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Serine/threonine-protein kinase D3 (EC 2.7.11.13) (Protein kinase C nu type) (Protein kinase EPK2) (nPKC-nu)

 KPCD3_HUMAN             Reviewed;         890 AA.
O94806; D6W587; Q53TR7; Q8NEL8;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 169.
RecName: Full=Serine/threonine-protein kinase D3;
EC=2.7.11.13;
AltName: Full=Protein kinase C nu type;
AltName: Full=Protein kinase EPK2;
AltName: Full=nPKC-nu;
Name=PRKD3; Synonyms=EPK2, PRKCN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=10231560; DOI=10.1016/S0167-4889(99)00040-3;
Hayashi A., Seki N., Hattori A., Kozuma S., Saito T.;
"PKCnu, a new member of the protein kinase C family, composes a fourth
subfamily with PKCmu.";
Biochim. Biophys. Acta 1450:99-106(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
THR-128 AND ARG-546.
TISSUE=Testis;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
ENZYME REGULATION, SUBCELLULAR LOCATION, PHORBOL-ESTER BINDING, AND
MUTAGENESIS OF THR-156; TYR-158; PRO-165; THR-166; TYR-170; PRO-282
AND LYS-293.
PubMed=18076381; DOI=10.1042/BJ20071334;
Chen J., Deng F., Li J., Wang Q.J.;
"Selective binding of phorbol esters and diacylglycerol by individual
C1 domains of the PKD family.";
Biochem. J. 411:333-342(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-27; SER-37;
SER-41; SER-213; SER-216; SER-364 AND THR-535, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND
SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213;
SER-216; SER-364 AND THR-535, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41 AND SER-44,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44 AND SER-364,
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).
[14]
STRUCTURE BY NMR OF 414-532.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PH domain of protein kinase C, nu type from
human.";
Submitted (JAN-2007) to the PDB data bank.
[15]
VARIANT [LARGE SCALE ANALYSIS] MET-716.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
prolonged physiological effects, downstream of PKC. Involved in
resistance to oxidative stress (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester
with high affinity and mediate translocation to the cell membrane.
Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by
PKC relieves auto-inhibition by the PH domain.
{ECO:0000269|PubMed:18076381}.
-!- INTERACTION:
P63027:VAMP2; NbExp=7; IntAct=EBI-1255366, EBI-520113;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18076381}.
Membrane {ECO:0000269|PubMed:18076381}. Note=Translocation to the
cell membrane is required for kinase activation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O94806-1; Sequence=Displayed;
Name=2;
IsoId=O94806-2; Sequence=VSP_029405, VSP_029406;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. PKD subfamily. {ECO:0000305}.
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EMBL; AB015982; BAA36514.1; -; mRNA.
EMBL; AC007390; AAY14817.1; -; Genomic_DNA.
EMBL; CH471053; EAX00398.1; -; Genomic_DNA.
EMBL; CH471053; EAX00399.1; -; Genomic_DNA.
EMBL; BC030706; AAH30706.1; -; mRNA.
CCDS; CCDS1789.1; -. [O94806-1]
RefSeq; NP_005804.1; NM_005813.4. [O94806-1]
RefSeq; XP_005264294.1; XM_005264237.3. [O94806-1]
UniGene; Hs.660757; -.
UniGene; Hs.716034; -.
PDB; 2D9Z; NMR; -; A=417-532.
PDBsum; 2D9Z; -.
ProteinModelPortal; O94806; -.
SMR; O94806; -.
BioGrid; 117199; 10.
IntAct; O94806; 13.
MINT; MINT-5003932; -.
STRING; 9606.ENSP00000234179; -.
BindingDB; O94806; -.
ChEMBL; CHEMBL2595; -.
GuidetoPHARMACOLOGY; 2174; -.
iPTMnet; O94806; -.
PhosphoSitePlus; O94806; -.
BioMuta; PRKD3; -.
EPD; O94806; -.
MaxQB; O94806; -.
PaxDb; O94806; -.
PeptideAtlas; O94806; -.
PRIDE; O94806; -.
DNASU; 23683; -.
Ensembl; ENST00000234179; ENSP00000234179; ENSG00000115825. [O94806-1]
Ensembl; ENST00000379066; ENSP00000368356; ENSG00000115825. [O94806-1]
GeneID; 23683; -.
KEGG; hsa:23683; -.
UCSC; uc002rqd.4; human. [O94806-1]
CTD; 23683; -.
DisGeNET; 23683; -.
EuPathDB; HostDB:ENSG00000115825.9; -.
GeneCards; PRKD3; -.
H-InvDB; HIX0030377; -.
HGNC; HGNC:9408; PRKD3.
HPA; HPA029529; -.
MIM; 607077; gene.
neXtProt; NX_O94806; -.
OpenTargets; ENSG00000115825; -.
PharmGKB; PA33772; -.
eggNOG; KOG4236; Eukaryota.
eggNOG; ENOG410XQZ3; LUCA.
GeneTree; ENSGT00840000129794; -.
HOGENOM; HOG000015135; -.
HOVERGEN; HBG003564; -.
InParanoid; O94806; -.
KO; K06070; -.
OMA; GRPTICQ; -.
OrthoDB; EOG091G02RG; -.
PhylomeDB; O94806; -.
TreeFam; TF314320; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
SignaLink; O94806; -.
SIGNOR; O94806; -.
ChiTaRS; PRKD3; human.
EvolutionaryTrace; O94806; -.
GeneWiki; PRKD3; -.
GenomeRNAi; 23683; -.
PRO; PR:O94806; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115825; -.
CleanEx; HS_PRKD3; -.
ExpressionAtlas; O94806; baseline and differential.
Genevisible; O94806; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:CACAO.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
CDD; cd00029; C1; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015727; Protein_Kinase_C_mu-related.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22968; PTHR22968; 1.
Pfam; PF00130; C1_1; 2.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 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; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Serine/threonine-protein kinase; Transferase; Zinc;
Zinc-finger.
CHAIN 1 890 Serine/threonine-protein kinase D3.
/FTId=PRO_0000055717.
DOMAIN 416 532 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 576 832 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 154 204 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 271 321 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 582 590 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 699 699 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 605 605 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 426 426 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 457 457 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 535 535 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K1Y2}.
MOD_RES 731 731 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q15139}.
MOD_RES 735 735 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q15139}.
VAR_SEQ 595 611 HRKTGRDVAIKVIDKMR -> QLQPFAYCTHYFKNWKM
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029405.
VAR_SEQ 612 890 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029406.
VARIANT 42 42 N -> D (in dbSNP:rs11896614).
/FTId=VAR_037147.
VARIANT 128 128 A -> T (in dbSNP:rs17852819).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037148.
VARIANT 225 225 P -> S (in dbSNP:rs34280934).
/FTId=VAR_050561.
VARIANT 445 445 L -> I (in dbSNP:rs55912911).
/FTId=VAR_061532.
VARIANT 546 546 Q -> R (in dbSNP:rs17856887).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_037149.
VARIANT 716 716 V -> M (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042336.
MUTAGEN 156 156 T->A: Slight loss in ability to bind DAG
and phorbol-ester; when associated with
F-158. {ECO:0000269|PubMed:18076381}.
MUTAGEN 158 158 Y->F: Slight loss in ability to bind DAG
and phorbol-ester; when associated with
A-156. {ECO:0000269|PubMed:18076381}.
MUTAGEN 165 165 P->G: No effect on ability to bind
phorbol ester, loss of ability to bind
DAG, reduced DAG-induced membrane
translocation.
{ECO:0000269|PubMed:18076381}.
MUTAGEN 166 166 T->A: Slight loss in ability to bind DAG
and phorbol-ester.
{ECO:0000269|PubMed:18076381}.
MUTAGEN 170 170 Y->F: Slight loss in ability to bind DAG
and phorbol-ester.
{ECO:0000269|PubMed:18076381}.
MUTAGEN 282 282 P->G: No effect on ability to bind
phorbol ester, increase in ability to
bind DAG. {ECO:0000269|PubMed:18076381}.
MUTAGEN 284 284 I->V: Slight increase in ability to bind
DAG, no effect on phorbol-ester binding.
MUTAGEN 293 293 K->W: Increased ability to bind DAG, no
effect on phorbol-ester binding.
{ECO:0000269|PubMed:18076381}.
STRAND 417 429 {ECO:0000244|PDB:2D9Z}.
STRAND 434 443 {ECO:0000244|PDB:2D9Z}.
STRAND 445 449 {ECO:0000244|PDB:2D9Z}.
TURN 462 464 {ECO:0000244|PDB:2D9Z}.
STRAND 477 479 {ECO:0000244|PDB:2D9Z}.
STRAND 485 489 {ECO:0000244|PDB:2D9Z}.
STRAND 494 497 {ECO:0000244|PDB:2D9Z}.
TURN 508 514 {ECO:0000244|PDB:2D9Z}.
HELIX 517 532 {ECO:0000244|PDB:2D9Z}.
SEQUENCE 890 AA; 100471 MW; 66D5E7E7235064F5 CRC64;
MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES
HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT
EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG
SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV
CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV VMEKLHGDML
EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL KPENVLLASA EPFPQVKLCD
FGFARIIGEK SFRRSVVGTP AYLAPEVLRS KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE
DINDQIQNAA FMYPPNPWRE ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD
LREFETRIGE RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP


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