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   27-MAR-2024, entry version 175.
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}.
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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; 9.
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   GlyGen; Q8WWL7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WWL7; -.
DR   PhosphoSitePlus; Q8WWL7; -.
DR   BioMuta; CCNB3; -.
DR   DMDM; 209572596; -.
DR   EPD; Q8WWL7; -.
DR   jPOST; Q8WWL7; -.
DR   MassIVE; Q8WWL7; -.
DR   PaxDb; 9606-ENSP00000365210; -.
DR   PeptideAtlas; Q8WWL7; -.
DR   ProteomicsDB; 74902; -. [Q8WWL7-1]
DR   Antibodypedia; 421; 350 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   AGR; HGNC:18709; -.
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; 5474295at2759; -.
DR   PhylomeDB; Q8WWL7; -.
DR   TreeFam; TF101001; -.
DR   PathwayCommons; Q8WWL7; -.
DR   SignaLink; Q8WWL7; -.
DR   BioGRID-ORCS; 85417; 11 hits in 780 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 primordial germ cell in gonad and 100 other cell types or tissues.
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: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   CDD; cd20508; CYCLIN_CCNB3_rpt1; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF601; G2_MITOTIC-SPECIFIC CYCLIN-B3; 1.
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; Cyclin-like; 2.
DR   Genevisible; Q8WWL7; HS.
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
FT                   A-68."
FT   MUTAGEN         63
FT                   /note="F->A: In cycB3XA; prevents its destruction after
FT                   completion of anaphase; when associated with A-60 and
FT                   A-68."
FT   MUTAGEN         68
FT                   /note="N->A: In cycB3XA; prevents its destruction after
FT                   completion of anaphase; when associated with A-60 and
FT                   A-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
//