STK31_HUMAN
ID STK31_HUMAN Reviewed; 1019 AA.
AC Q9BXU1; B4DZ06; B7WPP5; C9J4F9; Q6PCD3; Q9BXH8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Serine/threonine-protein kinase 31;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase NYD-SPK;
DE AltName: Full=Sugen kinase 396;
DE Short=SgK396;
GN Name=STK31; Synonyms=SGK396;
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=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Zhou Z.M.;
RT "Cloning of a new protein kinase gene related to human testis
RT development.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-71.
RC TISSUE=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-71; PHE-125; LYS-261; ASN-268; LYS-277;
RP THR-393; GLU-410; PRO-489; THR-600; LYS-621; ILE-623; ARG-684; TYR-684;
RP LYS-709; LEU-860; MET-1000 AND SER-1010.
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BXU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXU1-2; Sequence=VSP_024389;
CC Name=3;
CC IsoId=Q9BXU1-3; Sequence=VSP_045210;
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Ser-854 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AF285599; AAK31978.1; -; mRNA.
DR EMBL; AF332194; AAK17193.1; -; mRNA.
DR EMBL; AK302689; BAG63918.1; -; mRNA.
DR EMBL; AC003087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059374; AAH59374.1; -; mRNA.
DR CCDS; CCDS43556.1; -. [Q9BXU1-2]
DR CCDS; CCDS5386.1; -. [Q9BXU1-1]
DR CCDS; CCDS59049.1; -. [Q9BXU1-3]
DR RefSeq; NP_001247433.1; NM_001260504.1. [Q9BXU1-2]
DR RefSeq; NP_001247434.1; NM_001260505.1. [Q9BXU1-3]
DR RefSeq; NP_113602.2; NM_031414.4. [Q9BXU1-1]
DR RefSeq; NP_116562.2; NM_032944.3. [Q9BXU1-2]
DR AlphaFoldDB; Q9BXU1; -.
DR BioGRID; 121097; 10.
DR IntAct; Q9BXU1; 6.
DR MINT; Q9BXU1; -.
DR STRING; 9606.ENSP00000348132; -.
DR BindingDB; Q9BXU1; -.
DR ChEMBL; CHEMBL6151; -.
DR GuidetoPHARMACOLOGY; 2220; -.
DR GlyGen; Q9BXU1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXU1; -.
DR PhosphoSitePlus; Q9BXU1; -.
DR BioMuta; STK31; -.
DR DMDM; 143811463; -.
DR MassIVE; Q9BXU1; -.
DR MaxQB; Q9BXU1; -.
DR PaxDb; Q9BXU1; -.
DR PeptideAtlas; Q9BXU1; -.
DR PRIDE; Q9BXU1; -.
DR ProteomicsDB; 5561; -.
DR ProteomicsDB; 79517; -. [Q9BXU1-1]
DR ProteomicsDB; 79518; -. [Q9BXU1-2]
DR Antibodypedia; 12132; 240 antibodies from 29 providers.
DR DNASU; 56164; -.
DR Ensembl; ENST00000354639.7; ENSP00000346660.3; ENSG00000196335.13. [Q9BXU1-2]
DR Ensembl; ENST00000355870.8; ENSP00000348132.3; ENSG00000196335.13. [Q9BXU1-1]
DR Ensembl; ENST00000433467.6; ENSP00000411852.2; ENSG00000196335.13. [Q9BXU1-3]
DR GeneID; 56164; -.
DR KEGG; hsa:56164; -.
DR MANE-Select; ENST00000355870.8; ENSP00000348132.3; NM_031414.5; NP_113602.2.
DR UCSC; uc003sws.6; human. [Q9BXU1-1]
DR CTD; 56164; -.
DR DisGeNET; 56164; -.
DR GeneCards; STK31; -.
DR HGNC; HGNC:11407; STK31.
DR HPA; ENSG00000196335; Tissue enriched (testis).
DR MIM; 605790; gene.
DR neXtProt; NX_Q9BXU1; -.
DR OpenTargets; ENSG00000196335; -.
DR PharmGKB; PA36214; -.
DR VEuPathDB; HostDB:ENSG00000196335; -.
DR eggNOG; ENOG502QPJA; Eukaryota.
DR GeneTree; ENSGT00390000007287; -.
DR HOGENOM; CLU_011956_0_0_1; -.
DR InParanoid; Q9BXU1; -.
DR OMA; HRAWNQQ; -.
DR OrthoDB; 104495at2759; -.
DR PhylomeDB; Q9BXU1; -.
DR TreeFam; TF105335; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9BXU1; -.
DR SignaLink; Q9BXU1; -.
DR BioGRID-ORCS; 56164; 13 hits in 1103 CRISPR screens.
DR GenomeRNAi; 56164; -.
DR Pharos; Q9BXU1; Tchem.
DR PRO; PR:Q9BXU1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BXU1; protein.
DR Bgee; ENSG00000196335; Expressed in right testis and 102 other tissues.
DR ExpressionAtlas; Q9BXU1; baseline and differential.
DR Genevisible; Q9BXU1; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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:0006468; P:protein phosphorylation; IEA:Ensembl.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1019
FT /note="Serine/threonine-protein kinase 31"
FT /id="PRO_0000086715"
FT DOMAIN 78..137
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 710..1019
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 298..355
FT /evidence="ECO:0000255"
FT BINDING 716..724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 737
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024389"
FT VAR_SEQ 921..943
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045210"
FT VARIANT 71
FT /note="Q -> H (in dbSNP:rs6945306)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_031600"
FT VARIANT 125
FT /note="S -> F (in dbSNP:rs56268851)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041150"
FT VARIANT 261
FT /note="E -> K (in dbSNP:rs10264952)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_031601"
FT VARIANT 268
FT /note="K -> N (in dbSNP:rs10264967)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_031602"
FT VARIANT 277
FT /note="I -> K (in dbSNP:rs55950645)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041151"
FT VARIANT 362
FT /note="T -> P (in dbSNP:rs35545265)"
FT /id="VAR_031603"
FT VARIANT 385
FT /note="R -> C (in dbSNP:rs35995607)"
FT /id="VAR_051675"
FT VARIANT 393
FT /note="A -> T (in dbSNP:rs56244148)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041152"
FT VARIANT 410
FT /note="G -> E (in dbSNP:rs4722266)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_031604"
FT VARIANT 489
FT /note="A -> P (in dbSNP:rs34414354)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041153"
FT VARIANT 600
FT /note="A -> T (in dbSNP:rs55796076)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041154"
FT VARIANT 621
FT /note="N -> K (in dbSNP:rs10263079)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041155"
FT VARIANT 623
FT /note="S -> I (in dbSNP:rs10247878)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041156"
FT VARIANT 684
FT /note="H -> R (in dbSNP:rs41273999)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041157"
FT VARIANT 684
FT /note="H -> Y (in a lung neuroendocrine carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041158"
FT VARIANT 709
FT /note="E -> K (in dbSNP:rs56181834)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041159"
FT VARIANT 860
FT /note="V -> L (in a lung small cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041160"
FT VARIANT 1000
FT /note="T -> M (in dbSNP:rs55794023)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041161"
FT VARIANT 1009
FT /note="K -> T (in dbSNP:rs33998018)"
FT /id="VAR_031605"
FT VARIANT 1010
FT /note="T -> S (in dbSNP:rs56391043)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041162"
FT CONFLICT 300
FT /note="I -> F (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="F -> Y (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 621..623
FT /note="NKS -> KKI (in Ref. 1; AAK31978)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="Y -> C (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="V -> A (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="K -> I (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="A -> G (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 1000
FT /note="T -> P (in Ref. 2; AAK17193)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="T -> P (in Ref. 1; AAK31978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1019 AA; 115694 MW; C2EFF005A820E102 CRC64;
MWVQGHSSRA SATESVSFSG IVQMDEDTHY DKVEDVVGSH IEDAVTFWAQ SINRNKDIMK
IGCSLSEVCP QASSVLGNLD PNKIYGGLFS EDQCWYRCKV LKIISVEKCL VRYIDYGNTE
ILNRSDIVEI PLELQFSSVA KKYKLWGLHI PSDQEVTQFD QGTTFLGSLI FEKEIKMRIK
ATSEDGTVIA QAEYGSVDIG EEVLKKGFAE KCRLASRTDI CEEKKLDPGQ LVLRNLKSPI
PLWGHRSNQS TFSRPKGHLS EKMTLDLKDE NDAGNLITFP KESLAVGDFN LGSNVSLEKI
KQDQKLIEEN EKLKTEKDAL LESYKALELK VEQIAQELQQ EKAAAVDLTN HLEYTLKTYI
DTRMKNLAAK MEILKEMRHV DISVRFGKDL SDAIQVLDEG CFTTPASLNG LEIIWAEYSL
AQENIKTCEY VSEGNILIAQ RNEMQQKLYM SVEDFILEVD ESSLNKRLKT LQDLSVSLEA
VYGQAKEGAN SDEILKKFYD WKCDKREEFT SVRSETDASL HRLVAWFQRT LKVFDLSVEG
SLISEDAMDN IDEILEKTES SVCKELEIAL VDQGDADKEI ISNTYSQVLQ KIHSEERLIA
TVQAKYKDSI EFKKQLIEYL NKSPSVDHLL SIKKTLKSLK ALLRWKLVEK SNLEESDDPD
GSQIEKIKEE ITQLRNNVFQ EIYHEREEYE MLTSLAQKWF PELPLLHPEI GLLKYMNSGG
LLTMSLERDL LDAEPMKELS SKRPLVRSEV NGQIILLKGY SVDVDTEAKV IERAATYHRA
WREAEGDSGL LPLIFLFLCK SDPMAYLMVP YYPRANLNAV QANMPLNSEE TLKVMKGVAQ
GLHTLHKADI IHGSLHQNNV FALNREQGIV GDFDFTKSVS QRASVNMMVG DLSLMSPELK
MGKPASPGSD LYAYGCLLLW LSVQNQEFEI NKDGIPKVDQ FHLDDKVKSL LCSLICYRSS
MTAEQVLNAE CFLMPKEQSV PNPEKDTEYT LYKKEEEIKT ENLDKCMEKT RNGEANFDC
