PLK4_HUMAN
ID PLK4_HUMAN Reviewed; 970 AA.
AC O00444; B2RAL0; B7Z837; B7Z8G7; Q8IYF0; Q96Q95; Q9UD84; Q9UDE2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000305};
DE EC=2.7.11.21 {ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942};
DE AltName: Full=Polo-like kinase 4;
DE Short=PLK-4;
DE AltName: Full=Serine/threonine-protein kinase 18;
DE AltName: Full=Serine/threonine-protein kinase Sak;
GN Name=PLK4 {ECO:0000312|HGNC:HGNC:11397}; Synonyms=SAK, STK18;
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] (ISOFORM 1), AND VARIANTS THR-232 AND ASP-830.
RC TISSUE=Lung;
RA Karn T., Holtrich U., Wolf G., Hock B., Strebhardt K.,
RA Ruebsamen-Waigmann H.;
RT "Human SAK related to the PLK/polo family of cell cycle kinases shows high
RT mRNA expression in testis.";
RL Oncol. Rep. 4:505-510(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY TEC, AND
RP VARIANTS THR-232 AND ASP-830.
RC TISSUE=Blood;
RX PubMed=11489907; DOI=10.1074/jbc.m106249200;
RA Yamashita Y., Kajigaya S., Yoshida K., Ueno S., Ota J., Ohmine K., Ueda M.,
RA Miyazato A., Ohya K., Kitamura T., Ozawa K., Mano H.;
RT "Sak serine-threonine kinase acts as an effector of Tec tyrosine kinase.";
RL J. Biol. Chem. 276:39012-39020(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP THR-232 AND ASP-830.
RC TISSUE=Testis, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 134-196.
RX PubMed=8260651; DOI=10.1006/smim.1993.1041;
RA Mills G.B., Schmandt R., Gibson S., Leung B., Hill M., May C., Shi Y.F.,
RA Branch D.R., Radvanyi L., Truitt K.E., Imboden J.;
RT "Transmembrane signaling by the interleukin-2 receptor: progress and
RT conundrums.";
RL Semin. Immunol. 5:345-364(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 135-196.
RC TISSUE=Mammary carcinoma;
RX PubMed=1311287; DOI=10.1002/ijc.2910500419;
RA Lehtola L., Partanen J., Sistonen L., Korhonen J., Warri A., Harkonen P.,
RA Clarke R., Alitalo K.;
RT "Analysis of tyrosine kinase mRNAs including four FGF receptor mRNAs
RT expressed in MCF-7 breast-cancer cells.";
RL Int. J. Cancer 50:598-603(1992).
RN [7]
RP FUNCTION.
RX PubMed=16326102; DOI=10.1016/j.cub.2005.11.042;
RA Bettencourt-Dias M., Rodrigues-Martins A., Carpenter L., Riparbelli M.,
RA Lehmann L., Gatt M.K., Carmo N., Balloux F., Callaini G., Glover D.M.;
RT "SAK/PLK4 is required for centriole duplication and flagella development.";
RL Curr. Biol. 15:2199-2207(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-154.
RX PubMed=16244668; DOI=10.1038/ncb1320;
RA Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.;
RT "The Polo kinase Plk4 functions in centriole duplication.";
RL Nat. Cell Biol. 7:1140-1146(2005).
RN [9]
RP INDUCTION BY TP53.
RX PubMed=15967108; DOI=10.1593/neo.04325;
RA Li J., Tan M., Li L., Pamarthy D., Lawrence T.S., Sun Y.;
RT "SAK, a new polo-like kinase, is transcriptionally repressed by p53 and
RT induces apoptosis upon RNAi silencing.";
RL Neoplasia 7:312-323(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
RA Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D.,
RA Nigg E.A.;
RT "Plk4-induced centriole biogenesis in human cells.";
RL Dev. Cell 13:190-202(2007).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-41 AND THR-170.
RX PubMed=18239451; DOI=10.4161/cc.7.4.5387;
RA Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.;
RT "Human Plk4 phosphorylates Cdc25C.";
RL Cell Cycle 7:545-547(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
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).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-41 AND THR-170.
RX PubMed=19164942; DOI=10.4161/cc.8.2.7355;
RA Petrinac S., Ganuelas M.L., Bonni S., Nantais J., Hudson J.W.;
RT "Polo-like kinase 4 phosphorylates Chk2.";
RL Cell Cycle 8:327-329(2009).
RN [15]
RP INDUCTION.
RX PubMed=19454482; DOI=10.1242/jcs.036715;
RA Kuriyama R., Bettencourt-Dias M., Hoffmann I., Arnold M., Sandvig L.;
RT "Gamma-tubulin-containing abnormal centrioles are induced by insufficient
RT Plk4 in human HCT116 colorectal cancer cells.";
RL J. Cell Sci. 122:2014-2023(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP INTERACTION WITH CEP152.
RX PubMed=21059844; DOI=10.1083/jcb.201007107;
RA Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L.,
RA Haselmann-Weiss U., Antony C., Hoffmann I.;
RT "Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the
RT centrosome.";
RL J. Cell Biol. 191:731-739(2010).
RN [18]
RP INTERACTION WITH CEP152.
RX PubMed=20852615; DOI=10.1038/nature09445;
RA Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I.,
RA Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G.,
RA Glover D.M.;
RT "Asterless is a scaffold for the onset of centriole assembly.";
RL Nature 467:714-718(2010).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22020124; DOI=10.1038/emboj.2011.378;
RA Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C., Chang C.W.,
RA Wu K.S., Tang T.K.;
RT "The human microcephaly protein STIL interacts with CPAP and is required
RT for procentriole formation.";
RL EMBO J. 30:4790-4804(2011).
RN [20]
RP FUNCTION IN PHOSPHORYLATION OF FBXW5.
RX PubMed=21725316; DOI=10.1038/ncb2282;
RA Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U.,
RA Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P.,
RA Malek N.P.;
RT "The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6
RT to control centrosome duplication.";
RL Nat. Cell Biol. 13:1004-1009(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [22]
RP INVOLVEMENT IN MCPHCR.
RX PubMed=25344692; DOI=10.1038/ng.3122;
RA Martin C.A., Ahmad I., Klingseisen A., Hussain M.S., Bicknell L.S.,
RA Leitch A., Nuernberg G., Toliat M.R., Murray J.E., Hunt D., Khan F.,
RA Ali Z., Tinschert S., Ding J., Keith C., Harley M.E., Heyn P., Mueller R.,
RA Hoffmann I., Daire V.C., Dollfus H., Dupuis L., Bashamboo A.,
RA McElreavey K., Kariminejad A., Mendoza-Londono R., Moore A.T., Saggar A.,
RA Schlechter C., Weleber R., Thiele H., Altmueller J., Hoehne W.,
RA Hurles M.E., Noegel A.A., Baig S.M., Nuernberg P., Jackson A.P.;
RT "Mutations in PLK4, encoding a master regulator of centriole biogenesis,
RT cause microcephaly, growth failure and retinopathy.";
RL Nat. Genet. 46:1283-1292(2014).
RN [23]
RP INTERACTION WITH CEP78, AND SUBCELLULAR LOCATION.
RX PubMed=27246242; DOI=10.1242/jcs.184093;
RA Brunk K., Zhu M., Baerenz F., Kratz A.S., Haselmann-Weiss U., Antony C.,
RA Hoffmann I.;
RT "Cep78 is a new centriolar protein involved in Plk4-induced centriole
RT overduplication.";
RL J. Cell Sci. 129:2713-2718(2016).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACETYLATION AT LYS-45 AND LYS-46.
RX PubMed=27796307; DOI=10.1038/ncomms13227;
RA Fournier M., Orpinell M., Grauffel C., Scheer E., Garnier J.M., Ye T.,
RA Chavant V., Joint M., Esashi F., Dejaegere A., Goenczy P., Tora L.;
RT "KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in
RT preventing centrosome amplification.";
RL Nat. Commun. 7:13227-13227(2016).
RN [25]
RP FUNCTION, INTERACTION WITH CEP131, AND SUBCELLULAR LOCATION.
RX PubMed=30804208; DOI=10.1074/jbc.ra118.004867;
RA Denu R.A., Sass M.M., Johnson J.M., Potts G.K., Choudhary A., Coon J.J.,
RA Burkard M.E.;
RT "Polo-like kinase 4 maintains centriolar satellite integrity by
RT phosphorylation of centrosomal protein 131 (CEP131).";
RL J. Biol. Chem. 294:6531-6549(2019).
RN [26] {ECO:0007744|PDB:6W38, ECO:0007744|PDB:6W3I, ECO:0007744|PDB:6W3J}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 585-807 IN COMPLEXES WITH TENT5C
RP AND CEP192, INTERACTION WITH TENT5C, MUTAGENESIS OF ASN-669 AND ILE-670,
RP AND SUBCELLULAR LOCATION.
RX PubMed=32433990; DOI=10.1016/j.str.2020.04.023;
RA Chen H., Lu D., Shang G., Gao G., Zhang X.;
RT "Structural and Functional Analyses of the FAM46C/Plk4 Complex.";
RL Structure 28:910-921.e4(2020).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-275.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of PLK4 kinase.";
RL Submitted (JUN-2009) to the PDB data bank.
RN [28]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-86; HIS-146; THR-226; THR-232; LEU-317;
RP ASP-449; SER-519 AND ASP-830.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a central role in
CC centriole duplication. Able to trigger procentriole formation on the
CC surface of the parental centriole cylinder, leading to the recruitment
CC of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110,
CC CEP135 and gamma-tubulin. When overexpressed, it is able to induce
CC centrosome amplification through the simultaneous generation of
CC multiple procentrioles adjoining each parental centriole during S
CC phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition,
CC leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central
CC role in centriole replication suggests a possible role in
CC tumorigenesis, centrosome aberrations being frequently observed in
CC tumors. Also involved in deuterosome-mediated centriole amplification
CC in multiciliated that can generate more than 100 centrioles. Also
CC involved in trophoblast differentiation by phosphorylating HAND1,
CC leading to disrupt the interaction between HAND1 and MDFIC and activate
CC HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of
CC STIL to the centriole and for STIL-mediated centriole amplification
CC (PubMed:22020124). Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-
CC 372' which is essential for proper organization and integrity of
CC centriolar satellites (PubMed:30804208). {ECO:0000269|PubMed:16244668,
CC ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17681131,
CC ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942,
CC ECO:0000269|PubMed:21725316, ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:30804208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC Evidence={ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:18239451,
CC ECO:0000269|PubMed:19164942};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000269|PubMed:16244668,
CC ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CEP152 (via N-
CC terminus). Interacts with CEP78; this interaction may be important for
CC proper PLK4 localization to the centriole and PLK4-induced
CC overduplication of centrioles (PubMed:27246242). Interacts with CEP131
CC (PubMed:30804208). Interacts simultaneously with TENT5C and CEP192
CC (PubMed:32433990). Interacts with TENT5C; this interaction leads to the
CC TENT5C recruitment in the centrosome (PubMed:32433990).
CC {ECO:0000250|UniProtKB:Q64702, ECO:0000269|PubMed:20852615,
CC ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:27246242,
CC ECO:0000269|PubMed:30804208, ECO:0000269|PubMed:32433990}.
CC -!- INTERACTION:
CC O00444; P36575: ARR3; NbExp=3; IntAct=EBI-746202, EBI-718116;
CC O00444; Q9Y297: BTRC; NbExp=4; IntAct=EBI-746202, EBI-307461;
CC O00444; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-746202, EBI-8643161;
CC O00444; O94986: CEP152; NbExp=7; IntAct=EBI-746202, EBI-311012;
CC O00444; O94986-3: CEP152; NbExp=16; IntAct=EBI-746202, EBI-15878364;
CC O00444; Q8TEP8: CEP192; NbExp=2; IntAct=EBI-746202, EBI-2339778;
CC O00444; Q8TEP8-3: CEP192; NbExp=13; IntAct=EBI-746202, EBI-16111881;
CC O00444; P59910: DNAJB13; NbExp=3; IntAct=EBI-746202, EBI-11514233;
CC O00444; Q9H8V3: ECT2; NbExp=3; IntAct=EBI-746202, EBI-1054039;
CC O00444; Q14241: ELOA; NbExp=6; IntAct=EBI-746202, EBI-742350;
CC O00444; O95995: GAS8; NbExp=3; IntAct=EBI-746202, EBI-1052570;
CC O00444; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-746202, EBI-1051317;
CC O00444; P07237: P4HB; NbExp=3; IntAct=EBI-746202, EBI-395883;
CC O00444; O00444: PLK4; NbExp=10; IntAct=EBI-746202, EBI-746202;
CC O00444; P31947: SFN; NbExp=2; IntAct=EBI-746202, EBI-476295;
CC O00444; Q96R06: SPAG5; NbExp=3; IntAct=EBI-746202, EBI-413317;
CC O00444; Q15468: STIL; NbExp=11; IntAct=EBI-746202, EBI-7488405;
CC O00444; Q96A09: TENT5B; NbExp=3; IntAct=EBI-746202, EBI-752030;
CC O00444; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-746202, EBI-1105213;
CC O00444; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-746202, EBI-2130429;
CC O00444; O15060: ZBTB39; NbExp=3; IntAct=EBI-746202, EBI-9995672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:27246242, ECO:0000269|PubMed:27796307}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:30804208,
CC ECO:0000269|PubMed:32433990}. Note=Component of the deuterosome, a
CC structure that promotes de novo centriole amplification in
CC multiciliated cells that can generate more than 100 centrioles.
CC Associates with centrioles throughout the cell cycle. According to
CC PubMed:16244668, it is not present at cleavage furrows.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00444-2; Sequence=VSP_038117;
CC Name=3;
CC IsoId=O00444-3; Sequence=VSP_038116;
CC -!- INDUCTION: Down-regulated in HCT 116 colorectal cancer cells, leading
CC to aberrant centrioles composed of disorganized cylindrical
CC microtubules and displaced appendages. Down-regulated by p53/TP53.
CC {ECO:0000269|PubMed:15967108, ECO:0000269|PubMed:19454482}.
CC -!- DOMAIN: Cryptic POLO box 1 (CPB1) and Cryptic POLO box 2 (CPB2) domains
CC can simultaneously bind to both TENT5C and CEP192.
CC {ECO:0000269|PubMed:32433990}.
CC -!- PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting
CC the kinase to an inactive conformation. {ECO:0000269|PubMed:27796307}.
CC -!- PTM: Ubiquitinated; leading to its degradation by the proteasome.
CC {ECO:0000250}.
CC -!- PTM: Tyrosine-phosphorylated by TEC. {ECO:0000269|PubMed:11489907}.
CC -!- DISEASE: Microcephaly and chorioretinopathy, autosomal recessive, 2
CC (MCCRP2) [MIM:616171]: A severe disorder characterized by microcephaly,
CC delayed psychomotor development, growth retardation with dwarfism, and
CC ocular abnormalities. {ECO:0000269|PubMed:25344692}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU01328,
CC ECO:0000255|PROSITE-ProRule:PRU01329}.
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DR EMBL; Y13115; CAA73575.1; -; mRNA.
DR EMBL; AB006972; BAB69958.1; -; mRNA.
DR EMBL; AK302858; BAH13823.1; -; mRNA.
DR EMBL; AK303399; BAH13953.1; -; mRNA.
DR EMBL; AK314238; BAG36907.1; -; mRNA.
DR EMBL; BC036023; AAH36023.1; -; mRNA.
DR CCDS; CCDS3735.1; -. [O00444-1]
DR CCDS; CCDS54803.1; -. [O00444-2]
DR CCDS; CCDS54804.1; -. [O00444-3]
DR RefSeq; NP_001177728.1; NM_001190799.1. [O00444-2]
DR RefSeq; NP_001177730.1; NM_001190801.1. [O00444-3]
DR RefSeq; NP_055079.3; NM_014264.4. [O00444-1]
DR PDB; 2N19; NMR; -; A=884-970.
DR PDB; 3COK; X-ray; 2.25 A; A/B=2-275.
DR PDB; 4JXF; X-ray; 2.40 A; A=4-269.
DR PDB; 4N7V; X-ray; 2.76 A; A/B=580-808.
DR PDB; 4N7Z; X-ray; 2.85 A; A=580-808.
DR PDB; 4N9J; X-ray; 2.60 A; A/B=581-808.
DR PDB; 4YUR; X-ray; 2.65 A; A=2-275.
DR PDB; 4YYP; X-ray; 2.60 A; A=884-970.
DR PDB; 5LHY; X-ray; 3.31 A; 1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=884-970.
DR PDB; 5LHZ; X-ray; 2.51 A; A/B/C=884-970.
DR PDB; 6N45; X-ray; 2.64 A; A/B=581-808.
DR PDB; 6N46; X-ray; 3.71 A; A/B/C/D/E/F/G/H=581-808.
DR PDB; 6W38; X-ray; 4.48 A; B=585-807.
DR PDB; 6W3I; X-ray; 3.80 A; B=585-807.
DR PDB; 6W3J; X-ray; 4.38 A; B=585-807.
DR PDBsum; 2N19; -.
DR PDBsum; 3COK; -.
DR PDBsum; 4JXF; -.
DR PDBsum; 4N7V; -.
DR PDBsum; 4N7Z; -.
DR PDBsum; 4N9J; -.
DR PDBsum; 4YUR; -.
DR PDBsum; 4YYP; -.
DR PDBsum; 5LHY; -.
DR PDBsum; 5LHZ; -.
DR PDBsum; 6N45; -.
DR PDBsum; 6N46; -.
DR PDBsum; 6W38; -.
DR PDBsum; 6W3I; -.
DR PDBsum; 6W3J; -.
DR AlphaFoldDB; O00444; -.
DR BMRB; O00444; -.
DR SMR; O00444; -.
DR BioGRID; 115956; 93.
DR ComplexPortal; CPX-1161; CEP192-PLK4 complex.
DR ComplexPortal; CPX-1299; CEP152-PLK4 complex.
DR DIP; DIP-34467N; -.
DR IntAct; O00444; 60.
DR MINT; O00444; -.
DR STRING; 9606.ENSP00000270861; -.
DR BindingDB; O00444; -.
DR ChEMBL; CHEMBL3788; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O00444; -.
DR GuidetoPHARMACOLOGY; 2171; -.
DR iPTMnet; O00444; -.
DR PhosphoSitePlus; O00444; -.
DR BioMuta; PLK4; -.
DR jPOST; O00444; -.
DR MassIVE; O00444; -.
DR MaxQB; O00444; -.
DR PaxDb; O00444; -.
DR PeptideAtlas; O00444; -.
DR PRIDE; O00444; -.
DR ProteomicsDB; 47893; -. [O00444-1]
DR ProteomicsDB; 47894; -. [O00444-2]
DR ProteomicsDB; 47895; -. [O00444-3]
DR Antibodypedia; 26934; 223 antibodies from 35 providers.
DR DNASU; 10733; -.
DR Ensembl; ENST00000270861.10; ENSP00000270861.5; ENSG00000142731.11. [O00444-1]
DR Ensembl; ENST00000513090.5; ENSP00000427554.1; ENSG00000142731.11. [O00444-2]
DR Ensembl; ENST00000514379.5; ENSP00000423582.1; ENSG00000142731.11. [O00444-3]
DR GeneID; 10733; -.
DR KEGG; hsa:10733; -.
DR MANE-Select; ENST00000270861.10; ENSP00000270861.5; NM_014264.5; NP_055079.3.
DR UCSC; uc003ifo.4; human. [O00444-1]
DR CTD; 10733; -.
DR DisGeNET; 10733; -.
DR GeneCards; PLK4; -.
DR HGNC; HGNC:11397; PLK4.
DR HPA; ENSG00000142731; Group enriched (bone marrow, lymphoid tissue, testis).
DR MalaCards; PLK4; -.
DR MIM; 605031; gene.
DR MIM; 616171; phenotype.
DR neXtProt; NX_O00444; -.
DR OpenTargets; ENSG00000142731; -.
DR Orphanet; 2518; Autosomal recessive chorioretinopathy-microcephaly syndrome.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA36205; -.
DR VEuPathDB; HostDB:ENSG00000142731; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000156316; -.
DR InParanoid; O00444; -.
DR OMA; HSSWSEP; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; O00444; -.
DR TreeFam; TF101090; -.
DR BRENDA; 2.7.11.21; 2681.
DR PathwayCommons; O00444; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O00444; -.
DR SIGNOR; O00444; -.
DR BioGRID-ORCS; 10733; 722 hits in 1120 CRISPR screens.
DR EvolutionaryTrace; O00444; -.
DR GeneWiki; PLK4; -.
DR GenomeRNAi; 10733; -.
DR Pharos; O00444; Tchem.
DR PRO; PR:O00444; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O00444; protein.
DR Bgee; ENSG00000142731; Expressed in ventricular zone and 122 other tissues.
DR ExpressionAtlas; O00444; baseline and differential.
DR Genevisible; O00444; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0120098; C:procentriole; IDA:ComplexPortal.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IDA:ComplexPortal.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0046601; P:positive regulation of centriole replication; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
DR CDD; cd13114; POLO_box_Plk4_1; 1.
DR CDD; cd13115; POLO_box_Plk4_2; 1.
DR CDD; cd13116; POLO_box_Plk4_3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033700; Plk4.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR033699; POLO_box_Plk4_1.
DR InterPro; IPR033698; POLO_box_Plk4_2.
DR InterPro; IPR033696; POLO_box_Plk4_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24345:SF89; PTHR24345:SF89; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18190; Plk4_PB1; 1.
DR Pfam; PF18409; Plk4_PB2; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51984; CPB1; 1.
DR PROSITE; PS51985; CPB2; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Cytoskeleton; Dwarfism; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..970
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000086567"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 586..699
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 700..813
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 892..956
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 323..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:27796307"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:27796307"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038116"
FT VAR_SEQ 43..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038117"
FT VARIANT 86
FT /note="Y -> C (in dbSNP:rs34156294)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041027"
FT VARIANT 146
FT /note="R -> H (in dbSNP:rs35232579)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041028"
FT VARIANT 226
FT /note="A -> T (in dbSNP:rs35448573)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041029"
FT VARIANT 232
FT /note="S -> T (in dbSNP:rs3811740)"
FT /evidence="ECO:0000269|PubMed:11489907,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17344846,
FT ECO:0000269|Ref.1"
FT /id="VAR_019632"
FT VARIANT 317
FT /note="P -> L (in dbSNP:rs35049837)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041030"
FT VARIANT 449
FT /note="N -> D (in dbSNP:rs34906574)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041031"
FT VARIANT 519
FT /note="W -> S (in dbSNP:rs56043017)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041032"
FT VARIANT 830
FT /note="E -> D (in dbSNP:rs17012739)"
FT /evidence="ECO:0000269|PubMed:11489907,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17344846,
FT ECO:0000269|Ref.1"
FT /id="VAR_041033"
FT MUTAGEN 41
FT /note="K->M: Abolishes ability to phosphorylate CDC25C and
FT CHEK2."
FT /evidence="ECO:0000269|PubMed:18239451,
FT ECO:0000269|PubMed:19164942"
FT MUTAGEN 154
FT /note="D->A: Catalytically inactive mutant that causes some
FT centrosome amplification above background levels when
FT overexpressed."
FT /evidence="ECO:0000269|PubMed:16244668"
FT MUTAGEN 170
FT /note="T->D: Activating mutant."
FT /evidence="ECO:0000269|PubMed:18239451,
FT ECO:0000269|PubMed:19164942"
FT MUTAGEN 669
FT /note="N->R: Does not affect the interaction with TENT5C."
FT /evidence="ECO:0000269|PubMed:32433990"
FT MUTAGEN 670
FT /note="I->P: Decreases substantially the interaction with
FT TENT5C. Does not affect localization to the centrosome.
FT Loss of TENT5C recruitment to the centrosome."
FT /evidence="ECO:0000269|PubMed:32433990"
FT CONFLICT 34
FT /note="T -> S (in Ref. 2; BAB69958)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> K (in Ref. 1; CAA73575)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="D -> N (in Ref. 3; BAH13823)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="S -> R (in Ref. 2; BAB69958)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="F -> S (in Ref. 3; BAH13823)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="V -> L (in Ref. 2; BAB69958)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="Y -> F (in Ref. 1; CAA73575)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="A -> D (in Ref. 2; BAB69958)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:3COK"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4JXF"
FT HELIX 110..129
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3COK"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3COK"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:4JXF"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:4JXF"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3COK"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3COK"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 630..639
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 651..654
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 683..698
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 700..706
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 708..716
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 749..752
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 755..759
FT /evidence="ECO:0007829|PDB:4N9J"
FT HELIX 765..793
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 800..804
FT /evidence="ECO:0007829|PDB:4N9J"
FT STRAND 887..893
FT /evidence="ECO:0007829|PDB:5LHZ"
FT TURN 894..896
FT /evidence="ECO:0007829|PDB:5LHZ"
FT STRAND 897..902
FT /evidence="ECO:0007829|PDB:5LHZ"
FT STRAND 905..911
FT /evidence="ECO:0007829|PDB:5LHZ"
FT STRAND 916..922
FT /evidence="ECO:0007829|PDB:5LHZ"
FT STRAND 924..929
FT /evidence="ECO:0007829|PDB:5LHZ"
FT TURN 931..933
FT /evidence="ECO:0007829|PDB:2N19"
FT STRAND 935..939
FT /evidence="ECO:0007829|PDB:5LHZ"
FT HELIX 946..961
FT /evidence="ECO:0007829|PDB:5LHZ"
SQ SEQUENCE 970 AA; 108972 MW; 4D56F5FD983211A6 CRC64;
MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD
LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ ETSNSGRGRV
IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH SAEMLSVSKR SGGGENEERY
SPTDNNANIF NFFKEKTSSS SGSFERPDNN QALSNHLCPG KTPFPFADPT PQTETVQQWF
GNLQINAHLR KTTEYDSISP NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ
NTMKYMTALH SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK
PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY PNGGRGFPLA
DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG
ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL
ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH
SAASPTQAPI LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ KLQCLSSILL
MFSNPTPNFH
