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   24-JAN-2024, entry version 121.
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   GlyGen; Q6ZPY7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZPY7; -.
DR   PhosphoSitePlus; Q6ZPY7; -.
DR   SwissPalm; Q6ZPY7; -.
DR   EPD; Q6ZPY7; -.
DR   jPOST; Q6ZPY7; -.
DR   MaxQB; Q6ZPY7; -.
DR   PaxDb; 10090-ENSMUSP00000037628; -.
DR   PeptideAtlas; Q6ZPY7; -.
DR   ProteomicsDB; 264985; -. [Q6ZPY7-1]
DR   ProteomicsDB; 336542; -.
DR   Pumba; Q6ZPY7; -.
DR   Antibodypedia; 14936; 396 antibodies from 38 providers.
DR   Ensembl; ENSMUST00000043775.9; ENSMUSP00000037628.8; ENSMUSG00000038773.12. [Q6ZPY7-1]
DR   GeneID; 277250; -.
DR   KEGG; mmu:277250; -.
DR   UCSC; uc008elq.1; mouse.
DR   AGR; MGI:1923356; -.
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; ENSWVSA; -.
DR   OrthoDB; 3473445at2759; -.
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 82 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 264 other cell types or 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:0016209; F:antioxidant activity; ISO:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR   GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:UniProtKB-EC.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR045109; JHDM2-like.
DR   InterPro; IPR003347; JmjC_dom.
DR   PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR   PANTHER; PTHR12549:SF8; LYSINE-SPECIFIC DEMETHYLASE 3B; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 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
//