
RLGSRSQSAS SIDVSTHAPS EAAAGPGSEL GKGLESPLKK SPSADSIHTR TGFTKPMDVY
CQRFVQDAQN KMNDLSEIRS VAQKSEEGSH KTNRVSNEET QSEPMGQTPP RPSQLNVSCS
VAGPPFLSVE PVHSVLSQKT PSSGSSLLEL EAGLCVTPSS ESSSSRAVSP FAKIRSSMVQ
VANITQAGLT HGINLAVAKV QKSPAEPEAV NEIQQNELKN MFTQCQTRII QI
