ID P3C2B_HUMAN Reviewed; 1634 AA. AC O00750; O95666; Q5SW99; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta; DE Short=PI3K-C2-beta; DE Short=PtdIns-3-kinase C2 subunit beta; DE EC=2.7.1.137 {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063}; DE EC=2.7.1.154 {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; DE AltName: Full=C2-PI3K; DE AltName: Full=Phosphoinositide 3-kinase-C2-beta; GN Name=PIK3C2B; 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], AND TISSUE SPECIFICITY. RC TISSUE=Mammary gland; RX PubMed=9144573; DOI=10.1006/bbrc.1997.6495; RA Brown R.A., Ho L.K.F., Weber-Hall S.J., Shipley J.M., Fry M.J.; RT "Identification and cDNA cloning of a novel mammalian C2 domain-containing RT phosphoinositide 3-kinase, HsC2-PI3K."; RL Biochem. Biophys. Res. Commun. 233:537-544(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND COFACTOR. RC TISSUE=Monocyte; RX PubMed=9830063; DOI=10.1074/jbc.273.49.33082; RA Arcaro A., Volinia S., Zvelebil M.J., Stein R.C., Watton S.J., Layton M.J., RA Gout I., Ahmadi K., Downward J., Waterfield M.D.; RT "Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2 RT domain in enzyme activity."; RL J. Biol. Chem. 273:33082-33090(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 [4] RP IDENTIFICATION IN A COMPLEX WITH ERBB2 AND EGFR, INTERACTION WITH EGFR AND RP PDGFR, COFACTOR, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10805725; DOI=10.1128/mcb.20.11.3817-3830.2000; RA Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., RA Domin J.; RT "Class II phosphoinositide 3-kinases are downstream targets of activated RT polypeptide growth factor receptors."; RL Mol. Cell. Biol. 20:3817-3830(2000). RN [5] RP IDENTIFICATION IN A COMPLEX WITH GRB2 AND EGFR, INTERACTION WITH GRB2, RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11533253; DOI=10.1128/mcb.21.19.6660-6667.2001; RA Wheeler M., Domin J.; RT "Recruitment of the class II phosphoinositide 3-kinase C2beta to the RT epidermal growth factor receptor: role of Grb2."; RL Mol. Cell. Biol. 21:6660-6667(2001). RN [6] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=14563213; DOI=10.1186/1472-6890-3-4; RA El Sheikh S.S., Domin J., Tomtitchong P., Abel P., Stamp G., Lalani E.-N.; RT "Topographical expression of class IA and class II phosphoinositide 3- RT kinase enzymes in normal human tissues is consistent with a role in RT differentiation."; RL BMC Clin. Pathol. 3:4-4(2003). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). CC -!- FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for CC PtdIns (PubMed:10805725, PubMed:9830063, PubMed:11533253). Does not CC phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF CC and PDGF signaling cascades (PubMed:10805725). CC {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, CC ECO:0000269|PubMed:9830063}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4- CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; CC Evidence={ECO:0000305|PubMed:9830063}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; CC EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10805725, CC ECO:0000269|PubMed:11533253, ECO:0000269|PubMed:9830063}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; CC Evidence={ECO:0000305|PubMed:9830063}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10805725}; CC -!- ACTIVITY REGULATION: Activated by GRB2. {ECO:0000269|PubMed:11533253}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=120 uM for ATP-Mg(2+) {ECO:0000269|PubMed:9830063}; CC KM=120 uM for ATP-Ca(2+) {ECO:0000269|PubMed:9830063}; CC Vmax=737 nmol/min/mg enzyme for ATP-Mg(2+) CC {ECO:0000269|PubMed:9830063}; CC Vmax=737 nmol/min/mg enzyme for ATP-Ca(2+) CC {ECO:0000269|PubMed:9830063}; CC -!- SUBUNIT: Part of a complex with ERBB2 and EGFR. Part of a complex with CC phosphorylated EGFR and GRB2. Interacts with phosphorylated EGFR and CC PDGFR, maybe indirectly. Interacts with GRB2. CC {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253}. CC -!- INTERACTION: CC O00750; P00533: EGFR; NbExp=10; IntAct=EBI-641107, EBI-297353; CC O00750; P04626: ERBB2; NbExp=2; IntAct=EBI-641107, EBI-641062; CC O00750; P62993: GRB2; NbExp=5; IntAct=EBI-641107, EBI-401755; CC O00750; P16333: NCK1; NbExp=3; IntAct=EBI-641107, EBI-389883; CC O00750; P31947: SFN; NbExp=4; IntAct=EBI-641107, EBI-476295; CC O00750; P14373: TRIM27; NbExp=5; IntAct=EBI-641107, EBI-719493; CC O00750; P63104: YWHAZ; NbExp=3; IntAct=EBI-641107, EBI-347088; CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:14563213, CC ECO:0000269|PubMed:9830063}. Cell membrane CC {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. CC Nucleus {ECO:0000269|PubMed:14563213}. Endoplasmic reticulum CC {ECO:0000269|PubMed:14563213}. Note=Found mostly in the microsome, but CC also in the plasma membrane and cytosol. Nuclear in testis. CC -!- TISSUE SPECIFICITY: Expressed in columnar and transitional epithelia, CC mononuclear cells, and ganglion cells (at protein level). Widely CC expressed, with highest levels in thymus and placenta and lowest in CC peripheral blood, skeletal muscle and kidney. CC {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9144573}. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE- CC ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA74194.1; Type=Erroneous initiation; 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; Y11312; CAA72168.1; -; mRNA. DR EMBL; Y13892; CAA74194.1; ALT_INIT; mRNA. DR EMBL; AL606489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS1446.1; -. DR PIR; JC5500; JC5500. DR PIR; PC4346; PC4346. DR RefSeq; NP_002637.3; NM_002646.3. DR RefSeq; XP_005245314.1; XM_005245257.2. DR RefSeq; XP_011507932.1; XM_011509630.2. DR RefSeq; XP_011507933.1; XM_011509631.2. DR RefSeq; XP_016856962.1; XM_017001473.1. DR RefSeq; XP_016856963.1; XM_017001474.1. DR AlphaFoldDB; O00750; -. DR SMR; O00750; -. DR BioGRID; 111305; 48. DR CORUM; O00750; -. DR IntAct; O00750; 30. DR MINT; O00750; -. DR STRING; 9606.ENSP00000356155; -. DR BindingDB; O00750; -. DR ChEMBL; CHEMBL5554; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; O00750; -. DR GuidetoPHARMACOLOGY; 2151; -. DR SwissLipids; SLP:000000893; -. DR CarbonylDB; O00750; -. DR iPTMnet; O00750; -. DR PhosphoSitePlus; O00750; -. DR BioMuta; PIK3C2B; -. DR CPTAC; non-CPTAC-5672; -. DR CPTAC; non-CPTAC-5673; -. DR EPD; O00750; -. DR jPOST; O00750; -. DR MassIVE; O00750; -. DR MaxQB; O00750; -. DR PaxDb; 9606-ENSP00000356155; -. DR PeptideAtlas; O00750; -. DR ProteomicsDB; 48017; -. DR Pumba; O00750; -. DR Antibodypedia; 34558; 250 antibodies from 30 providers. DR DNASU; 5287; -. DR Ensembl; ENST00000367187.7; ENSP00000356155.3; ENSG00000133056.14. DR Ensembl; ENST00000684373.1; ENSP00000507222.1; ENSG00000133056.14. DR GeneID; 5287; -. DR KEGG; hsa:5287; -. DR MANE-Select; ENST00000684373.1; ENSP00000507222.1; NM_001377334.1; NP_001364263.1. DR UCSC; uc001haw.4; human. DR AGR; HGNC:8972; -. DR CTD; 5287; -. DR DisGeNET; 5287; -. DR GeneCards; PIK3C2B; -. DR HGNC; HGNC:8972; PIK3C2B. DR HPA; ENSG00000133056; Low tissue specificity. DR MIM; 602838; gene. DR neXtProt; NX_O00750; -. DR OpenTargets; ENSG00000133056; -. DR PharmGKB; PA33305; -. DR VEuPathDB; HostDB:ENSG00000133056; -. DR eggNOG; KOG0905; Eukaryota. DR GeneTree; ENSGT00940000158263; -. DR HOGENOM; CLU_002191_0_0_1; -. DR InParanoid; O00750; -. DR OMA; QMAAGFR; -. DR OrthoDB; 10350at2759; -. DR PhylomeDB; O00750; -. DR TreeFam; TF102031; -. DR BioCyc; MetaCyc:HS05725-MONOMER; -. DR BRENDA; 2.7.1.137; 2681. DR BRENDA; 2.7.1.154; 2681. DR PathwayCommons; O00750; -. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR SignaLink; O00750; -. DR SIGNOR; O00750; -. DR BioGRID-ORCS; 5287; 16 hits in 1159 CRISPR screens. DR ChiTaRS; PIK3C2B; human. DR GeneWiki; PIK3C2B; -. DR GenomeRNAi; 5287; -. DR Pharos; O00750; Tchem. DR PRO; PR:O00750; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O00750; Protein. DR Bgee; ENSG00000133056; Expressed in pancreatic ductal cell and 209 other cell types or tissues. DR ExpressionAtlas; O00750; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:UniProtKB. DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:1905037; P:autophagosome organization; IEA:Ensembl. DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central. DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd04012; C2A_PI3K_class_II; 1. DR CDD; cd08381; C2B_PI3K_class_II; 1. DR CDD; cd00869; PI3Ka_II; 1. DR CDD; cd00895; PI3Kc_C2_beta; 1. DR CDD; cd07290; PX_PI3K_C2_beta; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000403; PI3/4_kinase_cat_dom. DR InterPro; IPR036940; PI3/4_kinase_cat_sf. DR InterPro; IPR018936; PI3/4_kinase_CS. DR InterPro; IPR002420; PI3K-type_C2_dom. DR InterPro; IPR001263; PI3K_accessory_dom. DR InterPro; IPR042236; PI3K_accessory_sf. DR InterPro; IPR000341; PI3K_Ras-bd_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR042134; PX_PI3K_C2_beta. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 1. DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF00792; PI3K_C2; 1. DR Pfam; PF00794; PI3K_rbd; 1. DR Pfam; PF00613; PI3Ka; 1. DR Pfam; PF00787; PX; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00142; PI3K_C2; 1. DR SMART; SM00144; PI3K_rbd; 1. DR SMART; SM00145; PI3Ka; 1. DR SMART; SM00146; PI3Kc; 1. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF64268; PX domain; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS51547; C2_PI3K; 1. DR PROSITE; PS00915; PI3_4_KINASE_1; 1. DR PROSITE; PS00916; PI3_4_KINASE_2; 1. DR PROSITE; PS50290; PI3_4_KINASE_3; 1. DR PROSITE; PS51546; PI3K_RBD; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. DR PROSITE; PS50195; PX; 1. DR Genevisible; O00750; HS. PE 1: Evidence at protein level; KW ATP-binding; Cell membrane; Cytoplasm; Endoplasmic reticulum; Kinase; KW Lipid metabolism; Membrane; Microsome; Nucleotide-binding; Nucleus; KW Reference proteome; Transferase. FT CHAIN 1..1634 FT /note="Phosphatidylinositol 4-phosphate 3-kinase C2 domain- FT containing subunit beta" FT /id="PRO_0000088798" FT DOMAIN 375..463 FT /note="PI3K-RBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879" FT DOMAIN 635..786 FT /note="C2 PI3K-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041, FT ECO:0000255|PROSITE-ProRule:PRU00880" FT DOMAIN 805..981 FT /note="PIK helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878" FT DOMAIN 1050..1328 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT DOMAIN 1365..1481 FT /note="PX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147" FT DOMAIN 1504..1624 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 2..298 FT /note="Interaction with GRB2" FT /evidence="ECO:0000269|PubMed:11533253" FT REGION 45..188 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 259..315 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1056..1062 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 1192..1200 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 1211..1237 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT COMPBIAS 87..115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 154..176 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 6 FT /note="G -> D (in Ref. 1; CAA72168)" FT /evidence="ECO:0000305" FT CONFLICT 63 FT /note="P -> S (in Ref. 2; CAA74194)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="R -> W (in Ref. 2; CAA74194)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="Q -> L (in Ref. 2; CAA74194)" FT /evidence="ECO:0000305" FT CONFLICT 246 FT /note="A -> V (in Ref. 1; CAA72168)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="K -> E (in Ref. 2; CAA74194)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="P -> S (in Ref. 2; CAA74194)" FT /evidence="ECO:0000305" FT CONFLICT 664..665 FT /note="EL -> DM (in Ref. 1; CAA72168)" FT /evidence="ECO:0000305" SQ SEQUENCE 1634 AA; 184768 MW; CA817BA77C12E833 CRC64; MSSTQGNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEENRAK QNADPSLISW DEPGVDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSLSPQE GPPNHSTSQG PQPGSDPWPK GSLSGDYLYI FDGSDGGVSS SPGPGDIEGS CKKLSPPPLP PRASIWDTPP LPPRKGSPSS SKISQPSDIN TFSLVEQLPG KLLEHRILEE EEVLGGGGQG RLLGSVDYDG INDAITRLNL KSTYDAEMLR DATRGWKEGR GPLDFSKDTS GKPVARSKTM PPQVPPRTYA SRYGNRKNAT PGKNRRISAA PVGSRPHTVA NGHELFEVSE ERDEEVAAFC HMLDILRSGS DIQDYFLTGY VWSAVTPSPE HLGDEVNLKV TVLCDRLQEA LTFTCNCSST VDLLIYQTLC YTHDDLRNVD VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC RKFDIDIRLQ LMEQKVVRSD LARTVNDDQS PSTLNYLVHL QERPVKQTIS RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC NALAAVETPE ITSALNQLPP CPSRMQPKIQ KDPSVLAVRE NREKVVEALT AAILDLVELY CNTFNADFQT AVPGSRKHDL VQEACHFARS LAFTVYATHR IPIIWATSYE DFYLSCSLSH GGKELCSPLQ TRRAHFSKYL FHLIVWDQQI CFPVQVNRLP RETLLCATLY ALPIPPPGSS SEANKQRRVP EALGWVTTPL FNFRQVLTCG RKLLGLWPAT QENPSARWSA PNFHQPDSVI LQIDFPTSAF DIKFTSPPGD KFSPRYEFGS LREEDQRKLK DIMQKESLYW LTDADKKRLW EKRYYCHSEV SSLPLVLASA PSWEWACLPD IYVLLKQWTH MNHQDALGLL HATFPDQEVR RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV THYFFWLLKD GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNAL AKLAQQVREA APSARQGILR TGLEEVKQFF ALNGSCRLPL SPSLLVKGIV PRDCSYFNSN AVPLKLSFQN VDPLGENIRV IFKCGDDLRQ DMLTLQMIRI MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNAETLRK IQVEHGVTGS FKDRPLADWL QKHNPGEDEY EKAVENFIYS CAGCCVATYV LGICDRHNDN IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP SSRFHDFVDL CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY DALRPQDTEA NATTYFTRLI ESSLGSVATK LNFFIHNLAQ MKFTGSDDRL TLSFASRTHT LKSSGRISDV FLCRHEKIFH PNKGYIYVVK VMRENTHEAT YIQRTFEEFQ ELHNKLRLLF PSSHLPSFPS RFVIGRSRGE AVAERRREEL NGYIWHLIHA PPEVAECDLV YTFFHPLPRD EKAMGTSPAP KSSDGTWARP VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP QKTTKRKTKV ARKTCNPTYN EMLVYDGIPK GDLQQRELQL SVLSEQGFWE NVLLGEVNIR LRELDLAQEK TGWFALGSRS HGTL //