MOK_HUMAN
ID MOK_HUMAN Reviewed; 419 AA.
AC Q9UQ07; B2R6Z4; B7Z7P6; E7ER76; E7ERR8; Q92790; Q93067;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=MAPK/MAK/MRK overlapping kinase;
DE EC=2.7.11.22 {ECO:0000250|UniProtKB:Q9WVS4};
DE AltName: Full=MOK protein kinase;
DE AltName: Full=Renal tumor antigen 1;
DE Short=RAGE-1;
GN Name=MOK; Synonyms=RAGE, RAGE1;
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).
RC TISSUE=Fetal brain;
RX PubMed=10421840; DOI=10.1046/j.1365-2443.1999.00261.x;
RA Miyata Y., Akashi M., Nishida E.;
RT "Molecular cloning and characterization of a novel member of the MAP kinase
RT superfamily.";
RL Genes Cells 4:299-309(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Renal cell carcinoma;
RX PubMed=8781117; DOI=10.1007/bf02602776;
RA Gaugler B., Brouwenstijn N., Vantomme V., Szikora J.-P., Van der Spek C.W.,
RA Patard J.-J., Boon T., Schrier P., Van den Eynde B.J.;
RT "A new gene coding for an antigen recognized by autologous cytolytic T
RT lymphocytes on a human renal carcinoma.";
RL Immunogenetics 44:323-330(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT ILE-217.
RC TISSUE=Testis;
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=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, Lung, and Testis;
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 VARIANTS [LARGE SCALE ANALYSIS] HIS-38; ASN-86; ARG-230; SER-248; ASP-272
RP AND ARG-398.
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: Able to phosphorylate several exogenous substrates and to
CC undergo autophosphorylation. Negatively regulates cilium length in a
CC cAMP and mTORC1 signaling-dependent manner.
CC {ECO:0000250|UniProtKB:Q9WVS4}.
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=2.7.11.22;
CC Evidence={ECO:0000250|UniProtKB:Q9WVS4};
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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:Q9WVS4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9WVS4};
CC -!- ACTIVITY REGULATION: Phosphorylation appears to increase the enzymatic
CC activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9WVS4}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q9WVS4}. Nucleus
CC {ECO:0000250|UniProtKB:Q9WVS4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UQ07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQ07-2; Sequence=VSP_009144;
CC Name=3; Synonyms=RAGE-1 ORF5, RAGE-2 ORF5, RAGE-3 ORF5;
CC IsoId=Q9UQ07-3; Sequence=VSP_009143;
CC Name=4; Synonyms=RAGE-4 ORF3;
CC IsoId=Q9UQ07-4; Sequence=VSP_009142, VSP_009145, VSP_009146;
CC Name=5;
CC IsoId=Q9UQ07-5; Sequence=VSP_054734;
CC Name=6;
CC IsoId=Q9UQ07-6; Sequence=VSP_054735;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, kidney, and
CC pancreas, and at very low levels in placenta, liver and skeletal
CC muscle. Detected in retina.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38087.1; Type=Frameshift; 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; AB022694; BAA81688.1; -; mRNA.
DR EMBL; U46191; AAB38079.1; -; mRNA.
DR EMBL; U46192; AAB38082.1; -; mRNA.
DR EMBL; U46193; AAB38085.1; -; mRNA.
DR EMBL; U46194; AAB38087.1; ALT_FRAME; mRNA.
DR EMBL; AK302349; BAH13682.1; -; mRNA.
DR EMBL; AK312778; BAG35641.1; -; mRNA.
DR EMBL; AL352978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053536; AAH53536.1; -; mRNA.
DR CCDS; CCDS61552.1; -. [Q9UQ07-5]
DR CCDS; CCDS81854.1; -. [Q9UQ07-6]
DR CCDS; CCDS9971.1; -. [Q9UQ07-1]
DR RefSeq; NP_001258940.1; NM_001272011.1. [Q9UQ07-5]
DR RefSeq; NP_001317163.1; NM_001330234.1. [Q9UQ07-6]
DR RefSeq; NP_055041.1; NM_014226.2. [Q9UQ07-1]
DR AlphaFoldDB; Q9UQ07; -.
DR SMR; Q9UQ07; -.
DR BioGRID; 111828; 25.
DR IntAct; Q9UQ07; 14.
DR MINT; Q9UQ07; -.
DR STRING; 9606.ENSP00000355304; -.
DR BindingDB; Q9UQ07; -.
DR ChEMBL; CHEMBL4295983; -.
DR iPTMnet; Q9UQ07; -.
DR PhosphoSitePlus; Q9UQ07; -.
DR BioMuta; MOK; -.
DR EPD; Q9UQ07; -.
DR MassIVE; Q9UQ07; -.
DR PaxDb; Q9UQ07; -.
DR PeptideAtlas; Q9UQ07; -.
DR PRIDE; Q9UQ07; -.
DR TopDownProteomics; Q9UQ07-4; -. [Q9UQ07-4]
DR ABCD; Q9UQ07; 8 sequenced antibodies.
DR Antibodypedia; 27789; 436 antibodies from 33 providers.
DR DNASU; 5891; -.
DR Ensembl; ENST00000361847.7; ENSP00000355304.2; ENSG00000080823.23. [Q9UQ07-1]
DR Ensembl; ENST00000522874.5; ENSP00000429469.1; ENSG00000080823.23. [Q9UQ07-6]
DR Ensembl; ENST00000524214.5; ENSP00000428942.1; ENSG00000080823.23. [Q9UQ07-5]
DR GeneID; 5891; -.
DR KEGG; hsa:5891; -.
DR MANE-Select; ENST00000361847.7; ENSP00000355304.2; NM_014226.3; NP_055041.1.
DR UCSC; uc001ylm.5; human. [Q9UQ07-1]
DR CTD; 5891; -.
DR DisGeNET; 5891; -.
DR GeneCards; MOK; -.
DR HGNC; HGNC:9833; MOK.
DR HPA; ENSG00000080823; Tissue enhanced (retina, testis).
DR MIM; 605762; gene.
DR neXtProt; NX_Q9UQ07; -.
DR OpenTargets; ENSG00000080823; -.
DR PharmGKB; PA34187; -.
DR VEuPathDB; HostDB:ENSG00000080823; -.
DR eggNOG; KOG0661; Eukaryota.
DR GeneTree; ENSGT00940000159582; -.
DR InParanoid; Q9UQ07; -.
DR OMA; WQISKEG; -.
DR OrthoDB; 76933at2759; -.
DR PhylomeDB; Q9UQ07; -.
DR TreeFam; TF328769; -.
DR PathwayCommons; Q9UQ07; -.
DR SignaLink; Q9UQ07; -.
DR BioGRID-ORCS; 5891; 67 hits in 1103 CRISPR screens.
DR ChiTaRS; MOK; human.
DR GeneWiki; RAGE_(gene); -.
DR GenomeRNAi; 5891; -.
DR Pharos; Q9UQ07; Tbio.
DR PRO; PR:Q9UQ07; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UQ07; protein.
DR Bgee; ENSG00000080823; Expressed in right uterine tube and 129 other tissues.
DR ExpressionAtlas; Q9UQ07; baseline and differential.
DR Genevisible; Q9UQ07; HS.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..419
FT /note="MAPK/MAK/MRK overlapping kinase"
FT /id="PRO_0000086341"
FT DOMAIN 4..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 285..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..344
FT /note="Basic and acidic residues"
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 VAR_SEQ 1..346
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8781117"
FT /id="VSP_009143"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8781117"
FT /id="VSP_009142"
FT VAR_SEQ 42..71
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054734"
FT VAR_SEQ 138
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_054735"
FT VAR_SEQ 232..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009144"
FT VAR_SEQ 290..329
FT /note="KTEKRALGSHRKAGFPEHPVAPEPLSNSCQISKEGRKQKQ -> TQNGSEDE
FT ASAVLLPIQTRSSLNPLLSTCMLPGRSVTLLV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8781117"
FT /id="VSP_009145"
FT VAR_SEQ 330..419
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8781117"
FT /id="VSP_009146"
FT VARIANT 38
FT /note="R -> H (in dbSNP:rs34114580)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042011"
FT VARIANT 86
FT /note="D -> N (in dbSNP:rs34084056)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042012"
FT VARIANT 217
FT /note="V -> I (in dbSNP:rs148360666)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070930"
FT VARIANT 230
FT /note="K -> R (in dbSNP:rs34965156)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042013"
FT VARIANT 248
FT /note="P -> S (in dbSNP:rs34299975)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042014"
FT VARIANT 272
FT /note="E -> D (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation; dbSNP:rs1567133856)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042015"
FT VARIANT 398
FT /note="Q -> R (in dbSNP:rs2236493)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_024576"
FT CONFLICT 269
FT /note="D -> G (in Ref. 3; BAG35641)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="P -> L (in Ref. 3; BAG35641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48014 MW; CDA7D9C1E80AAE8F CRC64;
MKNYKAIGKI GEGTFSEVMK MQSLRDGNYY ACKQMKQRFE SIEQVNNLRE IQALRRLNPH
PNILMLHEVV FDRKSGSLAL ICELMDMNIY ELIRGRRYPL SEKKIMHYMY QLCKSLDHIH
RNGIFHRDVK PENILIKQDV LKLGDFGSCR SVYSKQPYTE YISTRWYRAP ECLLTDGFYT
YKMDLWSAGC VFYEIASLQP LFPGVNELDQ ISKIHDVIGT PAQKILTKFK QSRAMNFDFP
FKKGSGIPLL TTNLSPQCLS LLHAMVAYDP DERIAAHQAL QHPYFQEQRK TEKRALGSHR
KAGFPEHPVA PEPLSNSCQI SKEGRKQKQS LKQEEDRPKR RGPAYVMELP KLKLSGVVRL
SSYSSPTLQS VLGSGTNGRV PVLRPLKCIP ASKKTDPQKD LKPAPQQCRL PTIVRKGGR
