ID   NEK8_HUMAN              Reviewed;         692 AA.
AC   Q86SG6; A6NIC5; Q14CL7; Q2M1S6; Q8NDH1;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Serine/threonine-protein kinase Nek8;
DE            EC=2.7.11.1;
DE   AltName: Full=Never in mitosis A-related kinase 8;
DE            Short=NimA-related protein kinase 8;
DE   AltName: Full=Nima-related protein kinase 12a;
GN   Name=NEK8; Synonyms=JCK, NEK12A;
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].
RA   Huang C.Q., Wu S.L., Yu L.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nedwidek M.N., Roig J., Lenz G., Avruch J.;
RT   "NIMA-family kinase Nek8 complete human coding region.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
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].
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 445-692.
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   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15019993; DOI=10.1016/j.gene.2003.12.002;
RA   Bowers A.J., Boylan J.F.;
RT   "Nek8, a NIMA family kinase member, is overexpressed in primary human
RT   breast tumors.";
RL   Gene 328:135-142(2004).
RN   [8]
RP   INVOLVEMENT IN RHPD2, FUNCTION, AND INTERACTION WITH NPHP3.
RX   PubMed=23418306; DOI=10.1093/hmg/ddt070;
RA   Frank V., Habbig S., Bartram M.P., Eisenberger T., Veenstra-Knol H.E.,
RA   Decker C., Boorsma R.A., Goebel H., Nuernberg G., Griessmann A., Franke M.,
RA   Borgal L., Kohli P., Voelker L.A., Doetsch J., Nuernberg P., Benzing T.,
RA   Bolz H.J., Johnson C., Gerkes E.H., Schermer B., Bergmann C.;
RT   "Mutations in NEK8 link multiple organ dysplasia with altered Hippo
RT   signalling and increased c-MYC expression.";
RL   Hum. Mol. Genet. 22:2177-2185(2013).
RN   [9]
RP   INTERACTION WITH ANKS6; INVS AND NPHP3.
RX   PubMed=23793029; DOI=10.1038/ng.2681;
RA   Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M., van Reeuwijk J.,
RA   Boehlke C., Schell C., Yasunaga T., Helmstadter M., Mergen M., Filhol E.,
RA   Boldt K., Horn N., Ueffing M., Otto E.A., Eisenberger T., Elting M.W.,
RA   van Wijk J.A., Bockenhauer D., Sebire N.J., Rittig S., Vyberg M., Ring T.,
RA   Pohl M., Pape L., Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C.,
RA   Grahammer F., Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J.,
RA   Roepman R., Saunier S., Walz G., Hildebrandt F., Bergmann C.,
RA   Lienkamp S.S.;
RT   "ANKS6 is a central component of a nephronophthisis module linking NEK8 to
RT   INVS and NPHP3.";
RL   Nat. Genet. 45:951-956(2013).
RN   [10]
RP   INTERACTION WITH ANKS3.
RX   PubMed=26188091; DOI=10.1016/j.bbrc.2015.07.063;
RA   Ramachandran H., Engel C., Mueller B., Dengjel J., Walz G., Yakulov T.A.;
RT   "Anks3 alters the sub-cellular localization of the Nek7 kinase.";
RL   Biochem. Biophys. Res. Commun. 464:901-907(2015).
RN   [11]
RP   VARIANTS NPHP9 PHE-330; TYR-425 AND PRO-497, CHARACTERIZATION OF VARIANTS
RP   NPHP9 PHE-330; TYR-425 AND PRO-497, AND SUBCELLULAR LOCATION.
RX   PubMed=18199800; DOI=10.1681/asn.2007040490;
RA   Otto E.A., Trapp M.L., Schultheiss U.T., Helou J., Quarmby L.M.,
RA   Hildebrandt F.;
RT   "NEK8 mutations affect ciliary and centrosomal localization and may cause
RT   nephronophthisis.";
RL   J. Am. Soc. Nephrol. 19:587-592(2008).
CC   -!- FUNCTION: Required for renal tubular integrity. May regulate local
CC       cytoskeletal structure in kidney tubule epithelial cells. May regulate
CC       ciliary biogenesis through targeting of proteins to the cilia (By
CC       similarity). Plays a role in organogenesis and is involved in the
CC       regulation of the Hippo signaling pathway. {ECO:0000250,
CC       ECO:0000269|PubMed:23418306}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with PKD2; may regulate PKD2 targeting to the cilium
CC       (By similarity). Component of a complex containing at least ANKS6,
CC       INVS, NEK8 and NPHP3 (PubMed:23418306, PubMed:23793029). ANKS6 may
CC       organize complex assembly by linking INVS and NPHP3 to NEK8 and INVS
CC       may target the complex to the proximal ciliary axoneme
CC       (PubMed:23418306, PubMed:23793029). Interacts with ANKS3
CC       (PubMed:26188091). {ECO:0000250|UniProtKB:Q91ZR4,
CC       ECO:0000269|PubMed:23418306, ECO:0000269|PubMed:23793029,
CC       ECO:0000269|PubMed:26188091}.
CC   -!- INTERACTION:
CC       Q86SG6; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1752987, EBI-10173507;
CC       Q86SG6; P54253: ATXN1; NbExp=3; IntAct=EBI-1752987, EBI-930964;
CC       Q86SG6; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1752987, EBI-352572;
CC       Q86SG6; P42858: HTT; NbExp=3; IntAct=EBI-1752987, EBI-466029;
CC       Q86SG6; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-1752987, EBI-11953846;
CC       Q86SG6; Q8WVJ2: NUDCD2; NbExp=3; IntAct=EBI-1752987, EBI-1052153;
CC       Q86SG6; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-1752987, EBI-12813389;
CC       Q86SG6; O76081-6: RGS20; NbExp=3; IntAct=EBI-1752987, EBI-10178530;
CC       Q86SG6; P15884: TCF4; NbExp=3; IntAct=EBI-1752987, EBI-533224;
CC       Q86SG6; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-1752987, EBI-5235829;
CC       Q86SG6; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-1752987, EBI-749955;
CC       Q86SG6; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-1752987, EBI-11525489;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18199800}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZR4}. Cell
CC       projection, cilium {ECO:0000269|PubMed:18199800}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:18199800}. Note=Predominantly cytoplasmic.
CC       Localizes to the proximal region of the primary cilium and is not
CC       observed in dividing cells. {ECO:0000250|UniProtKB:Q91ZR4}.
CC   -!- TISSUE SPECIFICITY: Highest expression in thyroid, adrenal gland and
CC       skin. Low levels in spleen, colon and uterus. Overexpressed in breast
CC       tumors, with highest expression in infiltrating ductal carcinomas and
CC       moderate levels in mucinous adenocarcinoma.
CC       {ECO:0000269|PubMed:15019993}.
CC   -!- DISEASE: Nephronophthisis 9 (NPHP9) [MIM:613824]: An autosomal
CC       recessive disorder resulting in end-stage renal disease. It is a
CC       progressive tubulo-interstitial kidney disorder histologically
CC       characterized by modifications of the tubules with thickening of the
CC       basement membrane, interstitial fibrosis and, in the advanced stages,
CC       medullary cysts. {ECO:0000269|PubMed:18199800}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Renal-hepatic-pancreatic dysplasia 2 (RHPD2) [MIM:615415]: A
CC       form of renal-hepatic-pancreatic dysplasia, a disease characterized by
CC       cystic malformations of the kidneys, liver, and pancreas. The
CC       pathological findings consist of multicystic dysplastic kidneys,
CC       dilated and dysgenetic bile ducts, a dysplastic pancreas with dilated
CC       ducts, cysts, fibrosis and inflammatory infiltrates.
CC       {ECO:0000269|PubMed:23418306}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR   EMBL; AY242354; AAO88243.1; -; mRNA.
DR   EMBL; AY267371; AAP04006.1; -; mRNA.
DR   EMBL; AC010761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471159; EAW51136.1; -; Genomic_DNA.
DR   EMBL; BC112240; AAI12241.1; -; mRNA.
DR   EMBL; BC113705; AAI13706.1; -; mRNA.
DR   EMBL; AL833909; CAD38765.1; -; mRNA.
DR   CCDS; CCDS32597.1; -.
DR   RefSeq; NP_835464.1; NM_178170.2.
DR   AlphaFoldDB; Q86SG6; -.
DR   SMR; Q86SG6; -.
DR   BioGRID; 129755; 63.
DR   CORUM; Q86SG6; -.
DR   IntAct; Q86SG6; 64.
DR   STRING; 9606.ENSP00000268766; -.
DR   BindingDB; Q86SG6; -.
DR   ChEMBL; CHEMBL2417353; -.
DR   iPTMnet; Q86SG6; -.
DR   PhosphoSitePlus; Q86SG6; -.
DR   BioMuta; NEK8; -.
DR   DMDM; 34098463; -.
DR   jPOST; Q86SG6; -.
DR   MassIVE; Q86SG6; -.
DR   PaxDb; 9606-ENSP00000268766; -.
DR   PeptideAtlas; Q86SG6; -.
DR   ProteomicsDB; 69588; -.
DR   Pumba; Q86SG6; -.
DR   Antibodypedia; 26547; 310 antibodies from 26 providers.
DR   DNASU; 284086; -.
DR   Ensembl; ENST00000268766.11; ENSP00000268766.6; ENSG00000160602.14.
DR   GeneID; 284086; -.
DR   KEGG; hsa:284086; -.
DR   MANE-Select; ENST00000268766.11; ENSP00000268766.6; NM_178170.3; NP_835464.1.
DR   UCSC; uc002hcp.4; human.
DR   AGR; HGNC:13387; -.
DR   CTD; 284086; -.
DR   DisGeNET; 284086; -.
DR   GeneCards; NEK8; -.
DR   GeneReviews; NEK8; -.
DR   HGNC; HGNC:13387; NEK8.
DR   HPA; ENSG00000160602; Low tissue specificity.
DR   MalaCards; NEK8; -.
DR   MIM; 609799; gene.
DR   MIM; 613824; phenotype.
DR   MIM; 615415; phenotype.
DR   neXtProt; NX_Q86SG6; -.
DR   OpenTargets; ENSG00000160602; -.
DR   Orphanet; 93591; Infantile nephronophthisis.
DR   Orphanet; 294415; Renal-hepatic-pancreatic dysplasia.
DR   PharmGKB; PA38361; -.
DR   VEuPathDB; HostDB:ENSG00000160602; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   GeneTree; ENSGT00940000159297; -.
DR   HOGENOM; CLU_000288_123_1_1; -.
DR   InParanoid; Q86SG6; -.
DR   OrthoDB; 198307at2759; -.
DR   PhylomeDB; Q86SG6; -.
DR   TreeFam; TF106472; -.
DR   PathwayCommons; Q86SG6; -.
DR   SignaLink; Q86SG6; -.
DR   SIGNOR; Q86SG6; -.
DR   BioGRID-ORCS; 284086; 18 hits in 1190 CRISPR screens.
DR   GeneWiki; NEK8; -.
DR   GenomeRNAi; 284086; -.
DR   Pharos; Q86SG6; Tchem.
DR   PRO; PR:Q86SG6; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q86SG6; Protein.
DR   Bgee; ENSG00000160602; Expressed in buccal mucosa cell and 133 other cell types or tissues.
DR   ExpressionAtlas; Q86SG6; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR   GO; GO:0097543; C:ciliary inversin compartment; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; IMP:CACAO.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0035330; P:regulation of hippo signaling; IDA:UniProtKB.
DR   CDD; cd08220; STKc_Nek8; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR044120; STKc_Nek8.
DR   PANTHER; PTHR44535; PROTEIN CBG16200; 1.
DR   PANTHER; PTHR44535:SF4; SERINE_THREONINE-PROTEIN KINASE NEK8; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00415; RCC1; 4.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50012; RCC1_3; 5.
DR   Genevisible; Q86SG6; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Ciliopathy; Cilium; Cytoplasm; Cytoskeleton;
KW   Disease variant; Kinase; Magnesium; Metal-binding; Nephronophthisis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..692
FT                   /note="Serine/threonine-protein kinase Nek8"
FT                   /id="PRO_0000086432"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          312..350
FT                   /note="RCC1 1"
FT   REPEAT          410..461
FT                   /note="RCC1 2"
FT   REPEAT          462..513
FT                   /note="RCC1 3"
FT   REPEAT          580..631
FT                   /note="RCC1 4"
FT   REPEAT          632..684
FT                   /note="RCC1 5"
FT   REGION          277..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         162
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   VARIANT         330
FT                   /note="L -> F (in NPHP9; a full-length mouse NEK8 construct
FT                   containing the mutation shows a defect in ciliary
FT                   localization with no apparent effect on ciliation, mitosis
FT                   or centriole number; dbSNP:rs199962228)"
FT                   /evidence="ECO:0000269|PubMed:18199800"
FT                   /id="VAR_065769"
FT   VARIANT         425
FT                   /note="H -> Y (in NPHP9; a full-length mouse NEK8 construct
FT                   containing the mutation shows a defect in ciliary
FT                   localization with no apparent effect on ciliation, mitosis
FT                   or centriole number; dbSNP:rs118204032)"
FT                   /evidence="ECO:0000269|PubMed:18199800"
FT                   /id="VAR_065770"
FT   VARIANT         497
FT                   /note="A -> P (in NPHP9; a full-length mouse NEK8 construct
FT                   containing the mutation shows a defect in ciliary
FT                   localization with no apparent effect on ciliation, mitosis
FT                   or centriole number; dbSNP:rs146326420)"
FT                   /evidence="ECO:0000269|PubMed:18199800"
FT                   /id="VAR_065771"
SQ   SEQUENCE   692 AA;  74806 MW;  9E09820DFB3D5CA1 CRC64;
     MEKYERIRVV GRGAFGIVHL CLRKADQKLV IIKQIPVEQM TKEERQAAQN ECQVLKLLNH
     PNVIEYYENF LEDKALMIAM EYAPGGTLAE FIQKRCNSLL EEETILHFFV QILLALHHVH
     THLILHRDLK TQNILLDKHR MVVKIGDFGI SKILSSKSKA YTVVGTPCYI SPELCEGKPY
     NQKSDIWALG CVLYELASLK RAFEAANLPA LVLKIMSGTF APISDRYSPE LRQLVLSLLS
     LEPAQRPPLS HIMAQPLCIR ALLNLHTDVG SVRMRRAEKS VAPSNTGSRT TSVRCRGIPR
     GPVRPAIPPP LSSVYAWGGG LGTPLRLPML NTEVVQVAAG RTQKAGVTRS GRLILWEAPP
     LGAGGGSLLP GAVEQPQPQF ISRFLEGQSG VTIKHVACGD FFTACLTDRG IIMTFGSGSN
     GCLGHGSLTD ISQPTIVEAL LGYEMVQVAC GASHVLALST ERELFAWGRG DSGRLGLGTR
     ESHSCPQQVP MPPGQEAQRV VCGIDSSMIL TVPGQALACG SNRFNKLGLD HLSLGEEPVP
     HQQVEEALSF TLLGSAPLDQ EPLLSIDLGT AHSAAVTASG DCYTFGSNQH GQLGTNTRRG
     SRAPCKVQGL EGIKMAMVAC GDAFTVAIGA ESEVYSWGKG ARGRLGRRDE DAGLPRPVQL
     DETHPYTVTS VSCCHGNTLL AVRSVTDEPV PP
//