KDM5D_MOUSE
ID KDM5D_MOUSE Reviewed; 1548 AA.
AC Q62240; Q3US03; Q6PCX3; Q9QVR9; Q9R040;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lysine-specific demethylase 5D;
DE EC=1.14.11.67 {ECO:0000250|UniProtKB:Q9BY66};
DE AltName: Full=Histocompatibility Y antigen;
DE Short=H-Y;
DE AltName: Full=Histone demethylase JARID1D;
DE AltName: Full=Jumonji/ARID domain-containing protein 1D;
DE AltName: Full=Protein SmcY;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5D {ECO:0000305};
GN Name=Kdm5d; Synonyms=Hya, Jarid1d, Smcy;
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 [MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RX PubMed=10441747; DOI=10.1007/s003359901116;
RA Agulnik A.I., Longepied G., Ty M.T., Bishop C.E., Mitchell M.J.;
RT "Mouse H-Y encoding Smcy gene and its X chromosomal homolog Smcx.";
RL Mamm. Genome 10:926-929(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [MRNA] OF 23-1548 (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=7524912; DOI=10.1093/hmg/3.6.873;
RA Agulnik A.I., Mitchell M.J., Lerner J.L., Woods D.R., Bishop C.E.;
RT "A mouse Y chromosome gene encoded by a region essential for
RT spermatogenesis and expression of male-specific minor histocompatibility
RT antigens.";
RL Hum. Mol. Genet. 3:873-878(1994).
RN [5]
RP FUNCTION.
RX PubMed=7544442; DOI=10.1038/376695a0;
RA Scott D.M., Ehrmann I.E., Ellis P.S., Bishop C.E., Agulnik A.I.,
RA Simpson E., Mitchell M.J.;
RT "Identification of a mouse male-specific transplantation antigen, H-Y.";
RL Nature 376:695-698(1995).
RN [6]
RP FUNCTION.
RX PubMed=3951555; DOI=10.1038/320170a0;
RA Burgoyne P.S., Levy E.R., McLaren A.;
RT "Spermatogenic failure in male mice lacking H-Y antigen.";
RL Nature 320:170-172(1986).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, thereby playing a central role in histone code. Does not
CC demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not
CC monomethylated H3 'Lys-4'. May play a role in spermatogenesis. Involved
CC in transcriptional repression of diverse metastasis-associated genes;
CC in this function seems to cooperate with ZMYND8. Suppresses prostate
CC cancer cell invasion. Regulates androgen receptor (AR) transcriptional
CC activity by demethylating H3K4me3 active transcription marks (By
CC similarity). {ECO:0000250|UniProtKB:Q9BY66, ECO:0000269|PubMed:3951555,
CC ECO:0000269|PubMed:7544442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000250|UniProtKB:Q9BY66};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q9BY66};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9BY66};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9BY66};
CC -!- SUBUNIT: Interacts withPCGF6, MSH5, ZMYND8, AR.
CC {ECO:0000250|UniProtKB:Q9BY66}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BY66,
CC ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-
CC ProRule:PRU00537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q62240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62240-2; Sequence=VSP_026412;
CC Name=3;
CC IsoId=Q62240-3; Sequence=VSP_026413, VSP_026414;
CC Name=4;
CC IsoId=Q62240-4; Sequence=VSP_026415, VSP_026416;
CC -!- DOMAIN: The JmjC domain is required for enzymatic activity.
CC {ECO:0000250|UniProtKB:Q9BY66}.
CC -!- MISCELLANEOUS: KDM5D encodes an H-Y epitope that is defined by the
CC octamer peptide TENSGKDI; since no similar peptide was found in KDM5C,
CC it is presumably the genetic basis for the antigenic difference between
CC males and females that contributes toward a tissue transplant rejection
CC response.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AF127244; AAD53048.1; -; mRNA.
DR EMBL; AK140971; BAE24534.1; -; mRNA.
DR EMBL; BC059077; AAH59077.1; -; mRNA.
DR EMBL; Z29652; CAA82760.1; -; mRNA.
DR CCDS; CCDS30541.1; -. [Q62240-1]
DR PIR; I48776; I48776.
DR RefSeq; NP_035549.1; NM_011419.3. [Q62240-1]
DR AlphaFoldDB; Q62240; -.
DR SMR; Q62240; -.
DR BioGRID; 203342; 5.
DR IntAct; Q62240; 3.
DR STRING; 10090.ENSMUSP00000061095; -.
DR iPTMnet; Q62240; -.
DR PhosphoSitePlus; Q62240; -.
DR EPD; Q62240; -.
DR MaxQB; Q62240; -.
DR PaxDb; Q62240; -.
DR PeptideAtlas; Q62240; -.
DR PRIDE; Q62240; -.
DR ProteomicsDB; 269293; -. [Q62240-1]
DR ProteomicsDB; 269294; -. [Q62240-2]
DR ProteomicsDB; 269295; -. [Q62240-3]
DR ProteomicsDB; 269296; -. [Q62240-4]
DR Antibodypedia; 21879; 55 antibodies from 26 providers.
DR DNASU; 20592; -.
DR Ensembl; ENSMUST00000055032; ENSMUSP00000061095; ENSMUSG00000056673. [Q62240-1]
DR Ensembl; ENSMUST00000186696; ENSMUSP00000140663; ENSMUSG00000056673. [Q62240-4]
DR GeneID; 20592; -.
DR KEGG; mmu:20592; -.
DR UCSC; uc009uyz.1; mouse. [Q62240-3]
DR UCSC; uc009uzb.1; mouse. [Q62240-1]
DR CTD; 8284; -.
DR MGI; MGI:99780; Kdm5d.
DR VEuPathDB; HostDB:ENSMUSG00000056673; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000161236; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR InParanoid; Q62240; -.
DR OMA; CIELPQI; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q62240; -.
DR TreeFam; TF106476; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 20592; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Kdm5d; mouse.
DR PRO; PR:Q62240; -.
DR Proteomes; UP000000589; Chromosome Y.
DR RNAct; Q62240; protein.
DR Bgee; ENSMUSG00000056673; Expressed in embryonic post-anal tail and 202 other tissues.
DR ExpressionAtlas; Q62240; baseline and differential.
DR Genevisible; Q62240; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; ISO:MGI.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISO:MGI.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IDA:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1548
FT /note="Lysine-specific demethylase 5D"
FT /id="PRO_0000200589"
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 467..633
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 325..371
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 706..758
FT /note="C5HC2"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT ZN_FING 1182..1243
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 208..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 513
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 515
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 521
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 523
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 531
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 601
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41230"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT MOD_RES 1355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT CROSSLNK 1123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41229"
FT VAR_SEQ 1..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026412"
FT VAR_SEQ 583..586
FT /note="VRTN -> SIWK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7524912"
FT /id="VSP_026413"
FT VAR_SEQ 587..1548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7524912"
FT /id="VSP_026414"
FT VAR_SEQ 687..691
FT /note="GITEA -> LSLQA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026415"
FT VAR_SEQ 692..1548
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026416"
FT CONFLICT 160..162
FT /note="IIY -> SFT (in Ref. 4; CAA82760)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="F -> S (in Ref. 4; CAA82760)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="R -> K (in Ref. 4; CAA82760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1548 AA; 177018 MW; 44AAB94708EA4A02 CRC64;
MKPGSDDFLP PPECPVFEPS WAEFRDPLGY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERKIL DLYSLNKIVM
EEGGYEAICK DRRWARVAQR LNYPSGKNIG SLLRSHYERI IYPYEIFQSG ANLVQCNTDP
FDSEERDKEY KPHSIPLRQS VQPSKFSCYS RRGKRLQPEP EPTEEDIEKN PELKKLQIYG
AGPKMIGLGL KAKEKTLRKK DSKQPDKEEV TCPATIVVKG EASEFGKVTS AFSDKNLNHS
FEPCMKMTMQ LRNNHSSTQF MNSYVCRICS RGDEVDKFLL CDGCSDNYHI FCLLPPLSEV
PKGVWRCPKC ILAECKSPPE AFGFEQATQE YTLQSFGEMA DSFKADYFNM PVHMVPTEVV
EKEFWRLVSS IEEDVTVEYG ADIHSKEFGS GFPVNNSKWD LSPEEKEYAA CGWNLNVMPV
LDQSVLCHIN ADISGMKVPW LYVGMVFSAF CWHIEDHWSY SINYLHWGEP KTWYGVPSLA
AEHLEDVMKR LTPELFDSQP DLLHQLVTLM NPNTLMSHGV PVVRTNQCAG EFVITFPRAY
HSGFNQGYNF AEAVNFCTAD WLPVGRQCIE HYRRLRRYCV FSHEELICKM AAFPEKLDLN
LAVAVHKEMF IMVQEERRLR KTLLEKGITE AEREAFELLP DDERQCIKCK TTCFLSALAC
YDCPDSLVCL SHINDLCKCS RNRQYLRYRY TLDELPAMLQ KLKIRAESFD NWANKVQAAL
EVEDGRKRSF EELRALESEA RDRRFPNSEL LQRLKKCLTE AEACISQVLG LISNSEDRLQ
TPQITLTELQ LLLKQMGTLP CTMHQIDEVK DVLQQVESYQ IETREALTSL PYSLEILQSL
MEKGQQLRVE VPEAHQLEEL LEQAQWLDQV KQALAPSGQR HSLVIMKKLL VMGTKVASSP
SVNKARAELQ ELLTIAECWE EKAHFCLKAS QKHSPATLEV IIREAENIPV YLPNIQSLKE
ALTKAQAWIA DVNEIQNGDH YPCLDDLEGL VAVGRDLPVE LEELRQLENQ VLTAHSWKEK
ASKTFLKKNS CYTLLEVLCP CADAGSVSTK RSRWIEKEMG LYKYDTELLG LSAQDLRDPG
SVIMAFKEGE EKEKEGILHL RHINSAKPSP MSSSMNASAT SICICGQVCA GVESLQCDLC
HDWFHGQCVT VPHLLSSVRA SHTSSQLLAW WEWDTKFLCP LCMRSRRPRL ETILSLLVGL
QRLSVRLPEG EALQCLTERA IGWQGRARQA LASEDVTALL KQLEKSRQQL QDELRHKKPP
TLPSGFAFDC LTENSGKDIL KEEEELVLNE ERIKSSEKIV PKESSCKGDK ELLPSLLSQL
TGPVLELPEA TRAPLEELMM EGDLLEVTLD ENYSIWQLLQ AGQNPNLERI HTLLELEKPE
NPGNWSEEQT PERRRQRRQK VVLSRKGEDF TQKELESKRV KSSRIKPKEE KFQKPILGDN
VLYTHHTEHT NILKEHINSV QGKDPSPSSS FPSLTPLLHL SYFHQQKL
