PCNT_HUMAN
ID PCNT_HUMAN Reviewed; 3336 AA.
AC O95613; O43152; Q7Z7C9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Pericentrin;
DE AltName: Full=Kendrin;
DE AltName: Full=Pericentrin-B;
GN Name=PCNT; Synonyms=KIAA0402, PCNT2;
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), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND VARIANTS GLU-704; ALA-879; ALA-1038; ARG-2188 AND THR-2549.
RX PubMed=11171385; DOI=10.1242/jcs.114.4.797;
RA Li Q., Hansen D., Killilea A., Joshi H.C., Palazzo R.E., Balczon R.;
RT "Kendrin/pericentrin-B, a centrosome protein with homology to pericentrin
RT that complexes with PCM-1.";
RL J. Cell Sci. 114:797-809(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-704.
RA Gromley A.S., Jurczyk A., Sillibourne J.E., Halilovic E., Doxsey S.J.;
RT "Vertebrate centrosome proteins that share homology with yeast mitotic exit
RT proteins are required for cytokinesis and cell cycle progression.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-704
RP AND ALA-1038.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [4]
RP SEQUENCE REVISION TO 3023.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 787-1533 (ISOFORM 1), AND VARIANT
RP ALA-1038.
RC TISSUE=Trachea;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALMODULIN-BINDING
RP DOMAIN, AND MUTAGENESIS OF 3196-PHE-ARG-3197; VAL-3203 AND
RP 3208-ARG-LEU-3209.
RX PubMed=10823944; DOI=10.1073/pnas.97.11.5919;
RA Flory M.R., Moser M.J., Monnat R.J. Jr., Davis T.N.;
RT "Identification of a human centrosomal calmodulin-binding protein that
RT shares homology with pericentrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5919-5923(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP FUNCTION, INTERACTION WITH DISC1, AND SUBCELLULAR LOCATION.
RX PubMed=18955030; DOI=10.1016/j.bbrc.2008.10.100;
RA Shimizu S., Matsuzaki S., Hattori T., Kumamoto N., Miyoshi K., Katayama T.,
RA Tohyama M.;
RT "DISC1-kendrin interaction is involved in centrosomal microtubule network
RT formation.";
RL Biochem. Biophys. Res. Commun. 377:1051-1056(2008).
RN [11]
RP INVOLVEMENT IN MOPD2.
RX PubMed=18157127; DOI=10.1038/ng.2007.80;
RA Griffith E., Walker S., Martin C.-A., Vagnarelli P., Stiff T., Vernay B.,
RA Al Sanna N., Saggar A., Hamel B., Earnshaw W.C., Jeggo P.A., Jackson A.P.,
RA O'Driscoll M.;
RT "Mutations in pericentrin cause Seckel syndrome with defective ATR-
RT dependent DNA damage signaling.";
RL Nat. Genet. 40:232-236(2008).
RN [12]
RP INVOLVEMENT IN MOPD2.
RX PubMed=18174396; DOI=10.1126/science.1151174;
RA Rauch A., Thiel C.T., Schindler D., Wick U., Crow Y.J., Ekici A.B.,
RA van Essen A.J., Goecke T.O., Al-Gazali L., Chrzanowska K.H., Zweier C.,
RA Brunner H.G., Becker K., Curry C.J., Dallapiccola B., Devriendt K.,
RA Doerfler A., Kinning E., Megarbane A., Meinecke P., Semple R.K.,
RA Spranger S., Toutain A., Trembath R.C., Voss E., Wilson L., Hennekam R.,
RA de Zegher F., Doerr H.-G., Reis A.;
RT "Mutations in the pericentrin (PCNT) gene cause primordial dwarfism.";
RL Science 319:816-819(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2177 AND SER-2327, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH NEK2.
RX PubMed=20599736; DOI=10.1016/j.bbrc.2010.06.063;
RA Matsuo K., Nishimura T., Hayakawa A., Ono Y., Takahashi M.;
RT "Involvement of a centrosomal protein kendrin in the maintenance of
RT centrosome cohesion by modulating Nek2A kinase activity.";
RL Biochem. Biophys. Res. Commun. 398:217-223(2010).
RN [15]
RP INTERACTION WITH CDK5RAP2.
RX PubMed=20466722; DOI=10.1074/jbc.m110.105965;
RA Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.;
RT "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and
RT the Golgi complex.";
RL J. Biol. Chem. 285:22658-22665(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191; SER-682; SER-2044;
RP SER-2477; SER-2486 AND SER-3302, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP CLEAVAGE, AND MUTAGENESIS OF ARG-2231 AND LYS-2232.
RX PubMed=22722493; DOI=10.4161/cc.20878;
RA Lee K., Rhee K.;
RT "Separase-dependent cleavage of pericentrin B is necessary and sufficient
RT for centriole disengagement during mitosis.";
RL Cell Cycle 11:2476-2485(2012).
RN [19]
RP INTERACTION WITH CEP131, AND SUBCELLULAR LOCATION.
RX PubMed=22797915; DOI=10.1242/jcs.104059;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J., Swanton C.,
RA Howell M., Boulton S.J., Collis S.J.;
RT "The centriolar satellite protein Cep131 is important for genome
RT stability.";
RL J. Cell Sci. 125:4770-4779(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-188; THR-191;
RP SER-1245; SER-1653; SER-2192; SER-2352; SER-2355 AND SER-2477, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=27137183; DOI=10.1007/s00018-016-2236-8;
RA Fang C.T., Kuo H.H., Pan T.S., Yu F.C., Yih L.H.;
RT "HSP70 regulates the function of mitotic centrosomes.";
RL Cell. Mol. Life Sci. 73:3949-3960(2016).
RN [23]
RP VARIANTS ARG-1452 AND GLN-2424.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [24]
RP INTERACTION WITH CCDC13.
RX PubMed=24816561; DOI=10.1242/jcs.147785;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Howard A.E.,
RA Barone G., Lee A.J., Swanton C., Howell M., Maslen S., Skehel J.M.,
RA Boulton S.J., Collis S.J.;
RT "Ccdc13 is a novel human centriolar satellite protein required for
RT ciliogenesis and genome stability.";
RL J. Cell Sci. 127:2910-2919(2014).
RN [25]
RP INTERACTION WITH ATF5.
RX PubMed=26213385; DOI=10.1016/j.cell.2015.06.055;
RA Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J., Liu X.,
RA Lu Z., Liu D.X.;
RT "ATF5 Connects the Pericentriolar Materials to the Proximal End of the
RT Mother Centriole.";
RL Cell 162:580-592(2015).
RN [26]
RP INTERACTION WITH CEP68, AND MUTAGENESIS OF ARG-2231.
RX PubMed=25503564; DOI=10.1038/ncb3076;
RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L.,
RA Washburn M.P., Pagano M.;
RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM
RT to allow centriole separation, disengagement and licensing.";
RL Nat. Cell Biol. 17:31-43(2015).
CC -!- FUNCTION: Integral component of the filamentous matrix of the
CC centrosome involved in the initial establishment of organized
CC microtubule arrays in both mitosis and meiosis. Plays a role, together
CC with DISC1, in the microtubule network formation. Is an integral
CC component of the pericentriolar material (PCM). May play an important
CC role in preventing premature centrosome splitting during interphase by
CC inhibiting NEK2 kinase activity at the centrosome.
CC {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385,
CC ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736}.
CC -!- SUBUNIT: Interacts with CHD3. Interacts with CHD4; the interaction
CC regulates centrosome integrity (By similarity). Interacts with DISC1
CC and PCM1. Binds calmodulin. Interacts with CDK5RAP2; the interaction is
CC leading to centrosomal localization of PCNT and CDK5RAP2. Interacts
CC with isoform 1 of NEK2. Interacts with CEP131. Interacts with CCDC13
CC (PubMed:24816561). Interacts with CEP68 (PubMed:25503564). Interacts
CC with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite
CC unites the mother centriole and the pericentriolar material (PCM) in
CC the centrosome (PubMed:26213385). {ECO:0000250|UniProtKB:P48725,
CC ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030,
CC ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:20599736,
CC ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:24816561,
CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:26213385}.
CC -!- INTERACTION:
CC O95613; Q76N32: CEP68; NbExp=3; IntAct=EBI-530012, EBI-9051024;
CC O95613; Q9NRI5: DISC1; NbExp=5; IntAct=EBI-530012, EBI-529989;
CC O95613; Q15154: PCM1; NbExp=8; IntAct=EBI-530012, EBI-741421;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:10823944,
CC ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:22797915,
CC ECO:0000269|PubMed:27137183}. Note=Centrosomal at all stages of the
CC cell cycle. Remains associated with centrosomes following microtubule
CC depolymerization. Colocalized with DISC1 at the centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95613-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95613-2; Sequence=VSP_040104, VSP_040105;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
CC placenta, liver, kidney and thymus. {ECO:0000269|PubMed:10823944}.
CC -!- DOMAIN: Composed of a coiled-coil central region flanked by non-helical
CC N- and C-terminals.
CC -!- PTM: Cleaved during mitotis which leads to removal of CDK5RAP2 from the
CC centrosome and promotes centriole disengagement and subsequent
CC centriole separation (PubMed:22722493, PubMed:25503564). The C-terminal
CC fragment is rapidly degraded following cleavage (PubMed:22722493).
CC {ECO:0000269|PubMed:22722493, ECO:0000269|PubMed:25503564}.
CC -!- DISEASE: Microcephalic osteodysplastic primordial dwarfism 2 (MOPD2)
CC [MIM:210720]: Adults with this rare inherited condition have an average
CC height of 100 centimeters and a brain size comparable to that of a 3-
CC month-old baby, but are of near-normal intelligence.
CC {ECO:0000269|PubMed:18157127, ECO:0000269|PubMed:18174396}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10838.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA23698.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04252.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U52962; AAD10838.1; ALT_FRAME; mRNA.
DR EMBL; AF515282; AAP46636.1; -; mRNA.
DR EMBL; AB007862; BAA23698.3; ALT_INIT; mRNA.
DR EMBL; AP000471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK093923; BAC04252.1; ALT_INIT; mRNA.
DR CCDS; CCDS33592.1; -. [O95613-1]
DR RefSeq; NP_001302458.1; NM_001315529.1. [O95613-2]
DR RefSeq; NP_006022.3; NM_006031.5. [O95613-1]
DR SMR; O95613; -.
DR BioGRID; 111146; 185.
DR CORUM; O95613; -.
DR DIP; DIP-33829N; -.
DR ELM; O95613; -.
DR IntAct; O95613; 69.
DR MINT; O95613; -.
DR STRING; 9606.ENSP00000352572; -.
DR GlyGen; O95613; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95613; -.
DR MetOSite; O95613; -.
DR PhosphoSitePlus; O95613; -.
DR SwissPalm; O95613; -.
DR BioMuta; PCNT; -.
DR EPD; O95613; -.
DR jPOST; O95613; -.
DR MassIVE; O95613; -.
DR MaxQB; O95613; -.
DR PaxDb; O95613; -.
DR PeptideAtlas; O95613; -.
DR PRIDE; O95613; -.
DR ProteomicsDB; 50949; -. [O95613-1]
DR ProteomicsDB; 50950; -. [O95613-2]
DR Antibodypedia; 3139; 218 antibodies from 25 providers.
DR Ensembl; ENST00000359568.10; ENSP00000352572.5; ENSG00000160299.17. [O95613-1]
DR GeneID; 5116; -.
DR KEGG; hsa:5116; -.
DR MANE-Select; ENST00000359568.10; ENSP00000352572.5; NM_006031.6; NP_006022.3.
DR UCSC; uc002zji.4; human. [O95613-1]
DR CTD; 5116; -.
DR DisGeNET; 5116; -.
DR GeneCards; PCNT; -.
DR GeneReviews; PCNT; -.
DR HGNC; HGNC:16068; PCNT.
DR HPA; ENSG00000160299; Tissue enriched (skeletal).
DR MalaCards; PCNT; -.
DR MIM; 210720; phenotype.
DR MIM; 605925; gene.
DR neXtProt; NX_O95613; -.
DR OpenTargets; ENSG00000160299; -.
DR Orphanet; 2637; Microcephalic osteodysplastic primordial dwarfism type II.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA33079; -.
DR VEuPathDB; HostDB:ENSG00000160299; -.
DR eggNOG; ENOG502QV16; Eukaryota.
DR GeneTree; ENSGT00730000110871; -.
DR HOGENOM; CLU_000160_0_0_1; -.
DR InParanoid; O95613; -.
DR OMA; VSDHHPE; -.
DR OrthoDB; 8180at2759; -.
DR PhylomeDB; O95613; -.
DR TreeFam; TF336114; -.
DR PathwayCommons; O95613; -.
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 Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR SignaLink; O95613; -.
DR SIGNOR; O95613; -.
DR BioGRID-ORCS; 5116; 85 hits in 1089 CRISPR screens.
DR ChiTaRS; PCNT; human.
DR GeneWiki; PCNT; -.
DR GenomeRNAi; 5116; -.
DR Pharos; O95613; Tbio.
DR PRO; PR:O95613; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O95613; protein.
DR Bgee; ENSG00000160299; Expressed in gastrocnemius and 194 other tissues.
DR ExpressionAtlas; O95613; baseline and differential.
DR Genevisible; O95613; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IDA:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR028745; AKAP9/Pericentrin.
DR InterPro; IPR019528; PACT_domain.
DR PANTHER; PTHR44981; PTHR44981; 1.
DR Pfam; PF10495; PACT_coil_coil; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Dwarfism; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..3336
FT /note="Pericentrin"
FT /id="PRO_0000058257"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1954..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2168..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2875..2910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2983..3246
FT /note="Interaction with NEK2"
FT /evidence="ECO:0000269|PubMed:20599736"
FT REGION 3084..3126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3195..3208
FT /note="Calmodulin-binding"
FT REGION 3224..3300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..553
FT /evidence="ECO:0000255"
FT COILED 675..835
FT /evidence="ECO:0000255"
FT COILED 1010..1146
FT /evidence="ECO:0000255"
FT COILED 1299..1949
FT /evidence="ECO:0000255"
FT COILED 2064..2082
FT /evidence="ECO:0000255"
FT COILED 2536..3086
FT /evidence="ECO:0000255"
FT COMPBIAS 1..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2182..2202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2875..2895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3084..3099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3236..3250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3252..3266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3279..3300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48725"
FT MOD_RES 2044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48725"
FT MOD_RES 2226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48725"
FT MOD_RES 2327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9455477"
FT /id="VSP_040104"
FT VAR_SEQ 2839..2917
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9455477"
FT /id="VSP_040105"
FT VARIANT 539
FT /note="T -> I (in dbSNP:rs2249060)"
FT /id="VAR_043878"
FT VARIANT 704
FT /note="G -> E (in dbSNP:rs2839223)"
FT /evidence="ECO:0000269|PubMed:11171385,
FT ECO:0000269|PubMed:9455477, ECO:0000269|Ref.2"
FT /id="VAR_043879"
FT VARIANT 879
FT /note="T -> A (in dbSNP:rs2839227)"
FT /evidence="ECO:0000269|PubMed:11171385"
FT /id="VAR_043880"
FT VARIANT 1038
FT /note="V -> A (in dbSNP:rs6518289)"
FT /evidence="ECO:0000269|PubMed:11171385,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9455477"
FT /id="VAR_043881"
FT VARIANT 1163
FT /note="R -> C (in dbSNP:rs7279204)"
FT /id="VAR_043882"
FT VARIANT 1194
FT /note="A -> T (in dbSNP:rs35044802)"
FT /id="VAR_043883"
FT VARIANT 1452
FT /note="G -> R (found in a patient with intellectual
FT disability, no speech, facial and limbs dysmorphisms;
FT dbSNP:rs143796569)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069420"
FT VARIANT 1639
FT /note="I -> V (in dbSNP:rs6518291)"
FT /id="VAR_043884"
FT VARIANT 1841
FT /note="N -> S (in dbSNP:rs35940413)"
FT /id="VAR_043885"
FT VARIANT 1953
FT /note="R -> H (in dbSNP:rs34268261)"
FT /id="VAR_043886"
FT VARIANT 1960
FT /note="R -> Q (in dbSNP:rs34813667)"
FT /id="VAR_043887"
FT VARIANT 2097
FT /note="L -> P (in dbSNP:rs2839245)"
FT /id="VAR_043888"
FT VARIANT 2125
FT /note="H -> P (in dbSNP:rs35978208)"
FT /id="VAR_043889"
FT VARIANT 2188
FT /note="M -> R (in dbSNP:rs1044998)"
FT /evidence="ECO:0000269|PubMed:11171385"
FT /id="VAR_043890"
FT VARIANT 2191
FT /note="S -> P (in dbSNP:rs34151633)"
FT /id="VAR_043891"
FT VARIANT 2239
FT /note="W -> R (in dbSNP:rs35346764)"
FT /id="VAR_056961"
FT VARIANT 2274
FT /note="P -> L (in dbSNP:rs2070425)"
FT /id="VAR_056962"
FT VARIANT 2329
FT /note="P -> R (in dbSNP:rs35848602)"
FT /id="VAR_056963"
FT VARIANT 2361
FT /note="Q -> R (in dbSNP:rs7277175)"
FT /id="VAR_056964"
FT VARIANT 2424
FT /note="R -> Q (found in a patient with intellectual
FT disability, no speech, facial and limbs dysmorphisms;
FT dbSNP:rs371893416)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069421"
FT VARIANT 2549
FT /note="A -> T (in dbSNP:rs2839256)"
FT /evidence="ECO:0000269|PubMed:11171385"
FT /id="VAR_056965"
FT VARIANT 2625
FT /note="R -> Q (in dbSNP:rs8131693)"
FT /id="VAR_056966"
FT VARIANT 2659
FT /note="Q -> H (in dbSNP:rs2070426)"
FT /id="VAR_056967"
FT VARIANT 2753
FT /note="R -> H (in dbSNP:rs743346)"
FT /id="VAR_056968"
FT VARIANT 2792
FT /note="Q -> R (in dbSNP:rs2073376)"
FT /id="VAR_056969"
FT VARIANT 2903
FT /note="A -> T (in dbSNP:rs35147998)"
FT /id="VAR_056970"
FT VARIANT 2975
FT /note="L -> P (in dbSNP:rs35881595)"
FT /id="VAR_056971"
FT VARIANT 3091
FT /note="S -> G (in dbSNP:rs4818842)"
FT /id="VAR_056972"
FT VARIANT 3245
FT /note="R -> S (in dbSNP:rs2073380)"
FT /id="VAR_056973"
FT MUTAGEN 2231
FT /note="R->A: Produces non-cleavable protein which remains
FT on centrosomes in late mitosis until its levels eventually
FT drop in cells undergoing cytokinesis."
FT /evidence="ECO:0000269|PubMed:22722493,
FT ECO:0000269|PubMed:25503564"
FT MUTAGEN 2232
FT /note="K->M: Stabilizes the C-terminal fragment produced by
FT cleavage."
FT /evidence="ECO:0000269|PubMed:22722493"
FT MUTAGEN 3196..3197
FT /note="FR->AA: Decrease in calmodulin binding."
FT /evidence="ECO:0000269|PubMed:10823944"
FT MUTAGEN 3203
FT /note="V->A: Decrease in calmodulin binding."
FT /evidence="ECO:0000269|PubMed:10823944"
FT MUTAGEN 3208..3209
FT /note="RL->AA: Decrease in calmodulin binding."
FT /evidence="ECO:0000269|PubMed:10823944"
FT CONFLICT 703
FT /note="Y -> F (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="F -> L (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="G -> A (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 890..900
FT /note="Missing (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="S -> T (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="E -> K (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="T -> A (in Ref. 7; BAC04252)"
FT /evidence="ECO:0000305"
FT CONFLICT 1287
FT /note="I -> L (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1317
FT /note="K -> T (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534
FT /note="Q -> H (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 3136
FT /note="Y -> S (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
FT CONFLICT 3300
FT /note="E -> G (in Ref. 1; AAD10838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3336 AA; 378037 MW; 4F182D2C201662A8 CRC64;
MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV QEESPVTKED
SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED LEQLQQKQVN DHPPEQCGMF
TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD HPPEQHGMFT VSDHPPEQRG MFTISDHQPE
QRGMFTVSDH TPEQRGIFTI SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ
AVHGLELEAL RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ
HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW ESEKDLCLEN
LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ AERALRNLES HHQAAIEKLR
EDLQSEHGRC LEDLEFKFKE SEKEKQLELE NLQASYEDLK AQSQEEIRRL WSQLDSARTS
RQELSELHEQ LLARTSRVED LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL
LQQRLQGARE DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES
HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV HLQGVQDGDL
EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR NLYGKLQHET RLKDDLEKVK
HNLIEDHQKE LNNAKQKTEL MKQEFQRKET DWKVMKEELQ REAEEKLTLM LLELREKAES
EKQTIINKFE LREAEMRQLQ DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG
REPPTAQDGE LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE
LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ TKHAADLGAL
ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ LWKKDSLHQT ILTQELEKLK
RKHEGELQSV RDHLRTEVST ELAGTVAHEL QGVHQGEFGS EKKTALHEKE ETLRLQSAQA
QPFHQEEKES LSLQLQKKNH QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL
LSMLKADVNL SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL
STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR ECEQPIRRVF
QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE ETAQVVRKHQ ELLECLKEES
AAKAELALEL HKTQGTLEGF KVETADLKEV LAGKEDSEHR LVLELESLRR QLQQAAQEQA
ALREECTRLW SRGEATATDA EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE
SELEEQLSQH RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ
RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK ESADRQVLMQ
EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE VLKKQQMSSL LLASTLQSTL
DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR RESEVLDLKE QLEKMKGDLE SKNEEILHLN
LKLDMQNSQT AVSLRELEEE NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE
QLHEVIEKLQ HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE
ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE DMASRIQEFE
AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR IRRALEQQPL AAGAAPPELQ
WLRAQCARLS RQLQVLHQRF LRCQVELDRR QARRATAHTR VPGAHPQPRM DGGAKAQVTG
DVEASHDAAL EPVVPDPQGD LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE
MRLSLEDGGK GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM
ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC DANTTPGGVT
DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS RHQSHTAEAG PRKSPVGMLD
LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA LSLCSADTSL GDRADTSLPQ TQGPGLLCSP
GVSAAALALQ WAESPPADDH HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE
KSDGSGFGAR LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR
DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR GDLLQVVQEA
FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD LQEKSLEHLR LPDRSSLLSE
IQALRAQLRM THLQNQEKLQ HLRTALTSAE ARGSQQEHQL RRQVELLAYK VEQEKCIAGD
LQKTLSEEQE KANSVQKLLA AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM
LSSKENELKA ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ
SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE KSRTLELSEA
LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR VVDLQAMLEK VQQQALHSQQ
QLEAEAQKHC EALRREKEVS ATLKSTVEAL HTQKRELRCS LEREREKPAW LQAELEQSHP
RLKEQEGRKA ARRSAEARQS PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD
LESKDEVPGS RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT
VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK DNVSLTKALS
TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP DETAPQSSLR RPDPGRLPPA
ASEEAHTSNV KMEKLYLHYL RAESFRKALI YQKKYLLLLI GGFQDSEQET LSMIAHLGVF
PSKAERKITS RPFTRFRTAV RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP
QSPPRTRESP PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE
HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ
