WEE2_HUMAN
ID WEE2_HUMAN Reviewed; 567 AA.
AC P0C1S8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Wee1-like protein kinase 2;
DE EC=2.7.10.2;
DE AltName: Full=Wee1-like protein kinase 1B;
DE AltName: Full=Wee1B kinase;
GN Name=WEE2; Synonyms=WEE1B;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11029659; DOI=10.1046/j.1365-2443.2000.00367.x;
RA Nakanishi M., Ando H., Watanabe N., Kitamura K., Ito K., Okayama H.,
RA Miyamoto T., Agui T., Sasaki M.;
RT "Identification and characterization of human Wee1B, a new member of the
RT Wee1 family of Cdk-inhibitory kinases.";
RL Genes Cells 5:839-847(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
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 [4]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-8; LYS-332; HIS-398; GLU-470 AND
RP ASP-526.
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).
RN [5]
RP INVOLVEMENT IN OOMD5, VARIANT OOMD5 HIS-234, CHARACTERIZATION OF VARIANT
RP OOMD5 HIS-234, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RX PubMed=29606300; DOI=10.1016/j.ajhg.2018.02.015;
RA Sang Q., Li B., Kuang Y., Wang X., Zhang Z., Chen B., Wu L., Lyu Q., Fu Y.,
RA Yan Z., Mao X., Xu Y., Mu J., Li Q., Jin L., He L., Wang L.;
RT "Homozygous Mutations in WEE2 Cause Fertilization Failure and Female
RT Infertility.";
RL Am. J. Hum. Genet. 102:649-657(2018).
CC -!- FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates
CC and inhibits CDK1/CDC2 and acts as a key regulator of meiosis during
CC both prophase I and metaphase II (PubMed:29606300). Required to
CC maintain meiotic arrest in oocytes during the germinal vesicle (GV)
CC stage, a long period of quiescence at dictyate prophase I, by
CC phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and
CC prevent meiotic reentry. Also required for metaphase II exit during egg
CC activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from
CC meiosis in oocytes and promote pronuclear formation (By similarity).
CC {ECO:0000250|UniProtKB:Q66JT0, ECO:0000269|PubMed:29606300}.
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11029659,
CC ECO:0000269|PubMed:29606300}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level)
CC (PubMed:29606300). May also be expressed in testis (PubMed:11029659).
CC {ECO:0000269|PubMed:11029659, ECO:0000269|PubMed:29606300}.
CC -!- PTM: Phosphorylated on serine residues (PubMed:29606300).
CC Phosphorylation leads to increase its activity (By similarity).
CC {ECO:0000250|UniProtKB:Q66JT0, ECO:0000269|PubMed:29606300}.
CC -!- DISEASE: Oocyte maturation defect 5 (OOMD5) [MIM:617996]: An autosomal
CC recessive infertility disorder characterized by oocyte inability to
CC exit metaphase II, resulting in fertilization failure.
CC {ECO:0000269|PubMed:29606300}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK131218; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43660.1; -.
DR RefSeq; NP_001099028.1; NM_001105558.1.
DR PDB; 5VDK; X-ray; 2.70 A; A=202-492.
DR PDBsum; 5VDK; -.
DR AlphaFoldDB; P0C1S8; -.
DR SMR; P0C1S8; -.
DR BioGRID; 138978; 1.
DR STRING; 9606.ENSP00000380675; -.
DR BindingDB; P0C1S8; -.
DR ChEMBL; CHEMBL5095; -.
DR DrugCentral; P0C1S8; -.
DR iPTMnet; P0C1S8; -.
DR PhosphoSitePlus; P0C1S8; -.
DR BioMuta; WEE2; -.
DR DMDM; 254763343; -.
DR MassIVE; P0C1S8; -.
DR PaxDb; P0C1S8; -.
DR PeptideAtlas; P0C1S8; -.
DR PRIDE; P0C1S8; -.
DR Antibodypedia; 32491; 112 antibodies from 24 providers.
DR DNASU; 494551; -.
DR Ensembl; ENST00000397541.6; ENSP00000380675.2; ENSG00000214102.7.
DR Ensembl; ENST00000574659.5; ENSP00000459392.1; ENSG00000263042.5.
DR GeneID; 494551; -.
DR KEGG; hsa:494551; -.
DR MANE-Select; ENST00000397541.6; ENSP00000380675.2; NM_001105558.1; NP_001099028.1.
DR UCSC; uc003vwn.2; human.
DR CTD; 494551; -.
DR DisGeNET; 494551; -.
DR GeneCards; WEE2; -.
DR HGNC; HGNC:19684; WEE2.
DR HPA; ENSG00000214102; Not detected.
DR MalaCards; WEE2; -.
DR MIM; 614084; gene.
DR MIM; 617996; phenotype.
DR neXtProt; NX_P0C1S8; -.
DR OpenTargets; ENSG00000214102; -.
DR Orphanet; 488191; Female infertility due to oocyte meiotic arrest.
DR PharmGKB; PA134909633; -.
DR VEuPathDB; HostDB:ENSG00000214102; -.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000158803; -.
DR HOGENOM; CLU_000288_25_1_1; -.
DR InParanoid; P0C1S8; -.
DR OMA; GAAWHHI; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; P0C1S8; -.
DR TreeFam; TF101088; -.
DR PathwayCommons; P0C1S8; -.
DR SignaLink; P0C1S8; -.
DR BioGRID-ORCS; 494551; 11 hits in 1096 CRISPR screens.
DR GenomeRNAi; 494551; -.
DR Pharos; P0C1S8; Tchem.
DR PRO; PR:P0C1S8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P0C1S8; protein.
DR Bgee; ENSG00000214102; Expressed in ganglionic eminence and 82 other tissues.
DR ExpressionAtlas; P0C1S8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007143; P:female meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0035038; P:female pronucleus assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0080154; P:regulation of fertilization; IEA:Ensembl.
DR GO; GO:0060631; P:regulation of meiosis I; ISS:UniProtKB.
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 InterPro; IPR017164; Wee1-like_protein_kinase.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037281; Wee1-like_protein_kinase; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Disease variant; Kinase; Magnesium;
KW Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..567
FT /note="Wee1-like protein kinase 2"
FT /id="PRO_0000248079"
FT DOMAIN 212..486
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 494..519
FT /evidence="ECO:0000255"
FT MOTIF 173..175
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 315..329
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 218..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A4PES0"
FT VARIANT 8
FT /note="K -> T (in dbSNP:rs35672788)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041304"
FT VARIANT 234
FT /note="D -> H (in OOMD5; decreased WEE2 phosphorylation at
FT serine residues; decreased CDK1/CDC2 phosphorylation at 'Y-
FT 15'; dbSNP:rs1554415096)"
FT /evidence="ECO:0000269|PubMed:29606300"
FT /id="VAR_080992"
FT VARIANT 332
FT /note="N -> K (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041305"
FT VARIANT 398
FT /note="R -> H (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs200610853)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041306"
FT VARIANT 470
FT /note="D -> E (in dbSNP:rs55901099)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041307"
FT VARIANT 526
FT /note="Y -> D (in dbSNP:rs35683659)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041308"
FT CONFLICT 351
FT /note="M -> V (in Ref. 2; AK131218)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="H -> Y (in Ref. 2; AK131218)"
FT /evidence="ECO:0000305"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5VDK"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 313..332
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:5VDK"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 413..428
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:5VDK"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:5VDK"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5VDK"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:5VDK"
SQ SEQUENCE 567 AA; 62925 MW; BC05DDFE96D87E3F CRC64;
MDDKDIDKEL RQKLNFSYCE ETEIEGQKKV EESREASSQT PEKGEVQDSE AKGTPPWTPL
SNVHELDTSS EKDKESPDQI LRTPVSHPLK CPETPAQPDS RSKLLPSDSP STPKTMLSRL
VISPTGKLPS RGPKHLKLTP APLKDEMTSL ALVNINPFTP ESYKKLFLQS GGKRKIRGDL
EEAGPEEGKG GLPAKRCVLR ETNMASRYEK EFLEVEKIGV GEFGTVYKCI KRLDGCVYAI
KRSMKTFTEL SNENSALHEV YAHAVLGHHP HVVRYYSSWA EDDHMIIQNE YCNGGSLQAA
ISENTKSGNH FEEPKLKDIL LQISLGLNYI HNSSMVHLDI KPSNIFICHK MQSESSGVIE
EVENEADWFL SANVMYKIGD LGHATSINKP KVEEGDSRFL ANEILQEDYR HLPKADIFAL
GLTIAVAAGA ESLPTNGAAW HHIRKGNFPD VPQELSESFS SLLKNMIQPD AEQRPSAAAL
ARNTVLRPSL GKTEELQQQL NLEKFKTATL ERELREAQQA QSPQGYTHHG DTGVSGTHTG
SRSTKRLVGG KSARSSSFTS GEREPLH
