PCNT_MOUSE
ID PCNT_MOUSE Reviewed; 2898 AA.
AC P48725; A0JBT0; A0JBT1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Pericentrin;
GN Name=Pcnt; Synonyms=Pcnt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=8124707; DOI=10.1016/0092-8674(94)90504-5;
RA Doxsey S.J., Stein P., Evans L., Calarco P.D., Kirschner M.;
RT "Pericentrin, a highly conserved centrosome protein involved in microtubule
RT organization.";
RL Cell 76:639-650(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=17084386; DOI=10.1016/j.bbrc.2006.10.101;
RA Miyoshi K., Asanuma M., Miyazaki I., Matsuzaki S., Tohyama M., Ogawa N.;
RT "Characterization of pericentrin isoforms in vivo.";
RL Biochem. Biophys. Res. Commun. 351:745-749(2006).
RN [3]
RP INTERACTION WITH CHD3 AND CHD4, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17626165; DOI=10.1091/mbc.e06-07-0604;
RA Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.;
RT "Chromatin remodeling proteins interact with pericentrin to regulate
RT centrosome integrity.";
RL Mol. Biol. Cell 18:3667-3680(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437; SER-1859 AND SER-1860,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH CDK5RAP2, AND DEVELOPMENTAL STAGE.
RX PubMed=20471352; DOI=10.1016/j.neuron.2010.03.036;
RA Buchman J.J., Tseng H.C., Zhou Y., Frank C.L., Xie Z., Tsai L.H.;
RT "Cdk5rap2 interacts with pericentrin to maintain the neural progenitor pool
RT in the developing neocortex.";
RL Neuron 66:386-402(2010).
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:0000250|UniProtKB:O95613, ECO:0000269|PubMed:17626165}.
CC -!- SUBUNIT: Interacts with DISC1 and PCM1. Binds calmodulin. Interacts
CC with CEP131 (By similarity). Interacts with CDK5RAP2; the interaction
CC is leading to centrosomal localization of PCNT and CDK5RAP2
CC (PubMed:20471352). Interacts with CHD3 (PubMed:17626165). Interacts
CC with CHD4; the interaction regulates centrosome integrity
CC (PubMed:17626165). Interacts with NEK2 (By similarity). Interacts with
CC CCDC13 (By similarity). Interacts with CEP68 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:O95613,
CC ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:20471352}.
CC -!- INTERACTION:
CC P48725; Q6A078: Cep290; NbExp=2; IntAct=EBI-2290976, EBI-1811999;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:O95613}. Note=Centrosomal at
CC all stages of the cell cycle. Remains associated with centrosomes
CC following microtubule depolymerization. Colocalized with DISC1 at the
CC centrosome. {ECO:0000250|UniProtKB:O95613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Pericentrin B, Pericentrin-360;
CC IsoId=P48725-1; Sequence=Displayed;
CC Name=2; Synonyms=Pericentrin S, Pericentrin-255;
CC IsoId=P48725-2; Sequence=VSP_038927;
CC Name=3;
CC IsoId=P48725-3; Sequence=VSP_038928, VSP_038929;
CC -!- TISSUE SPECIFICITY: Expressed in heart and lung (at protein level).
CC Expressed in kidney, thymus, liver, brain, muscle, testis, spleen, lung
CC and heart. {ECO:0000269|PubMed:17084386}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 17 dpc (at protein level).
CC Expressed in embryos at 7, 11, 15 and 17 dpc. Strongly expressed in
CC brain tissues at early stages of development.
CC {ECO:0000269|PubMed:17084386, ECO:0000269|PubMed:20471352}.
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. The C-terminal fragment is rapidly degraded
CC following cleavage. {ECO:0000250|UniProtKB:O95613}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17886.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; U05823; AAA17886.1; ALT_SEQ; mRNA.
DR EMBL; AB207233; BAF36559.1; -; mRNA.
DR EMBL; AB207234; BAF36560.1; -; mRNA.
DR CCDS; CCDS88027.1; -. [P48725-1]
DR PIR; A53188; A53188.
DR RefSeq; NP_001269921.1; NM_001282992.1.
DR RefSeq; NP_032813.3; NM_008787.3.
DR SMR; P48725; -.
DR BioGRID; 202052; 8.
DR CORUM; P48725; -.
DR IntAct; P48725; 3.
DR STRING; 10090.ENSMUSP00000001179; -.
DR iPTMnet; P48725; -.
DR PhosphoSitePlus; P48725; -.
DR EPD; P48725; -.
DR jPOST; P48725; -.
DR MaxQB; P48725; -.
DR PaxDb; P48725; -.
DR PeptideAtlas; P48725; -.
DR PRIDE; P48725; -.
DR ProteomicsDB; 287893; -. [P48725-1]
DR ProteomicsDB; 287894; -. [P48725-2]
DR ProteomicsDB; 287895; -. [P48725-3]
DR GeneID; 18541; -.
DR KEGG; mmu:18541; -.
DR UCSC; uc007fuj.1; mouse. [P48725-1]
DR CTD; 5116; -.
DR MGI; MGI:102722; Pcnt.
DR eggNOG; ENOG502QV16; Eukaryota.
DR InParanoid; P48725; -.
DR OrthoDB; 8180at2759; -.
DR PhylomeDB; P48725; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR BioGRID-ORCS; 18541; 13 hits in 71 CRISPR screens.
DR ChiTaRS; Pcnt; mouse.
DR PRO; PR:P48725; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P48725; protein.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0060322; P:head development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IDA:MGI.
DR GO; GO:0001944; P:vasculature development; IMP:MGI.
DR InterPro; IPR028745; AKAP9/Pericentrin.
DR InterPro; IPR019528; PACT_domain.
DR PANTHER; PTHR44981; PTHR44981; 3.
DR Pfam; PF10495; PACT_coil_coil; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..2898
FT /note="Pericentrin"
FT /id="PRO_0000058258"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1822
FT /note="Interaction with CDK5RAP2"
FT /evidence="ECO:0000269|PubMed:20471352"
FT REGION 1815..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..1979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2046..2088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2509..2532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2545..2810
FT /note="Interaction with NEK2"
FT /evidence="ECO:0000250"
FT REGION 2653..2684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2758..2771
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 2787..2898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 127..343
FT /evidence="ECO:0000255"
FT COILED 382..434
FT /evidence="ECO:0000255"
FT COILED 468..527
FT /evidence="ECO:0000255"
FT COILED 611..696
FT /evidence="ECO:0000255"
FT COILED 727..787
FT /evidence="ECO:0000255"
FT COILED 872..939
FT /evidence="ECO:0000255"
FT COILED 1069..1383
FT /evidence="ECO:0000255"
FT COILED 1429..1482
FT /evidence="ECO:0000255"
FT COILED 1529..1593
FT /evidence="ECO:0000255"
FT COILED 2211..2403
FT /evidence="ECO:0000255"
FT COILED 2429..2590
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2653..2667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2803..2828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2839..2864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 1437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1959
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 1987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT MOD_RES 2865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95613"
FT VAR_SEQ 1..916
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17084386"
FT /id="VSP_038927"
FT VAR_SEQ 2044..2050
FT /note="ALSESQD -> GNSRLLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8124707"
FT /id="VSP_038928"
FT VAR_SEQ 2501..2898
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8124707"
FT /id="VSP_038929"
FT CONFLICT 652
FT /note="Missing (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="Missing (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 896..897
FT /note="EL -> DV (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="R -> G (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="A -> P (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1022
FT /note="S -> R (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="Q -> E (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1266..1267
FT /note="EH -> DD (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1533
FT /note="N -> D (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1548
FT /note="R -> G (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1726
FT /note="N -> G (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1736
FT /note="E -> Q (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="C -> S (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
FT CONFLICT 2040
FT /note="H -> L (in Ref. 1; AAA17886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2898 AA; 329465 MW; 50E66D93F7E4E283 CRC64;
MEDEQEQRRR KVEAGRAKLA NFRQRKTKGD CPNSKKKTAK RKGSAVHASV QEEGSVATPN
SELPQGGAVF ESPSCSNTLE GTRGASAAQE QEDCELDVTD LQGQQQTQPP PPQTAHSLEL
EALRLSLNNM HTAQLELTQA NLQKEKETAL TELREMLNGR RAQELALLQS RQQCELELLR
EQHAREKEEM ALRSGQEAAE LKEKLRSEME KNAQTIETLK QDWESERELC LENLRQELSL
KHQSEMEGLQ SQFQKELSEQ KVELEKIFQA KHEAEVSLKN LEAQHQAAIK KLQEDLQSEH
CQYLQDLEQK FREKEKAKEL ELETLQASYE DLKAQSQEEI RLLWSQLESM KTNREELNGS
WDPVLAQASH LEELEHLRSG FAQQQQQERA QHESELEHLR VYFEKKLKDA EKTYQEDLTV
FQQRLQEARE DSLESTEISS SCVLPEETSG REGKEPPDPL DLQLGQPKVQ ESLVEDCQVK
LSKAEEKIQQ MKEEFQKKEA EWELSREELK REAEERLASM FLELREKAES EKLSIISRFE
HRESSMRHLQ DQQAAQILDL ERSLMEQQGH LRQLEQELTR DDLLPCSQCG QEPAMAQEEK
NGALLREKED CALQLLMAQN RFLEERKEIM EKFAKEQDAF LRDAQEKHNH ELQLLQQGHQ
QQLLALRMEL ETKHRSELTE QLASSESRRQ ALLETHVAEL QVKHNAEISA LEKRHLSNLD
ELESCYVADV QTIRDEHQQA LELLRAELEE QLQKKESCHR EMLTQELENL KRQHAEELQS
VRDSLRMEMS AQHIENGKGP AADLQGAHQQ DPAMALHNEG HLLVEDGDAV LRSVDAEGLL
HQAGPQELGD AHTVEMQKSQ AELAKPQELQ ASQDQVAQVR DKVFLLNREL EECRAELEQL
QQRRERENQE GTTLICMLRA DLELAQGEGK ALRDALRRLL DLFGDTLKAA VTLKSRISER
AGLLLDHEDA ADTSDARLAA AALGDMWSDE GLLEIDRTLP EGAETSSVCE ISSHVCESFF
ISPENTLDCE QPIRRVYQSL STAVEGLLEM ALDSSKQLEE ARQLHRCVER EFRHRNEEMA
QAMQKQQELL ERLREESAAK DRLALELHTA KGLLEGFKVE KVDLQEALGK KEESEQQLIL
ELEDLRKQLQ QAARELLTLK EEKSVLWNQK ETLTNEAKER EAALQEEVES LTRVQWESRK
QSEKDRATLL SQMRVLESEL EDQLVQHRGC AQLAEEVATL KQQLAALDKH LRSQRQFMDD
QAAEREHERE EFQQEIQRLE GQLRQAARPR PPGPRDSQCV QLDEEVELLQ EKLREKLDGF
NELVIKKDFA DQQLLIQEEE IKRLEETNAS IQRQMVQLQE ELEKQKKSME ELKEKEILKQ
ENMGDLLLTT VSRSGLDEAG CPMLPQGSSS RGPEAQPDVT ERALLQHENE VVHRRNSEID
ELKSLIENLQ ENQRQLQKDK AEEIEQLHEV IEKLQSELSL MGPKVHEVSD PQAGSLHSEL
ACLRGEGLGG QALRSELQAA QAAKEVFGQL LANQAHGHSQ ALEALQQRLQ DAEEVAARHL
AELEHCVALR EAEVEAMASQ IQEFAATLKA KEAIIEQRDL EIDAVNKWKV SHSLELEAIL
LALAHFRHAL EQQTCATPDE PPELRQLRVQ CARLSHQLQV LYRPFLKCRM QLDQHQPHVA
SIGCANPCAD DELEQEGVSN RLALAPHSLA AQAKEELEDC PLGKANLMAQ VRQLQEELDH
RVHSVASRDT NSETCKLQQP NLSENGPRNH CCNGEESKPS PPDDVLNIAK TTWDVIDIIK
NQDLLVQVEM PDFPTQEKLT SQGGPFSSQA SGHSGSLLPE EAAEPQQDPV RALDLSSWSS
PEVVRKDPSL EPQHSLPLTP GVGTVSLHSV DISPDWTDPL LQADVSGLLC YPGKSASGQA
PLWAVAPSAG KHHAERTATE KDVEDFIVTS FDSQELLTSP SHELARRSDG SRKSDGPDIA
MMLTLGSEGS ETPTTDLVAA AAAAVPFSRR FVQSPGAMKE KEIHAKQMKA LLQMVFDESH
QILALSESQD PSSALNKGEP RDPLDGFPRD SQALSEVTTD KGEKESLETH LTWSEELLRA
IQEVFAREQE KAELQPRPYG SNLGDYNSLV QRLEKVIQEQ GDPQKVQDHL CLSDRSSLLA
EIQALRAQLR MTHLQNQEKL QQLCAALTST EARGSQREHQ LRRQVELLAY KVEQEKCIAN
ELQKTLSKEQ ETASDVRKRL VVEQNAVQDL KSELHACKQE NTSLLESLDK VQQEVLRLRA
VLDGKEKELK VVLEELESER GKGQALQAQQ EEQQLRYLQR EGQSSRALEE LKLSLEKQLA
QNNQLCVALK HERAAKDNLQ KELQIEASRC EALLAQEKGQ LSELQKSLEA ERSRSLELSE
ALQHERLLTE QLSRNSQEAC ARQETQVQHA LLRKLKAEKT RALELEAMLE KVQKQAAHTQ
QQLEAQAQER CVELRREKER ELEIQRQRDE HKIEQLQRLV RELRWKEEVS GGNGPCRGSP
GRGSLERDQF QEQQQELEKI RQQLLCAAGL LTSFTNHTVD RTIKDWTSSN EKAVSSLMRT
LEELKSELSM PTSFQKKMTA ELQVQLMNEL LSDNDALTKA VGMATREKAE LCRTVSRLEK
TLKHHTQKGC VLNRQSKSSL KQDGTDLQSS LRHSDPEWHS QTTSGDTNTC NIKMEKLYLH
YLRAESFRKA LIYQKKYLLL LIGGFQDSEQ ETLSMIAHLG VFPSKADKKI TMSRPFTKFR
TAVRVVIAVL RLRFLVKKWQ EVDRKGALVH PKSTRHGHRT SQRQRSPSGP RASLPTRDTS
SGPTKASRHS PRSAAAGSPG KERSTSTPSS RLERSLTASQ DPEHSLTEYI HHLEMIQQRL
GGLPPDSTQK SCHQKIKQ
