KDM3B_MOUSE
ID KDM3B_MOUSE Reviewed; 1762 AA.
AC Q6ZPY7; B9EKS2; Q2VPQ5; Q5U5V7; Q6P9K3; Q8CCE2; Q8K2A5; Q9CU57;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Lysine-specific demethylase 3B;
DE EC=1.14.11.65 {ECO:0000250|UniProtKB:Q7LBC6};
DE AltName: Full=JmjC domain-containing histone demethylation protein 2B;
DE AltName: Full=Jumonji domain-containing protein 1B;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3B {ECO:0000305};
GN Name=Kdm3b; Synonyms=Jhdm2b, Jmjd1b, Kiaa1082;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Eye, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1319-1762 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547; SER-557 AND SER-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC Demethylation of Lys residue generates formaldehyde and succinate May
CC have tumor suppressor activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000250|UniProtKB:Q7LBC6};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPY7-3; Sequence=VSP_061228, VSP_061229, VSP_061230;
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38376.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC98091.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AK129281; BAC98091.1; ALT_INIT; mRNA.
DR EMBL; GL456180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031981; AAH31981.1; -; mRNA.
DR EMBL; BC038376; AAH38376.1; ALT_FRAME; mRNA.
DR EMBL; BC060727; AAH60727.1; -; mRNA.
DR EMBL; BC108415; AAI08416.1; -; mRNA.
DR EMBL; BC151084; AAI51085.1; -; mRNA.
DR EMBL; AK018027; BAB31043.1; -; mRNA.
DR EMBL; AK033343; BAC28239.1; -; mRNA.
DR CCDS; CCDS37761.1; -. [Q6ZPY7-1]
DR RefSeq; NP_001074725.1; NM_001081256.1. [Q6ZPY7-1]
DR AlphaFoldDB; Q6ZPY7; -.
DR SMR; Q6ZPY7; -.
DR BioGRID; 234928; 1.
DR STRING; 10090.ENSMUSP00000037628; -.
DR iPTMnet; Q6ZPY7; -.
DR PhosphoSitePlus; Q6ZPY7; -.
DR SwissPalm; Q6ZPY7; -.
DR EPD; Q6ZPY7; -.
DR jPOST; Q6ZPY7; -.
DR MaxQB; Q6ZPY7; -.
DR PaxDb; Q6ZPY7; -.
DR PeptideAtlas; Q6ZPY7; -.
DR PRIDE; Q6ZPY7; -.
DR ProteomicsDB; 264985; -. [Q6ZPY7-1]
DR ProteomicsDB; 336542; -.
DR Antibodypedia; 14936; 361 antibodies from 38 providers.
DR Ensembl; ENSMUST00000043775; ENSMUSP00000037628; ENSMUSG00000038773. [Q6ZPY7-1]
DR GeneID; 277250; -.
DR KEGG; mmu:277250; -.
DR UCSC; uc008elq.1; mouse.
DR CTD; 51780; -.
DR MGI; MGI:1923356; Kdm3b.
DR VEuPathDB; HostDB:ENSMUSG00000038773; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000158095; -.
DR HOGENOM; CLU_002991_0_0_1; -.
DR InParanoid; Q6ZPY7; -.
DR OMA; VGAGICK; -.
DR OrthoDB; 1185631at2759; -.
DR PhylomeDB; Q6ZPY7; -.
DR TreeFam; TF324723; -.
DR BRENDA; 1.14.11.65; 3474.
DR BRENDA; 1.14.11.66; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 277250; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Kdm3b; mouse.
DR PRO; PR:Q6ZPY7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6ZPY7; protein.
DR Bgee; ENSMUSG00000038773; Expressed in embryonic post-anal tail and 260 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT CHAIN 2..1762
FT /note="Lysine-specific demethylase 3B"
FT /id="PRO_0000234374"
FT DOMAIN 1499..1722
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1032..1057
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 253..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1294..1298
FT /note="LXXLL motif"
FT COMPBIAS 274..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1561
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1563
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1690
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT CROSSLNK 789
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7LBC6"
FT VAR_SEQ 262..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_061228"
FT VAR_SEQ 1270..1324
FT /note="LTPKLFNSLLLGPTASNSKTEGSSLRDLLHSGPGKLPQTPLDTGIPFPPVFS
FT SSS -> HVTSDLAHPRRWGCSPSRTLHEHRSLQDPGRAHCFSQEAPGLGNVYLVKNRF
FT VVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_061229"
FT VAR_SEQ 1325..1762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_061230"
FT CONFLICT 1326
FT /note="V -> G (in Ref. 3; AAH31981)"
FT /evidence="ECO:0000305"
FT CONFLICT 1569..1570
FT /note="NV -> SL (in Ref. 4; BAB31043)"
FT /evidence="ECO:0000305"
FT CONFLICT 1745
FT /note="V -> G (in Ref. 4; BAB31043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1762 AA; 191460 MW; EB0D535476236CDF CRC64;
MADAAASPVG KRLLLLFADP TASASASAPT AAAVVSGDPG PALRTRAWRA GTVRAMSGAV
PQDLAIFVEF DGCNWKQHSW VKVHAEDVLA LLLEGSLVWA PRKDPVLLQG TRVPVAQWPA
LTFTPLVDKL GLGSVVPVEY LVDRELRFLS DANGMHLFQM GTDVQNQILL EHAALRETVN
ALISDQKLQE IFSRGPYSVQ GHRVKVYQPE GEEVWLCGVV SRQDSVTRLM EVSITETGEV
KSVDPRLTHV MLMDSSTPQS EGGTIKAVKS SKGKKKRESI EGRDGRRRKS ASDSGCDPAT
KKLKGDRGEV DSNGSDGGEA SRGPWKGGNA SGEPGLEQRA KQPPSTFVPQ INRNIRFATY
TKENGRTLVV QDEPVGGDTP VPFTPYASAT GQTPLAPEVG GAENKEAGKT LEQVSQGMVA
SAAVVTTASS TPTTVRISDT GLASGTGPEK QKGSWSQASG ENSRNSSLAS SGFGVSLSSL
SQPLTFGSGR SQSNGVLATD NKPLGFSFSC SSASESQKDS DLSKNLFFQC MSQNVPSTNY
LSRVSESVAD DSSSRDSFTQ SLESLTSGLC KGRSVLGADT QPGPKAGSSV DRKVPAESMP
TLTPAFPRSL LNTRTPENHE NLFLQPPKLS REEPSNPFLA FVEKVEHSPF SSFVSQASGS
SSSATSVTSK ATASWPESHS SAESAPLAKK KPLFITTDSS KLVSGVLGSA LSTGSPSLSA
VGNGRSSSPT NSLTQPIEMP TLSSSPTEER PTVGPGQQDN PLLKTFSTVF GRHSGSFLSA
PAEFAQENKA PFEAVKRFSL DERSLACRQD SDSSTNSDLS DLSDSEEQLQ AKSGLKGIPE
HLMGKLGPNG ERSAELLLGK GKGKQAPKGR PRTAPLKVGQ SVLKDVSKVR KLKQSGEPFL
QDGSCINVAP HLHKCRECRL ERYRKFKEQE QDDSTVACRF FHFRRLVFTR KGVLRVEGFL
SPQQSDPDAM NLWIPSSSLA EGIDLETSKY ILANVGDQFC QLVMSEKEAM MMVEPHQKVA
WKRAVRGVRE MCDVCETTLF NIHWVCRKCG FGVCLDCYRL RKSRPRSETE EMGDEEVFSW
LKCAKGQSHE PENLMPTQII PGTALYNIGD MVHAARGKWG IKANCPCISR QSKSVLRPAV
TNGISQLPSV TPSASSGNET TFSSGGGAAA VTNPEPDQVP KGAGTDGRSE EPLKAEGSAS
NSNSELKAIR PPCPDTAPPS SALHWLADLA TQKAKEETKD AGSLRSVLNK ESHSPFGLDS
FNSTAKVSPL TPKLFNSLLL GPTASNSKTE GSSLRDLLHS GPGKLPQTPL DTGIPFPPVF
SSSSAVAKSK ASLPDFLDHI IASVVENKKT SDPSKRSCNL TDTQKEVKEM AMGLNVLDPH
TSHSWLCDGR LLCLHDPSNK NNWKIFRECW KQGQPVLVSG VHKKLKSELW KPEAFSQEFG
DQDVDLVNCR NCAIISDVKV RDFWDGFEII CKRLRSEDGQ PMVLKLKDWP PGEDFRDMMP
TRFEDLMENL PLPEYTKRDG RLNLASRLPS YFVRPDLGPK MYNAYGLITA EDRRVGTTNL
HLDVSDAVNV MVYVGIPVGE GAHDEEVLKT IDEGDADEVT KQRIHDGKEK PGALWHIYAA
KDAEKIRELL RKVGEEQGQE NPPDHDPIHD QSWYLDQILR KRLFEEYGVQ GWAIVQFLGD
AVFIPAGAPH QVHNLYSCIK VAEDFVSPEH VKHCFRLTQE FRHLSNTHTN HEDKLQVKNI
IYHAVKDAVG TLKAHESKLA RS
