TESK2_HUMAN
ID TESK2_HUMAN Reviewed; 571 AA.
AC Q96S53; Q5T422; Q5T423; Q8N520; Q9Y3Q6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Dual specificity testis-specific protein kinase 2;
DE EC=2.7.12.1;
DE AltName: Full=Testicular protein kinase 2;
GN Name=TESK2;
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 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10512679; DOI=10.1006/geno.1999.5922;
RA Rosok O., Pedeutour F., Ree A.H., Aasheim H.-C.;
RT "Identification and characterization of TESK2, a novel member of the
RT LIMK/TESK family of protein kinases, predominantly expressed in testis.";
RL Genomics 61:44-54(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11418599; DOI=10.1074/jbc.m102988200;
RA Toshima J., Toshima J.Y., Takeuchi K., Mori R., Mizuno K.;
RT "Cofilin phosphorylation and actin reorganization activities of testicular
RT protein kinase 2 and its predominant expression in testicular Sertoli
RT cells.";
RL J. Biol. Chem. 276:31449-31458(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-11.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Dual specificity protein kinase activity catalyzing
CC autophosphorylation and phosphorylation of exogenous substrates on both
CC serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-
CC 3'. May play an important role in spermatogenesis.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Ser-219.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q96S53; P08238: HSP90AB1; NbExp=3; IntAct=EBI-1384110, EBI-352572;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q96S53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96S53-2; Sequence=VSP_004930;
CC Name=3;
CC IsoId=Q96S53-3; Sequence=VSP_004931;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis and prostate.
CC Found predominantly in non-germinal Sertoli cells.
CC {ECO:0000269|PubMed:10512679, ECO:0000269|PubMed:11418599}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ132545; CAB41970.1; -; mRNA.
DR EMBL; AB057597; BAB62909.1; -; mRNA.
DR EMBL; AK027573; BAG51348.1; -; mRNA.
DR EMBL; AL359540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06987.1; -; Genomic_DNA.
DR EMBL; BC033085; AAH33085.1; -; mRNA.
DR CCDS; CCDS41323.1; -. [Q96S53-1]
DR RefSeq; NP_001307729.1; NM_001320800.1.
DR RefSeq; NP_009101.2; NM_007170.2. [Q96S53-1]
DR RefSeq; XP_006710350.1; XM_006710287.2.
DR RefSeq; XP_011538799.1; XM_011540497.1.
DR AlphaFoldDB; Q96S53; -.
DR SMR; Q96S53; -.
DR BioGRID; 115689; 79.
DR IntAct; Q96S53; 31.
DR STRING; 9606.ENSP00000361158; -.
DR BindingDB; Q96S53; -.
DR ChEMBL; CHEMBL2069163; -.
DR GuidetoPHARMACOLOGY; 2240; -.
DR iPTMnet; Q96S53; -.
DR PhosphoSitePlus; Q96S53; -.
DR BioMuta; TESK2; -.
DR DMDM; 25009462; -.
DR EPD; Q96S53; -.
DR jPOST; Q96S53; -.
DR MassIVE; Q96S53; -.
DR PaxDb; Q96S53; -.
DR PeptideAtlas; Q96S53; -.
DR PRIDE; Q96S53; -.
DR ProteomicsDB; 78067; -. [Q96S53-1]
DR ProteomicsDB; 78068; -. [Q96S53-2]
DR ProteomicsDB; 78069; -. [Q96S53-3]
DR Antibodypedia; 32628; 318 antibodies from 32 providers.
DR DNASU; 10420; -.
DR Ensembl; ENST00000372084.5; ENSP00000361156.1; ENSG00000070759.17. [Q96S53-3]
DR Ensembl; ENST00000372086.4; ENSP00000361158.3; ENSG00000070759.17. [Q96S53-1]
DR GeneID; 10420; -.
DR KEGG; hsa:10420; -.
DR MANE-Select; ENST00000372086.4; ENSP00000361158.3; NM_007170.3; NP_009101.2.
DR UCSC; uc001cns.2; human. [Q96S53-1]
DR CTD; 10420; -.
DR DisGeNET; 10420; -.
DR GeneCards; TESK2; -.
DR HGNC; HGNC:11732; TESK2.
DR HPA; ENSG00000070759; Low tissue specificity.
DR MIM; 604746; gene.
DR neXtProt; NX_Q96S53; -.
DR OpenTargets; ENSG00000070759; -.
DR PharmGKB; PA36449; -.
DR VEuPathDB; HostDB:ENSG00000070759; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000158765; -.
DR HOGENOM; CLU_018577_1_0_1; -.
DR InParanoid; Q96S53; -.
DR OMA; PPYCRQR; -.
DR OrthoDB; 219904at2759; -.
DR PhylomeDB; Q96S53; -.
DR TreeFam; TF318014; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; Q96S53; -.
DR SignaLink; Q96S53; -.
DR SIGNOR; Q96S53; -.
DR BioGRID-ORCS; 10420; 10 hits in 1112 CRISPR screens.
DR ChiTaRS; TESK2; human.
DR GeneWiki; TESK2; -.
DR GenomeRNAi; 10420; -.
DR Pharos; Q96S53; Tchem.
DR PRO; PR:Q96S53; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96S53; protein.
DR Bgee; ENSG00000070759; Expressed in cartilage tissue and 144 other tissues.
DR Genevisible; Q96S53; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..571
FT /note="Dual specificity testis-specific protein kinase 2"
FT /id="PRO_0000086749"
FT DOMAIN 58..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 521..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 64..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 219
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCT9"
FT VAR_SEQ 116..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10512679"
FT /id="VSP_004930"
FT VAR_SEQ 265..293
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004931"
FT VARIANT 11
FT /note="G -> A (in a breast infiltrating ductal carcinoma
FT sample; somatic mutation; dbSNP:rs1428512439)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041214"
FT CONFLICT 455
FT /note="R -> C (in Ref. 6; AAH33085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 63639 MW; D83B0E58321A46FA CRC64;
MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF SRLTRLDDFT
CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK EVQLMNRLSH PNILRFMGVC
VHQGQLHALT EYINSGNLEQ LLDSNLHLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK
NCLIKRDENG YSAVVADFGL AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF
SYGIILCEII ARIQADPDYL PRTENFGLDY DAFQHMVGDC PPDFLQLTFN CCNMDPKLRP
SFVEIGKTLE EILSRLQEEE QERDRKLQPT ARGLLEKAPG VKRLSSLDDK IPHKSPCPRR
TIWLSRSQSD IFSRKPPRTV SVLDPYYRPR DGAARTPKVN PFSARQDLMG GKIKFFDLPS
KSVISLVFDL DAPGPGTMPL ADWQEPLAPP IRRWRSLPGS PEFLHQEACP FVGREESLSD
GPPPRLSSLK YRVKEIPPFR ASALPAAQAH EAMDCSILQE ENGFGSRPQG TSPCPAGASE
EMEVEERPAG STPATFSTSG IGLQTQGKQD G
