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Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13)

 KPCA_RAT                Reviewed;         672 AA.
P05696;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 183.
RecName: Full=Protein kinase C alpha type;
Short=PKC-A;
Short=PKC-alpha;
EC=2.7.11.13;
Name=Prkca; Synonyms=Pkca;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3387228; DOI=10.1093/nar/16.11.5199;
Ono Y., Fujii T., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y.;
"Nucleotide sequences of cDNAs for alpha and gamma subspecies of rat
brain protein kinase C.";
Nucleic Acids Res. 16:5199-5200(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3666147; DOI=10.1016/0014-5793(87)80291-0;
Kikkawa U., Ogita K., Ono Y., Asaoka Y., Shearman M.S., Fujii T.,
Ase K., Sekiguchi K., Igarashi K., Nishizuka Y.;
"The common structure and activities of four subspecies of rat brain
protein kinase C family.";
FEBS Lett. 223:212-216(1987).
[3]
INTERACTION WITH CAVIN2.
PubMed=9566962; DOI=10.1083/jcb.141.3.601;
Mineo C., Ying Y.-S., Chapline C., Jaken S., Anderson R.G.W.;
"Targeting of protein kinase Calpha to caveolae.";
J. Cell Biol. 141:601-610(1998).
[4]
FUNCTION IN CELL CYCLE ARREST.
PubMed=11076962; DOI=10.1083/jcb.151.4.763;
Frey M.R., Clark J.A., Leontieva O., Uronis J.M., Black A.R.,
Black J.D.;
"Protein kinase C signaling mediates a program of cell cycle
withdrawal in the intestinal epithelium.";
J. Cell Biol. 151:763-778(2000).
[5]
FUNCTION IN CARDIAC HYPERTROPHY.
PubMed=11864993; DOI=10.1083/jcb.200108062;
Braz J.C., Bueno O.F., De Windt L.J., Molkentin J.D.;
"PKC alpha regulates the hypertrophic growth of cardiomyocytes through
extracellular signal-regulated kinase1/2 (ERK1/2).";
J. Cell Biol. 156:905-919(2002).
[6]
FUNCTION IN HEART FAILURE, AND SUBCELLULAR LOCATION.
PubMed=15271671; DOI=10.1152/ajpheart.00171.2004;
Vijayan K., Szotek E.L., Martin J.L., Samarel A.M.;
"Protein kinase C-alpha-induced hypertrophy of neonatal rat
ventricular myocytes.";
Am. J. Physiol. 287:H2777-H2789(2004).
[7]
REVIEW.
PubMed=3045562; DOI=10.1038/334661a0;
Nishizuka Y.;
"The molecular heterogeneity of protein kinase C and its implications
for cellular regulation.";
Nature 334:661-665(1988).
[8]
FUNCTION.
PubMed=19176525; DOI=10.1074/jbc.M808719200;
Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.;
"Phosphorylation of activation transcription factor-2 at serine 121 by
protein kinase c controls c-Jun-mediated activation of
transcription.";
J. Biol. Chem. 284:8567-8581(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-319 AND
THR-638, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 155-293 IN COMPLEX WITH
PHOSPHATIDYLSERINE AND CALCIUM.
PubMed=10562545; DOI=10.1093/emboj/18.22.6329;
Verdaguer N., Corbalan-Garcia S., Ochoa W.F., Fita I.,
Gomez-Fernandez J.C.;
"Ca(2+) bridges the C2 membrane-binding domain of protein kinase
Calpha directly to phosphatidylserine.";
EMBO J. 18:6329-6338(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 156-292 IN COMPLEX WITH
PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE AND CALCIUM, MUTAGENESIS OF
TYR-195; LYS-209; LYS-211 AND TRP-245, AND SUBCELLULAR LOCATION.
PubMed=19346474; DOI=10.1073/pnas.0813099106;
Guerrero-Valero M., Ferrer-Orta C., Querol-Audi J., Marin-Vicente C.,
Fita I., Gomez-Fernandez J.C., Verdaguer N., Corbalan-Garcia S.;
"Structural and mechanistic insights into the association of PKCalpha-
C2 domain to PtdIns(4,5)P2.";
Proc. Natl. Acad. Sci. U.S.A. 106:6603-6607(2009).
-!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that is involved
in positive and negative regulation of cell proliferation,
apoptosis, differentiation, migration and adhesion, cardiac
hypertrophy, angiogenesis, platelet function and inflammation, by
directly phosphorylating targets such as RAF1, BCL2, CSPG4,
TNNT2/CTNT, or activating signaling cascades involving MAPK1/3
(ERK1/2) and RAP1GAP. Depending on the cell type, is involved in
cell proliferation and cell growth arrest by positive and negative
regulation of the cell cycle. Can promote cell growth by
phosphorylating and activating RAF1, which mediates the activation
of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A,
which facilitates active cyclin-dependent kinase (CDK) complex
formation. In cells stimulated by the phorbol ester PMA, can
trigger a cell cycle arrest program which is associated with the
accumulation of the hyper-phosphorylated growth-suppressive form
of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B.
Depending on the cell type, exhibits anti-apoptotic function and
protects cells from apoptosis by suppressing the p53/TP53-mediated
activation of IGFBP3, or mediates anti-apoptotic action by
phosphorylating BCL2. During macrophage differentiation induced by
macrophage colony-stimulating factor (CSF1), is translocated to
the nucleus and is associated with macrophage development. After
wounding, translocates from focal contacts to lamellipodia and
participates in the modulation of desmosomal adhesion. Plays a
role in cell motility by phosphorylating CSPG4, which induces
association of CSPG4 with extensive lamellipodia at the cell
periphery and polarization of the cell accompanied by increases in
cell motility. During chemokine-induced CD4(+) T cell migration,
phosphorylates CDC42-guanine exchange factor DOCK8 resulting in
its dissociation from LRCH1 and the activation of GTPase CDC42 (By
similarity). Negatively regulates myocardial contractility and
positively regulates angiogenesis, platelet aggregation and
thrombus formation in arteries. Mediates hypertrophic growth of
neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-
dependent signaling pathway, and upon PMA treatment, is required
to induce cardiomyocyte hypertrophy up to heart failure and death,
by increasing protein synthesis, protein-DNA ratio and cell
surface area. Regulates cardiomyocyte function by phosphorylating
cardiac troponin T (TNNT2/CTNT), which induces significant
reduction in actomyosin ATPase activity, myofilament calcium
sensitivity and myocardial contractility. In angiogenesis, is
required for full endothelial cell migration, adhesion to
vitronectin (VTN), and vascular endothelial growth factor A
(VEGFA)-dependent regulation of kinase activation and vascular
tube formation. Involved in the stabilization of VEGFA mRNA at
post-transcriptional level and mediates VEGFA-induced cell
proliferation. In the regulation of calcium-induced platelet
aggregation, mediates signals from the CD36/GP4 receptor for
granule release, and activates the integrin heterodimer ITGA2B-
ITGB3 through the RAP1GAP pathway for adhesion. During response to
lipopolysaccharides (LPS), may regulate selective LPS-induced
macrophage functions involved in host defense and inflammation.
But in some inflammatory responses, may negatively regulate NF-
kappa-B-induced genes, through IL1A-dependent induction of NF-
kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-
tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1,
which modulates EIF4G1 binding to MKNK1 and may be involved in the
regulation of EIF4E phosphorylation. Phosphorylates KIT, leading
to inhibition of KIT activity. Phosphorylates ATF2 which promotes
cooperation between ATF2 and JUN, activating transcription.
{ECO:0000250|UniProtKB:P17252, ECO:0000269|PubMed:11076962,
ECO:0000269|PubMed:11864993, ECO:0000269|PubMed:15271671,
ECO:0000269|PubMed:19176525}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domain. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474};
-!- ENZYME REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB
and PRKCG) are activated by calcium and diacylglycerol (DAG) in
the presence of phosphatidylserine. Three specific sites; Thr-497
(activation loop of the kinase domain), Thr-638 (turn motif) and
Ser-657 (hydrophobic region), need to be phosphorylated for its
full activation.
-!- SUBUNIT: Interacts with ADAP1/CENTA1, CSPG4 and PRKCABP (By
similarity). Binds to CAVIN2 in the presence of phosphatidylserine
(PubMed:9566962). Interacts with PICK1 (via PDZ domain). Interacts
with TRIM41. Recruited in a circadian manner into a nuclear
complex which also includes BMAL1 and RACK1 (By similarity).
{ECO:0000250|UniProtKB:P17252, ECO:0000250|UniProtKB:P20444,
ECO:0000269|PubMed:9566962}.
-!- INTERACTION:
P34901:Sdc4; NbExp=3; IntAct=EBI-935801, EBI-1173182;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15271671}.
Cell membrane {ECO:0000269|PubMed:15271671,
ECO:0000269|PubMed:19346474}; Peripheral membrane protein
{ECO:0000305|PubMed:15271671}. Mitochondrion membrane
{ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P17252}. Nucleus
{ECO:0000269|PubMed:15271671}. Note=Translocated to the nucleus
upon treatment with PMA or IGF1. {ECO:0000269|PubMed:15271671}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; X07286; CAA30266.1; -; mRNA.
PIR; S02248; KIRTC.
UniGene; Rn.86669; -.
PDB; 1DSY; X-ray; 2.60 A; A=155-293.
PDB; 2NCE; NMR; -; A=155-293.
PDB; 3GPE; X-ray; 2.00 A; A=156-292.
PDB; 3RDJ; X-ray; 1.90 A; A=156-292.
PDB; 3TWY; X-ray; 1.50 A; A=156-292.
PDB; 4L1L; X-ray; 1.60 A; A=155-293.
PDBsum; 1DSY; -.
PDBsum; 2NCE; -.
PDBsum; 3GPE; -.
PDBsum; 3RDJ; -.
PDBsum; 3TWY; -.
PDBsum; 4L1L; -.
ProteinModelPortal; P05696; -.
SMR; P05696; -.
CORUM; P05696; -.
IntAct; P05696; 10.
MINT; MINT-86103; -.
STRING; 10116.ENSRNOP00000004699; -.
BindingDB; P05696; -.
ChEMBL; CHEMBL2855; -.
iPTMnet; P05696; -.
PhosphoSitePlus; P05696; -.
SwissPalm; P05696; -.
PaxDb; P05696; -.
PRIDE; P05696; -.
RGD; 3395; Prkca.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P05696; -.
PhylomeDB; P05696; -.
BRENDA; 2.7.11.13; 5301.
EvolutionaryTrace; P05696; -.
PRO; PR:P05696; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004698; F:calcium-dependent protein kinase C activity; IDA:RGD.
GO; GO:0004697; F:protein kinase C activity; IDA:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:RGD.
GO; GO:0045184; P:establishment of protein localization; TAS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0007611; P:learning or memory; IMP:RGD.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0045822; P:negative regulation of heart contraction; IMP:RGD.
GO; GO:0017148; P:negative regulation of translation; IMP:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:RGD.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISS:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:RGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IMP:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IMP:RGD.
GO; GO:0045471; P:response to ethanol; IMP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0000302; P:response to reactive oxygen species; IMP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
CDD; cd00029; C1; 2.
CDD; cd05615; STKc_cPKC_alpha; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR034663; cPKC_alpha.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014375; Protein_kinase_C_a/b/g.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000550; PKC_alpha; 1.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Angiogenesis; Apoptosis; ATP-binding;
Calcium; Cell adhesion; Cell membrane; Complete proteome; Cytoplasm;
Kinase; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P17252}.
CHAIN 2 672 Protein kinase C alpha type.
/FTId=PRO_0000055682.
DOMAIN 172 260 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 339 597 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 598 668 AGC-kinase C-terminal.
ZN_FING 36 86 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 101 151 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 345 353 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 463 463 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 186 186 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:10562545}.
METAL 187 187 Calcium 1. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 187 187 Calcium 2. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 193 193 Calcium 2. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 246 246 Calcium 1. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 246 246 Calcium 2. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 247 247 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 248 248 Calcium 1. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 248 248 Calcium 2. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 248 248 Calcium 3. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 252 252 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 254 254 Calcium 1. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
METAL 254 254 Calcium 3. {ECO:0000269|PubMed:10562545,
ECO:0000269|PubMed:19346474}.
BINDING 195 195 Inositol phosphate group.
{ECO:0000269|PubMed:19346474}.
BINDING 245 245 Inositol phosphate group.
{ECO:0000269|PubMed:19346474}.
BINDING 368 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 497 497 Phosphothreonine; by PDPK1.
{ECO:0000250}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 628 628 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 631 631 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P68403,
ECO:0000255}.
MOD_RES 638 638 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 658 658 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:P20444}.
MUTAGEN 195 195 Y->S: Reduced phosphatidylinositol 4,5-
bisphosphate recognition and impaired
membrane docking. Loss of
phosphatidylinositol 4,5-bisphosphate-
binding and strong decrease of membrane
docking; when associated with A-209; A-
211 and A-245.
{ECO:0000269|PubMed:19346474}.
MUTAGEN 209 209 K->A: Loss of phosphatidylinositol 4,5-
bisphosphate-binding and strong decrease
of membrane docking; when associated with
S-195; A-211 and A-245.
{ECO:0000269|PubMed:19346474}.
MUTAGEN 211 211 K->A: Loss of phosphatidylinositol 4,5-
bisphosphate-binding and strong decrease
of membrane docking; when associated with
S-195; A-209 and A-245.
{ECO:0000269|PubMed:19346474}.
MUTAGEN 245 245 W->A: Reduced phosphatidylinositol 4,5-
bisphosphate recognition and impaired
membrane docking. Loss of
phosphatidylinositol 4,5-bisphosphate-
binding and strong decrease of membrane
docking; when associated with S-195; A-
209 and A-211.
{ECO:0000269|PubMed:19346474}.
STRAND 161 169 {ECO:0000244|PDB:3TWY}.
STRAND 172 182 {ECO:0000244|PDB:3TWY}.
STRAND 194 201 {ECO:0000244|PDB:3TWY}.
STRAND 222 230 {ECO:0000244|PDB:3TWY}.
HELIX 233 237 {ECO:0000244|PDB:3TWY}.
STRAND 239 246 {ECO:0000244|PDB:3TWY}.
STRAND 249 251 {ECO:0000244|PDB:3TWY}.
STRAND 254 262 {ECO:0000244|PDB:3TWY}.
HELIX 263 268 {ECO:0000244|PDB:3TWY}.
STRAND 271 276 {ECO:0000244|PDB:3TWY}.
HELIX 280 283 {ECO:0000244|PDB:3TWY}.
STRAND 288 290 {ECO:0000244|PDB:1DSY}.
SEQUENCE 672 AA; 76792 MW; 94889E7339C17719 CRC64;
MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS
LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL
SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNVE
LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG
TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV
NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA
DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG
EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKHPAKR LGCGPEGERD VREHAFFRRI
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN
PQFVHPILQS AV


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