ID PI5PA_HUMAN Reviewed; 1006 AA. AC Q15735; B3KS54; Q32M61; Q6ZTH6; Q8N902; Q9UDT9; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 187. DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A; DE EC=3.1.3.36 {ECO:0000250|UniProtKB:Q9JMC1}; DE AltName: Full=Inositol polyphosphate 5-phosphatase J; DE AltName: Full=Phosphatidylinositol 1,3,4,5-tetrakisphosphate 5-phosphatase; DE EC=3.1.3.56 {ECO:0000250|UniProtKB:Q9JMC1}; DE AltName: Full=Phosphatidylinositol 1,4,5-trisphosphate 5-phosphatase; DE EC=3.1.3.56 {ECO:0000250|UniProtKB:Q9JMC1}; GN Name=INPP5J; Synonyms=PIB5PA, PIPP; 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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Cerebellum, Heart, and Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 610-1006. RC TISSUE=Brain; RA Nussbaum R.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-990, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Inositol 5-phosphatase, which converts inositol 1,4,5- CC trisphosphate to inositol 1,4-bisphosphate. Also converts CC phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4- CC phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4- CC trisphosphate in vitro. May be involved in modulation of the function CC of inositol and phosphatidylinositol polyphosphate-binding proteins CC that are present at membranes ruffles. {ECO:0000250|UniProtKB:Q9JMC1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, CC ChEBI:CHEBI:203600; EC=3.1.3.56; CC Evidence={ECO:0000250|UniProtKB:Q9JMC1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19798; CC Evidence={ECO:0000250|UniProtKB:Q9JMC1}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo- CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895, CC ChEBI:CHEBI:58414; EC=3.1.3.56; CC Evidence={ECO:0000250|UniProtKB:Q9JMC1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11393; CC Evidence={ECO:0000250|UniProtKB:Q9JMC1}; 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:0000250|UniProtKB:Q9JMC1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765; CC Evidence={ECO:0000250|UniProtKB:Q9JMC1}; CC -!- INTERACTION: CC Q15735; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10236940, EBI-396137; CC Q15735; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10236940, EBI-739624; CC Q15735; Q96EY1-2: DNAJA3; NbExp=3; IntAct=EBI-10236940, EBI-3952284; CC Q15735; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10236940, EBI-2349927; CC Q15735; Q12929: EPS8; NbExp=3; IntAct=EBI-10236940, EBI-375576; CC Q15735; P51116: FXR2; NbExp=3; IntAct=EBI-10236940, EBI-740459; CC Q15735; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10236940, EBI-618309; CC Q15735; O75031: HSF2BP; NbExp=3; IntAct=EBI-10236940, EBI-7116203; CC Q15735; P50221: MEOX1; NbExp=3; IntAct=EBI-10236940, EBI-2864512; CC Q15735; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10236940, EBI-16439278; CC Q15735; Q96FA3: PELI1; NbExp=3; IntAct=EBI-10236940, EBI-448369; CC Q15735; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10236940, EBI-79165; CC Q15735; P31321: PRKAR1B; NbExp=3; IntAct=EBI-10236940, EBI-2805516; CC Q15735; P61289: PSME3; NbExp=3; IntAct=EBI-10236940, EBI-355546; CC Q15735; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10236940, EBI-726876; CC Q15735; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10236940, EBI-11741437; CC Q15735; P14373: TRIM27; NbExp=3; IntAct=EBI-10236940, EBI-719493; CC Q15735; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-10236940, EBI-2130429; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Predominantly CC localized to membrane ruffles. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q15735-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15735-2; Sequence=VSP_007296; CC Name=3; CC IsoId=Q15735-3; Sequence=VSP_021017; CC -!- DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute CC binding sites for the 14-3-3 protein. CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase CC type II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD15618.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK092859; BAG52616.1; -; mRNA. DR EMBL; AK095944; BAC04657.1; -; mRNA. DR EMBL; AK126610; BAC86611.1; -; mRNA. DR EMBL; AC005005; AAD15618.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471095; EAW59936.1; -; Genomic_DNA. DR EMBL; BC109288; AAI09289.1; -; mRNA. DR EMBL; U45975; AAB03216.1; -; mRNA. DR CCDS; CCDS46687.1; -. [Q15735-3] DR CCDS; CCDS63453.1; -. [Q15735-1] DR CCDS; CCDS63455.1; -. [Q15735-2] DR RefSeq; NP_001002837.1; NM_001002837.2. [Q15735-3] DR RefSeq; NP_001271214.1; NM_001284285.1. [Q15735-1] DR RefSeq; NP_001271217.1; NM_001284288.1. [Q15735-2] DR RefSeq; NP_001271218.1; NM_001284289.1. [Q15735-2] DR RefSeq; XP_016884260.1; XM_017028771.1. DR AlphaFoldDB; Q15735; -. DR SMR; Q15735; -. DR BioGRID; 118015; 18. DR IntAct; Q15735; 18. DR STRING; 9606.ENSP00000333262; -. DR DEPOD; INPP5J; -. DR GlyCosmos; Q15735; 2 sites, 1 glycan. DR GlyGen; Q15735; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q15735; -. DR PhosphoSitePlus; Q15735; -. DR BioMuta; INPP5J; -. DR DMDM; 116242713; -. DR EPD; Q15735; -. DR jPOST; Q15735; -. DR MassIVE; Q15735; -. DR MaxQB; Q15735; -. DR PaxDb; 9606-ENSP00000333262; -. DR PeptideAtlas; Q15735; -. DR ProteomicsDB; 60724; -. [Q15735-1] DR ProteomicsDB; 60725; -. [Q15735-2] DR ProteomicsDB; 60726; -. [Q15735-3] DR Antibodypedia; 5745; 222 antibodies from 30 providers. DR DNASU; 27124; -. DR Ensembl; ENST00000331075.10; ENSP00000333262.5; ENSG00000185133.14. [Q15735-1] DR Ensembl; ENST00000400294.6; ENSP00000383150.2; ENSG00000185133.14. [Q15735-2] DR Ensembl; ENST00000404390.7; ENSP00000384534.3; ENSG00000185133.14. [Q15735-3] DR Ensembl; ENST00000405300.5; ENSP00000384596.1; ENSG00000185133.14. [Q15735-2] DR GeneID; 27124; -. DR KEGG; hsa:27124; -. DR MANE-Select; ENST00000331075.10; ENSP00000333262.5; NM_001284285.2; NP_001271214.1. DR UCSC; uc003ajs.5; human. [Q15735-1] DR AGR; HGNC:8956; -. DR CTD; 27124; -. DR DisGeNET; 27124; -. DR GeneCards; INPP5J; -. DR HGNC; HGNC:8956; INPP5J. DR HPA; ENSG00000185133; Tissue enhanced (parathyroid gland, thyroid gland). DR MIM; 606481; gene. DR neXtProt; NX_Q15735; -. DR OpenTargets; ENSG00000185133; -. DR PharmGKB; PA164720918; -. DR VEuPathDB; HostDB:ENSG00000185133; -. DR eggNOG; KOG0565; Eukaryota. DR GeneTree; ENSGT00940000156855; -. DR InParanoid; Q15735; -. DR OMA; NMAKSSW; -. DR OrthoDB; 21647at2759; -. DR PhylomeDB; Q15735; -. DR TreeFam; TF317034; -. DR BioCyc; MetaCyc:HS11950-MONOMER; -. DR BRENDA; 3.1.3.56; 2681. DR PathwayCommons; Q15735; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. 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 SignaLink; Q15735; -. DR BioGRID-ORCS; 27124; 10 hits in 1181 CRISPR screens. DR ChiTaRS; INPP5J; human. DR GeneWiki; PIB5PA; -. DR GenomeRNAi; 27124; -. DR Pharos; Q15735; Tbio. DR PRO; PR:Q15735; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q15735; Protein. DR Bgee; ENSG00000185133; Expressed in right lobe of thyroid gland and 107 other cell types or tissues. DR ExpressionAtlas; Q15735; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0001726; C:ruffle; IDA:MGI. DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome. DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IBA:GO_Central. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome. DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central. DR CDD; cd09094; INPP5c_INPP5J-like; 1. DR Gene3D; 2.60.40.2840; -; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR046985; IP5. DR InterPro; IPR000300; IPPc. DR InterPro; IPR041611; SKICH. DR PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1. DR PANTHER; PTHR11200:SF127; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 5-PHOSPHATASE A; 1. DR Pfam; PF17751; SKICH; 1. DR SMART; SM00128; IPPc; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR Genevisible; Q15735; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Hydrolase; Methylation; Phosphoprotein; KW Reference proteome; Repeat; SH3-binding. FT CHAIN 1..1006 FT /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase FT A" FT /id="PRO_0000209738" FT REGION 1..416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 425..728 FT /note="Catalytic" FT /evidence="ECO:0000255" FT REGION 729..840 FT /note="Required for ruffle localization" FT /evidence="ECO:0000250" FT REGION 844..1006 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 102..107 FT /note="RSXSXX motif 1" FT MOTIF 345..350 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT MOTIF 350..355 FT /note="RSXSXX motif 2" FT MOTIF 874..879 FT /note="RSXSXX motif 3" FT MOTIF 885..890 FT /note="RSXSXX motif 4" FT MOTIF 911..916 FT /note="RSXSXX motif 5" FT COMPBIAS 96..116 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 210..232 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 253..267 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 332..367 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 378..416 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..863 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 908..939 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 56 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 56 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 65 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 76 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 83 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 83 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 324 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59644" FT MOD_RES 903 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 990 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..367 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_007296" FT VAR_SEQ 56..423 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021017" FT VARIANT 333 FT /note="S -> I (in dbSNP:rs12485025)" FT /id="VAR_028107" FT CONFLICT 610..612 FT /note="SYD -> ARG (in Ref. 5)" FT /evidence="ECO:0000305" FT CONFLICT 662 FT /note="V -> A (in Ref. 1; BAC86611)" FT /evidence="ECO:0000305" FT CONFLICT 791 FT /note="W -> R (in Ref. 4; AAI09289)" FT /evidence="ECO:0000305" SQ SEQUENCE 1006 AA; 107197 MW; ADB6382AA33E15AC CRC64; MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL GPSEPRLALA PVGPRAAMSA SSEGPRLALA SPRPILAPLC TPEGQKTATA HRSSSLAPTS VGQLVMSASA GPKPPPATTG SVLAPTSLGL VMPASAGPRS PPVTLGPNLA PTSRDQKQEP PASVGPKPTL AASGLSLALA SEEQPPELPS TPSPVPSPVL SPTQEQALAP ASTASGAASV GQTSARKRDA PAPRPLPASE GHLQPPAQTS GPTGSPPCIQ TSPDPRLSPS FRARPEALHS SPEDPVLPRP PQTLPLDVGQ GPSEPGTHSP GLLSPTFRPG APSGQTVPPP LPKPPRSPSR SPSHSPNRSP CVPPAPDMAL PRLGTQSTGP GRCLSPNLQA QEAPAPVTTS SSTSTLSSSP WSAQPTWKSD PGFRITVVTW NVGTAMPPDD VTSLLHLGGG DDSDGADMIA IGLQEVNSML NKRLKDALFT DQWSELFMDA LGPFNFVLVS SVRMQGVILL LFAKYYHLPF LRDVQTDCTR TGLGGYWGNK GGVSVRLAAF GHMLCFLNCH LPAHMDKAEQ RKDNFQTILS LQQFQGPGAQ GILDHDLVFW FGDLNFRIES YDLHFVKFAI DSDQLHQLWE KDQLNMAKNT WPILKGFQEG PLNFAPTFKF DVGTNKYDTS AKKRKPAWTD RILWKVKAPG GGPSPSGRKS HRLQVTQHSY RSHMEYTVSD HKPVAAQFLL QFAFRDDMPL VRLEVADEWV RPEQAVVRYR METVFARSSW DWIGLYRVGF RHCKDYVAYV WAKHEDVDGN TYQVTFSEES LPKGHGDFIL GYYSHNHSIL IGITEPFQIS LPSSELASSS TDSSGTSSEG EDDSTLELLA PKSRSPSPGK SKRHRSRSPG LARFPGLALR PSSRERRGAS RSPSPQSRRL SRVAPDRSSN GSSRGSSEEG PSGLPGPWAF PPAVPRSLGL LPALRLETVD PGGGGSWGPD REALAPNSLS PSPQGHRGLE EGGLGP //