CCNB3_HUMAN
ID CCNB3_HUMAN Reviewed; 1395 AA.
AC Q8WWL7; B1AQI5; B1AQI6; Q96SB5; Q96SB6; Q96SB7; Q9NT38;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=G2/mitotic-specific cyclin-B3;
GN Name=CCNB3; Synonyms=CYCB3;
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, SUBCELLULAR LOCATION,
RP DOMAIN, TISSUE SPECIFICITY, MUTANT CYCB3XA, AND INTERACTION WITH CDK2.
RC TISSUE=Testis;
RX PubMed=12185076; DOI=10.1074/jbc.m203951200;
RA Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y.,
RA Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.;
RT "Characterization and expression of mammalian cyclin b3, a prepachytene
RT meiotic cyclin.";
RL J. Biol. Chem. 277:41960-41969(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11846420; DOI=10.1006/bbrc.2002.6458;
RA Lozano J.-C., Perret E., Schatt P., Arnould C., Peaucellier G., Picard A.;
RT "Molecular cloning, gene localization, and structure of human cyclin B3.";
RL Biochem. Biophys. Res. Commun. 291:406-413(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1249-1395 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] THR-597.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cyclins are positive regulatory subunits of the cyclin-
CC dependent kinases (CDKs), and thereby play an essential role in the
CC control of the cell cycle, notably via their destruction during cell
CC division. Its tissue specificity suggest that it may be required during
CC early meiotic prophase I. {ECO:0000269|PubMed:12185076}.
CC -!- SUBUNIT: Interacts with CDK2 kinase. {ECO:0000269|PubMed:12185076}.
CC -!- INTERACTION:
CC Q8WWL7; A8UKE6: CDK2; Xeno; NbExp=2; IntAct=EBI-767764, EBI-767796;
CC Q8WWL7; Q64702: Plk4; Xeno; NbExp=4; IntAct=EBI-767764, EBI-2552433;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12185076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WWL7-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 1;
CC IsoId=Q8WWL7-2; Sequence=VSP_010514;
CC Name=3; Synonyms=Variant 2;
CC IsoId=Q8WWL7-3; Sequence=VSP_010515;
CC -!- TISSUE SPECIFICITY: Testis specific. In testis, it is expressed in
CC developing germ cells, but not in Leydig cells. Weakly or not expressed
CC in other tissues. {ECO:0000269|PubMed:11846420,
CC ECO:0000269|PubMed:12185076}.
CC -!- DOMAIN: The N-terminal destruction box (D-box) probably acts as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000250}.
CC -!- PTM: Ubiquitinated (Probable). Ubiquitination leads to its degradation
CC during anaphase entry, after degradation of CCNB1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ416458; CAC94915.1; -; mRNA.
DR EMBL; AJ314764; CAC40024.1; -; mRNA.
DR EMBL; AJ314765; CAC40025.1; -; mRNA.
DR EMBL; AJ314766; CAC40026.1; -; mRNA.
DR EMBL; AL591367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX323840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471180; EAW89922.1; -; Genomic_DNA.
DR EMBL; CH471180; EAW89923.1; -; Genomic_DNA.
DR EMBL; AL137550; CAB70806.1; -; mRNA.
DR CCDS; CCDS14331.1; -. [Q8WWL7-1]
DR CCDS; CCDS14332.1; -. [Q8WWL7-2]
DR PIR; T46391; T46391.
DR RefSeq; NP_149020.2; NM_033031.2. [Q8WWL7-1]
DR RefSeq; NP_391990.1; NM_033670.2. [Q8WWL7-2]
DR RefSeq; XP_016885407.1; XM_017029918.1.
DR AlphaFoldDB; Q8WWL7; -.
DR SMR; Q8WWL7; -.
DR BioGRID; 124523; 8.
DR ComplexPortal; CPX-2009; Cyclin B3-CDK2 complex.
DR IntAct; Q8WWL7; 5.
DR MINT; Q8WWL7; -.
DR STRING; 9606.ENSP00000365210; -.
DR BindingDB; Q8WWL7; -.
DR ChEMBL; CHEMBL2094127; -.
DR DrugCentral; Q8WWL7; -.
DR iPTMnet; Q8WWL7; -.
DR PhosphoSitePlus; Q8WWL7; -.
DR BioMuta; CCNB3; -.
DR DMDM; 209572596; -.
DR EPD; Q8WWL7; -.
DR jPOST; Q8WWL7; -.
DR MassIVE; Q8WWL7; -.
DR PaxDb; Q8WWL7; -.
DR PeptideAtlas; Q8WWL7; -.
DR PRIDE; Q8WWL7; -.
DR ProteomicsDB; 74902; -. [Q8WWL7-1]
DR Antibodypedia; 421; 313 antibodies from 27 providers.
DR DNASU; 85417; -.
DR Ensembl; ENST00000276014.11; ENSP00000276014.7; ENSG00000147082.18. [Q8WWL7-1]
DR Ensembl; ENST00000348603.2; ENSP00000338682.2; ENSG00000147082.18. [Q8WWL7-2]
DR Ensembl; ENST00000376038.5; ENSP00000365206.1; ENSG00000147082.18. [Q8WWL7-2]
DR Ensembl; ENST00000376042.6; ENSP00000365210.1; ENSG00000147082.18. [Q8WWL7-1]
DR Ensembl; ENST00000476167.5; ENSP00000431645.1; ENSG00000147082.18. [Q8WWL7-3]
DR GeneID; 85417; -.
DR KEGG; hsa:85417; -.
DR MANE-Select; ENST00000376042.6; ENSP00000365210.1; NM_033031.3; NP_149020.2.
DR UCSC; uc004dox.5; human. [Q8WWL7-1]
DR CTD; 85417; -.
DR DisGeNET; 85417; -.
DR GeneCards; CCNB3; -.
DR HGNC; HGNC:18709; CCNB3.
DR HPA; ENSG00000147082; Group enriched (brain, epididymis, testis).
DR MalaCards; CCNB3; -.
DR MIM; 300456; gene.
DR neXtProt; NX_Q8WWL7; -.
DR OpenTargets; ENSG00000147082; -.
DR PharmGKB; PA38653; -.
DR VEuPathDB; HostDB:ENSG00000147082; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000160459; -.
DR HOGENOM; CLU_006366_0_0_1; -.
DR InParanoid; Q8WWL7; -.
DR OMA; EEPNAPC; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q8WWL7; -.
DR TreeFam; TF101001; -.
DR PathwayCommons; Q8WWL7; -.
DR SignaLink; Q8WWL7; -.
DR BioGRID-ORCS; 85417; 11 hits in 707 CRISPR screens.
DR ChiTaRS; CCNB3; human.
DR GenomeRNAi; 85417; -.
DR Pharos; Q8WWL7; Tbio.
DR PRO; PR:Q8WWL7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WWL7; protein.
DR Bgee; ENSG00000147082; Expressed in secondary oocyte and 98 other tissues.
DR Genevisible; Q8WWL7; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR015452; Cyclin_B3.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 2.
DR PANTHER; PTHR10177:SF214; PTHR10177:SF214; 2.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Meiosis; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1395
FT /note="G2/mitotic-specific cyclin-B3"
FT /id="PRO_0000080373"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..68
FT /note="D-box"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 69..1172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11846420"
FT /id="VSP_010514"
FT VAR_SEQ 112..1395
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11846420"
FT /id="VSP_010515"
FT VARIANT 597
FT /note="K -> T (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036580"
FT VARIANT 1001
FT /note="G -> R (in dbSNP:rs6614336)"
FT /id="VAR_047027"
FT MUTAGEN 60
FT /note="R->A: In cycB3XA; prevents its destruction after
FT completion of anaphase; when associated with A-63 and A-
FT 68."
FT MUTAGEN 63
FT /note="F->A: In cycB3XA; prevents its destruction after
FT completion of anaphase; when associated with A-60 and A-
FT 68."
FT MUTAGEN 68
FT /note="N->A: In cycB3XA; prevents its destruction after
FT completion of anaphase; when associated with A-60 and A-
FT 63."
FT CONFLICT 295
FT /note="K -> R (in Ref. 2; CAC40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> F (in Ref. 1; CAC94915)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="S -> P (in Ref. 2; CAC40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="R -> K (in Ref. 2; CAC40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="N -> S (in Ref. 2; CAC40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="K -> E (in Ref. 2; CAC40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="E -> K (in Ref. 1; CAC94915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1395 AA; 157916 MW; 454552BC5A67E34E CRC64;
MLLPLPPQSS KPVPKKSQSS KIVPSHHDPS EKTGENCQTK ISPSSLQESP SSLQGALKKR
SAFEDLTNAS QCQPVQPKKE ANKEFVKVVS KKINRNTHAL GLAKKNKRNL KWHKLEVTPV
VASTTVVPNI MEKPLILDIS TTSKTPNTEE ASLFRKPLVL KEEPTIEDET LINKSLSLKK
CSNHEEVSLL EKLQPLQEES DSDDAFVIEP MTFKKTHKTE EAAITKKTLS LKKKMCASQR
KQSCQEESLA VQDVNMEEDS FFMESMSFKK KPKTEESIPT HKLSSLKKKC TIYGKICHFR
KPPVLQTTIC GAMSSIKKPT TEKETLFQEL SVLQEKHTTE HEMSILKKSL ALQKTNFKED
SLVKESLAFK KKPSTEEAIM MPVILKEQCM TEGKRSRLKP LVLQEITSGE KSLIMKPLSI
KEKPSTEKES FSQEPSALQK KHTTQEEVSI LKEPSSLLKS PTEESPFDEA LAFTKKCTIE
EAPPTKKPLI LKRKHATQGT MSHLKKPLIL QTTSGEKSLI KEPLPFKEEK VSLKKKCTTQ
EMMSICPELL DFQDMIGEDK NSFFMEPMSF RKNPTTEETV LTKTSLSLQE KKITQGKMSH
LKKPLVLQKI TSEEESFYKK LLPFKMKSTT EEKFLSQEPS ALKEKHTTLQ EVSLSKESLA
IQEKATTEEE FSQELFSLHV KHTNKSGSLF QEALVLQEKT DAEEDSLKNL LALQEKSTME
EESLINKLLA LKEELSAEAA TNIQTQLSLK KKSTSHGKVF FLKKQLALNE TINEEEFLNK
QPLALEGYPS IAEGETLFKK LLAMQEEPSI EKEAVLKEPT IDTEAHFKEP LALQEEPSTE
KEAVLKEPSV DTEAHFKETL ALQEKPSIEQ EALFKRHSAL WEKPSTEKET IFKESLDLQE
KPSIKKETLL KKPLALKMST INEAVLFEDM IALNEKPTTG KELSFKEPLA LQESPTYKED
TFLKTLLVPQ VGTSPNVSST APESITSKSS IATMTSVGKS GTINEAFLFE DMITLNEKPT
TGKELSFKEP LALQESPTCK EDTFLETFLI PQIGTSPYVF STTPESITEK SSIATMTSVG
KSRTTTESSA CESASDKPVS PQAKGTPKEI TPREDIDEDS SDPSFNPMYA KEIFSYMKER
EEQFILTDYM NRQIEITSDM RAILVDWLVE VQVSFEMTHE TLYLAVKLVD LYLMKAVCKK
DKLQLLGATA FMIAAKFEEH NSPRVDDFVY ICDDNYQRSE VLSMEINILN VLKCDINIPI
AYHFLRRYAR CIHTNMKTLT LSRYICEMTL QEYHYVQEKA SKLAAASLLL ALYMKKLGYW
VPFLEHYSGY SISELHPLVR QLNKLLTFSS YDSLKAVYYK YSHPVFFEVA KIPALDMLKL
EEILNCDCEA QGLVL
