TLK2_MOUSE
ID TLK2_MOUSE Reviewed; 718 AA.
AC O55047; B1ASU7; B1ASU8; Q9D5Y5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein kinase tousled-like 2;
DE EC=2.7.11.1;
DE AltName: Full=PKU-alpha;
DE AltName: Full=Tousled-like kinase 2;
GN Name=Tlk2; Synonyms=Tlk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB29570.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis {ECO:0000269|PubMed:10092119};
RX PubMed=10092119;
RX DOI=10.1002/(sici)1098-2795(199904)52:4<392::aid-mrd8>3.0.co;2-y;
RA Shalom S., Don J.;
RT "Tlk, a novel evolutionarily conserved murine serine threonine kinase,
RT encodes multiple testis transcripts.";
RL Mol. Reprod. Dev. 52:392-405(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10523312; DOI=10.1093/emboj/18.20.5691;
RA Sillje H.H.W., Takahashi K., Tanaka K., Van Houwe G., Nigg E.A.;
RT "Mammalian homologues of the plant tousled gene code for cell-cycle-
RT regulated kinases with maximal activities linked to ongoing DNA
RT replication.";
RL EMBO J. 18:5691-5702(1999).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH YWHAZ.
RX PubMed=10455159; DOI=10.1074/jbc.274.35.24865;
RA Zhang S., Xing H., Muslin A.J.;
RT "Nuclear localization of protein kinase U-alpha is regulated by 14-3-3.";
RL J. Biol. Chem. 274:24865-24872(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-99 (ISOFORM 2),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the process of
CC chromatin assembly and probably also DNA replication, transcription,
CC repair, and chromosome segregation. Phosphorylates the chromatin
CC assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its
CC proteasome-mediated degradation, thereby enhancing chromatin assembly
CC (By similarity). Negative regulator of amino acid starvation-induced
CC autophagy (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Testis-specific isoforms may play a role in spermatogenesis.
CC Highly expressed in embryos throughout development.
CC {ECO:0000269|PubMed:10092119}.
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 Evidence={ECO:0000250|UniProtKB:Q86UE8};
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; Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- ACTIVITY REGULATION: Cell cycle-regulated, with maximal activity in the
CC S-phase. Rapidly and transiently inhibited by phosphorylation following
CC the generation of DNA double-stranded breaks during S-phase, probably
CC by CHEK1, possibly at Ser-696. This inhibition is cell cycle
CC checkpoint- and ATM-dependent (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and heterodimer with TLK1. Interacts with ASF1A and
CC ASF1B. May also interact with FEZ1/LZTS1 and FEZ2 (By similarity).
CC Association with 14-3-3 proteins such as YWHAZ regulates subcellular
CC location. {ECO:0000250, ECO:0000269|PubMed:10455159}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10455159}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the
CC cytoplasmic intermediate filament system during the G1 phase of the
CC cell cycle. Present in the perinuclear region at S phase and in the
CC nucleus at late G2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000303|PubMed:10092119};
CC Name=1 {ECO:0000269|PubMed:10092119};
CC IsoId=O55047-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=O55047-2; Sequence=VSP_050575, VSP_050576;
CC Name=3 {ECO:0000269|PubMed:10092119};
CC IsoId=O55047-3; Sequence=VSP_050574;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined,
CC with high levels in heart and testis, in particular the pachytene
CC spermatocytes and in round spermatids. Some evidence for the existence
CC of a testis-specific isoform suggesting a role in spermatogenesis.
CC {ECO:0000269|PubMed:10092119, ECO:0000269|PubMed:10455159,
CC ECO:0000269|PubMed:10523312, ECO:0000303|PubMed:10092119}.
CC -!- PTM: Phosphorylated at Ser-696, probably by CHEK1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF045252; AAC02225.1; ALT_INIT; mRNA.
DR EMBL; AF045254; AAC02227.1; -; mRNA.
DR EMBL; AF045253; AAC02226.1; -; mRNA.
DR EMBL; AK014829; BAB29570.2; -; mRNA.
DR EMBL; AL645471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36356.2; -. [O55047-1]
DR CCDS; CCDS79062.1; -. [O55047-2]
DR RefSeq; NP_001281260.1; NM_001294331.1. [O55047-1]
DR RefSeq; NP_001281263.1; NM_001294334.1. [O55047-2]
DR RefSeq; XP_011247316.1; XM_011249014.2. [O55047-1]
DR AlphaFoldDB; O55047; -.
DR SMR; O55047; -.
DR BioGRID; 204893; 3.
DR IntAct; O55047; 1.
DR STRING; 10090.ENSMUSP00000102554; -.
DR iPTMnet; O55047; -.
DR PhosphoSitePlus; O55047; -.
DR EPD; O55047; -.
DR jPOST; O55047; -.
DR MaxQB; O55047; -.
DR PaxDb; O55047; -.
DR PeptideAtlas; O55047; -.
DR PRIDE; O55047; -.
DR ProteomicsDB; 259201; -. [O55047-1]
DR ProteomicsDB; 259202; -. [O55047-2]
DR ProteomicsDB; 259203; -. [O55047-3]
DR Antibodypedia; 31236; 373 antibodies from 31 providers.
DR DNASU; 24086; -.
DR Ensembl; ENSMUST00000015107; ENSMUSP00000015107; ENSMUSG00000020694. [O55047-1]
DR Ensembl; ENSMUST00000092537; ENSMUSP00000090198; ENSMUSG00000020694. [O55047-2]
DR Ensembl; ENSMUST00000106939; ENSMUSP00000102552; ENSMUSG00000020694. [O55047-1]
DR GeneID; 24086; -.
DR KEGG; mmu:24086; -.
DR UCSC; uc007lxd.3; mouse. [O55047-2]
DR UCSC; uc007lxg.3; mouse. [O55047-1]
DR CTD; 11011; -.
DR MGI; MGI:1346023; Tlk2.
DR VEuPathDB; HostDB:ENSMUSG00000020694; -.
DR eggNOG; KOG1151; Eukaryota.
DR GeneTree; ENSGT00950000182984; -.
DR HOGENOM; CLU_000288_85_1_1; -.
DR InParanoid; O55047; -.
DR OMA; FETQASS; -.
DR OrthoDB; 693214at2759; -.
DR PhylomeDB; O55047; -.
DR BioGRID-ORCS; 24086; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Tlk2; mouse.
DR PRO; PR:O55047; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O55047; protein.
DR Bgee; ENSMUSG00000020694; Expressed in undifferentiated genital tubercle and 259 other tissues.
DR ExpressionAtlas; O55047; baseline and differential.
DR Genevisible; O55047; MM.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; IPR027086; TLK2.
DR PANTHER; PTHR22974:SF20; PTHR22974:SF20; 2.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Chromatin regulator;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; DNA damage; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Spermatogenesis; Transferase.
FT CHAIN 1..718
FT /note="Serine/threonine-protein kinase tousled-like 2"
FT /id="PRO_0000086755"
FT DOMAIN 408..687
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 193..244
FT /evidence="ECO:0000255"
FT COILED 285..315
FT /evidence="ECO:0000255"
FT COILED 349..397
FT /evidence="ECO:0000255"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 414..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE8"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE8"
FT MOD_RES 696
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q86UE8"
FT VAR_SEQ 2..117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10092119"
FT /id="VSP_050574"
FT VAR_SEQ 89
FT /note="E -> EFAGGSGPGTSPGRSVPPVARSSPQHSLSNPLP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_050575"
FT VAR_SEQ 626..718
FT /note="PFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRID
FT VQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN -> VRKKAVEQPGAIPT
FT TSLGFFFAVNHWNPESSGLKKIQTSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_050576"
FT CONFLICT 520
FT /note="I -> M (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="K -> T (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="I -> T (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="K -> E (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="N -> D (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="N -> D (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="I -> M (in Ref. 2; BAB29570)"
FT /evidence="ECO:0000305"
FT MOD_RES O55047-2:94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES O55047-2:99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 718 AA; 82261 MW; 60009617C162BB05 CRC64;
MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV ETPEKKQNDQ
RNRKRKAEPY DTSQGKGTPR GHKISDYFER RAEQPLYGLD GSAAKEASEE QSALPTLMSV
MLAKPRLDTE QLAPRGAGLC FTFVSAQQNS PSSTGSGNTE HSCSSQKQIS IQHRQTQSDL
TIEKISALEN SKNSDLEKKE GRIDDLLRAN CDLRRQIDEQ QKMLEKYKER LNRCVTMSKK
LLIEKSKQEK MACRDKSMQD RLRLGHFTTV RHGASFTEQW TDGYAFQNLI KQQERINSQR
EEIERQRKML AKRKPPAMGQ APPATNEQKQ RKSKTNGAEN ETLTLAEYHE QEEIFKLRLG
HLKKEEAEIQ AELERLERVR NLHIRELKRI HNEDNSQFKD HPTLNDRYLL LHLLGRGGFS
EVYKAFDLTE QRYVAVKIHQ LNKNWRDEKK ENYHKHACRE YRIHKELDHP RIVKLYDYFS
LDTDSFCTVL EYCEGNDLDF YLKQHKLMSE KEARSIIMQI VNALKYLNEI KPPIIHYDLK
PGNILLVNGT ACGEIKITDF GLSKIMDDDS YNSVDGMELT SQGAGTYWYL PPECFVVGKE
PPKISNKVDV WSVGVIFYQC LYGRKPFGHN QSQQDILQEN TILKATEVQF PPKPVVTPEA
KAFIRRCLAY RKEDRIDVQQ LACDPYLLPH IRKSVSTSSP AGAAIASTSG ASNNSSSN
