NEK8_HUMAN
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 03-AUG-2022, entry version 173.
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; 37.
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; Q86SG6; -.
DR PeptideAtlas; Q86SG6; -.
DR PRIDE; Q86SG6; -.
DR ProteomicsDB; 69588; -.
DR Antibodypedia; 26547; 295 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 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; 1062377at2759; -.
DR PhylomeDB; Q86SG6; -.
DR TreeFam; TF106472; -.
DR PathwayCommons; Q86SG6; -.
DR SignaLink; Q86SG6; -.
DR SIGNOR; Q86SG6; -.
DR BioGRID-ORCS; 284086; 17 hits in 1111 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 131 other tissues.
DR ExpressionAtlas; Q86SG6; baseline and differential.
DR Genevisible; Q86SG6; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0035330; P:regulation of hippo signaling; IDA:UniProtKB.
DR CDD; cd08220; STKc_Nek8; 1.
DR Gene3D; 2.130.10.30; -; 2.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 4.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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
