CCNO_HUMAN
ID CCNO_HUMAN Reviewed; 350 AA.
AC P22674; A8K1W5; Q0P6J2; Q9H6B0; Q9UMD5;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Cyclin-O {ECO:0000305};
GN Name=CCNO {ECO:0000312|HGNC:HGNC:18576};
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 [GENOMIC DNA / MRNA].
RC TISSUE=T-cell;
RX PubMed=2001396; DOI=10.1016/0167-4781(91)90055-q;
RA Muller S.J., Caradonna S.;
RT "Isolation and characterization of a human cDNA encoding uracil-DNA
RT glycosylase.";
RL Biochim. Biophys. Acta 1088:197-207(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Kidney epithelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [6]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8419333; DOI=10.1016/s0021-9258(18)54076-x;
RA Muller S.J., Caradonna S.;
RT "Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA
RT glycosylase.";
RL J. Biol. Chem. 268:1310-1319(1993).
RN [7]
RP IDENTIFICATION.
RX PubMed=16697536; DOI=10.1016/j.gene.2006.02.030;
RA Hirst R., Gosden R., Miller D.;
RT "The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its
RT relationship to human and chimpanzee homologues.";
RL Gene 375:95-102(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=28860486; DOI=10.1038/s41598-017-10770-8;
RA Gasa L., Sanchez-Botet A., Quandt E., Hernandez-Ortega S., Jimenez J.,
RA Carrasco-Garcia M.A., Simonetti S., Kron S.J., Ribeiro M.P., Nadal E.,
RA Villanueva A., Clotet J.;
RT "A systematic analysis of orphan cyclins reveals CNTD2 as a new oncogenic
RT driver in lung cancer.";
RL Sci. Rep. 7:10228-10228(2017).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=30087414; DOI=10.1038/s41598-018-30307-x;
RA Sanchez-Botet A., Gasa L., Quandt E., Hernandez-Ortega S., Jimenez J.,
RA Mezquita P., Carrasco-Garcia M.A., Kron S.J., Vidal A., Villanueva A.,
RA Ribeiro M.P.C., Clotet J.;
RT "The atypical cyclin CNTD2 promotes colon cancer cell proliferation and
RT migration.";
RL Sci. Rep. 8:11797-11797(2018).
RN [13]
RP VARIANT CILD29 ARG-239, INVOLVEMENT IN CILD29, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24747639; DOI=10.1038/ng.2961;
RA Wallmeier J., Al-Mutairi D.A., Chen C.T., Loges N.T., Pennekamp P.,
RA Menchen T., Ma L., Shamseldin H.E., Olbrich H., Dougherty G.W., Werner C.,
RA Alsabah B.H., Koehler G., Jaspers M., Boon M., Griese M., Schmitt-Grohe S.,
RA Zimmermann T., Koerner-Rettberg C., Horak E., Kintner C., Alkuraya F.S.,
RA Omran H.;
RT "Mutations in CCNO result in congenital mucociliary clearance disorder with
RT reduced generation of multiple motile cilia.";
RL Nat. Genet. 46:646-651(2014).
RN [14]
RP VARIANT CILD29 PRO-213, CHARACTERIZATION OF VARIANT CILD29, AND FUNCTION.
RX PubMed=26777464; DOI=10.1002/humu.22957;
RG Israeli PCD Consortium Investigators;
RA Amirav I., Wallmeier J., Loges N.T., Menchen T., Pennekamp P., Mussaffi H.,
RA Abitbul R., Avital A., Bentur L., Dougherty G.W., Nael E., Lavie M.,
RA Olbrich H., Werner C., Kintner C., Omran H.;
RT "Systematic analysis of CCNO variants in a defined population: implications
RT for clinical phenotype and differential diagnosis.";
RL Hum. Mutat. 37:396-405(2016).
CC -!- FUNCTION: Specifically required for generation of multiciliated cells,
CC possibly by promoting a cell cycle state compatible with centriole
CC amplification and maturation. Acts downstream of MCIDAS to promote
CC mother centriole amplification and maturation in preparation for apical
CC docking. {ECO:0000269|PubMed:24747639, ECO:0000269|PubMed:26777464}.
CC -!- INTERACTION:
CC P22674; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2556878, EBI-11741437;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24747639}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:28860486, ECO:0000269|PubMed:30087414}.
CC Note=Localizes to the apical part of cytoplasm.
CC {ECO:0000269|PubMed:24747639}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22674-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22674-2; Sequence=VSP_021655, VSP_021656;
CC -!- TISSUE SPECIFICITY: Present in respiratory cells (at protein level).
CC {ECO:0000269|PubMed:24747639}.
CC -!- DEVELOPMENTAL STAGE: Maximum levels during G(1) phase. Levels decrease
CC through S and G(2) phases. {ECO:0000269|PubMed:8419333}.
CC -!- DISEASE: Ciliary dyskinesia, primary, 29 (CILD29) [MIM:615872]: A
CC disorder characterized by abnormalities of motile cilia. Respiratory
CC infections leading to chronic inflammation and bronchiectasis are
CC recurrent, due to defects in the respiratory cilia. CILD29 patients do
CC not exhibit situs inversus, a congenital abnormality in which visceral
CC organs are opposite to their normal positions (situs solitus) due to
CC lateral transposition. {ECO:0000269|PubMed:24747639,
CC ECO:0000269|PubMed:26777464}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Marked reduction of cilia
CC in multiciliate cells due to defective mother centriole generation and
CC placement. Remaining cilia correctly express axonemal motor proteins,
CC are motile and do not show beating defects. Defects are probably caused
CC by a strong reduction in the number of multiple motile cilia covering
CC the cell surface in respiratory epithelial cells (PubMed:24747639).
CC {ECO:0000269|PubMed:24747639}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have uracil-DNA glycosylase (UDG)
CC activity and wrongly named UNG2 and UDG2 (PubMed:2001396). It was later
CC shown that it is a member of the cyclin family (PubMed:8419333). UNG2
CC corresponds to the isoform 2 of UNG gene. {ECO:0000305|PubMed:2001396,
CC ECO:0000305|PubMed:8419333}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB05817.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAA36728.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={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; X52486; CAA36728.1; ALT_SEQ; mRNA.
DR EMBL; M87499; AAB05817.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK026075; BAB15351.1; -; mRNA.
DR EMBL; AK290030; BAF82719.1; -; mRNA.
DR EMBL; AC026704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471123; EAW54913.1; -; Genomic_DNA.
DR EMBL; BC004877; AAH04877.1; -; mRNA.
DR CCDS; CCDS34157.1; -. [P22674-1]
DR PIR; S14266; S14266.
DR RefSeq; NP_066970.3; NM_021147.4. [P22674-1]
DR AlphaFoldDB; P22674; -.
DR SMR; P22674; -.
DR BioGRID; 115595; 26.
DR DIP; DIP-24234N; -.
DR IntAct; P22674; 6.
DR MINT; P22674; -.
DR STRING; 9606.ENSP00000282572; -.
DR BindingDB; P22674; -.
DR ChEMBL; CHEMBL4105895; -.
DR iPTMnet; P22674; -.
DR PhosphoSitePlus; P22674; -.
DR BioMuta; CCNO; -.
DR DMDM; 118572733; -.
DR jPOST; P22674; -.
DR MassIVE; P22674; -.
DR MaxQB; P22674; -.
DR PaxDb; P22674; -.
DR PeptideAtlas; P22674; -.
DR PRIDE; P22674; -.
DR ProteomicsDB; 54013; -. [P22674-1]
DR ProteomicsDB; 54014; -. [P22674-2]
DR Antibodypedia; 11078; 220 antibodies from 26 providers.
DR DNASU; 10309; -.
DR Ensembl; ENST00000282572.5; ENSP00000282572.4; ENSG00000152669.9. [P22674-1]
DR Ensembl; ENST00000501463.2; ENSP00000422485.1; ENSG00000152669.9. [P22674-2]
DR GeneID; 10309; -.
DR KEGG; hsa:10309; -.
DR MANE-Select; ENST00000282572.5; ENSP00000282572.4; NM_021147.5; NP_066970.3.
DR UCSC; uc003jpv.4; human. [P22674-1]
DR CTD; 10309; -.
DR DisGeNET; 10309; -.
DR GeneCards; CCNO; -.
DR GeneReviews; CCNO; -.
DR HGNC; HGNC:18576; CCNO.
DR HPA; ENSG00000152669; Tissue enhanced (choroid plexus, pancreas, testis).
DR MalaCards; CCNO; -.
DR MIM; 607752; gene.
DR MIM; 615872; phenotype.
DR neXtProt; NX_P22674; -.
DR OpenTargets; ENSG00000152669; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA38350; -.
DR VEuPathDB; HostDB:ENSG00000152669; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000155998; -.
DR HOGENOM; CLU_1926882_0_0_1; -.
DR InParanoid; P22674; -.
DR OMA; EHFTHAR; -.
DR OrthoDB; 752095at2759; -.
DR PhylomeDB; P22674; -.
DR TreeFam; TF332057; -.
DR BRENDA; 3.2.2.27; 2681.
DR PathwayCommons; P22674; -.
DR SignaLink; P22674; -.
DR BioGRID-ORCS; 10309; 6 hits in 1080 CRISPR screens.
DR GeneWiki; Cyclin_O; -.
DR GenomeRNAi; 10309; -.
DR Pharos; P22674; Tbio.
DR PRO; PR:P22674; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P22674; protein.
DR Bgee; ENSG00000152669; Expressed in oocyte and 115 other tissues.
DR Genevisible; P22674; HS.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
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:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR028864; Ccno.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF401; PTHR10177:SF401; 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; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Ciliopathy;
KW Cilium biogenesis/degradation; Cyclin; Cytoplasm; Disease variant; Nucleus;
KW Phosphoprotein; Primary ciliary dyskinesia; Reference proteome.
FT CHAIN 1..350
FT /note="Cyclin-O"
FT /id="PRO_0000176175"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 129..131
FT /note="TAE -> RCW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_021655"
FT VAR_SEQ 132..350
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_021656"
FT VARIANT 161
FT /note="L -> M (in dbSNP:rs13169396)"
FT /id="VAR_029081"
FT VARIANT 213
FT /note="L -> P (in CILD29; decreases formation of basal
FT bodies in multiciliated cells; dbSNP:rs775051461)"
FT /evidence="ECO:0000269|PubMed:26777464"
FT /id="VAR_077581"
FT VARIANT 239
FT /note="H -> R (in CILD29; dbSNP:rs797045150)"
FT /evidence="ECO:0000269|PubMed:24747639"
FT /id="VAR_071197"
FT CONFLICT 246
FT /note="E -> G (in Ref. 2; BAB15351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38096 MW; AF1C1D1C34334BED CRC64;
MVTPCPTSPS SPAARAGRRD NDQNLRAPVK KSRRPRLRRK QPLHPLNPCP LPGDSGICDL
FESPSSGSDG AESPSAARGG SPLPGPAQPV AQLDLQTFRD YGQSCYAFRK AQESHFHPRE
ALARQPQVTA ESRCKLLSWL IPVHRQFGLS FESLCLTVNT LDRFLTTTPV AADCFQLLGV
TSLLIACKQV EVHPPRVKQL LALCCGAFSR QQLCNLECIV LHKLHFTLGA PTISFFLEHF
THARVEAGQA EASEALEAQA LARGVAELSL ADYAFTSYSP SLLAICCLAL ADRMLRVSRP
VDLRLGDHPE AALEDCMGKL QLLVAINSTS LTHMLPVQIC EKCSLPPSSK
