JADE2_HUMAN
ID JADE2_HUMAN Reviewed; 790 AA.
AC Q9NQC1; D3DQA3; Q6IE80; Q8TEK0; Q92513; Q96GQ6;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E3 ubiquitin-protein ligase Jade-2 {ECO:0000303|PubMed:25018020};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25018020};
DE AltName: Full=Jade family PHD finger protein 2;
DE AltName: Full=PHD finger protein 15;
GN Name=JADE2; Synonyms=KIAA0239, PHF15;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Melanoma, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-790 (ISOFORM 1).
RA Tesmann S., Biederbick A., Elsaesser H.P.;
RT "Isolation and characterisation of a 64 kDa protein associated with the
RT lysosomal/autophagic compartment.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=14612400; DOI=10.1128/mcb.23.23.8553-8562.2003;
RA Tzouanacou E., Tweedie S., Wilson V.;
RT "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a
RT gene trap mutagenesis screen for genes involved in anteroposterior axis
RT development.";
RL Mol. Cell. Biol. 23:8553-8562(2003).
RN [8]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-38 AND LYS-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KDM1A, DOMAIN, AND
RP MUTAGENESIS OF CYS-202 AND CYS-243.
RX PubMed=25018020; DOI=10.1016/j.molcel.2014.06.006;
RA Han X., Gui B., Xiong C., Zhao L., Liang J., Sun L., Yang X., Yu W., Si W.,
RA Yan R., Yi X., Zhang D., Li W., Li L., Yang J., Wang Y., Sun Y.E.,
RA Zhang D., Meng A., Shang Y.;
RT "Destabilizing LSD1 by Jade-2 promotes neurogenesis: an antibraking system
RT in neural development.";
RL Mol. Cell 55:482-494(2014).
CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC H4 acetyltransferase activity (PubMed:16387653). Acts as a E3
CC ubiquitin-protein ligase mediating the ubiquitination and subsequent
CC proteasomal degradation of target protein histone demethylase KDM1A
CC (PubMed:25018020). Also acts as a ubiquitin ligase E3 toward itself.
CC Positive regulator of neurogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZQF7, ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:25018020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:25018020};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:25018020}.
CC -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or
CC ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3
CC (PubMed:16387653). Interacts (via C-terminus) with KDM1A (via AOD/Tower
CC domain) (PubMed:25018020). {ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:25018020}.
CC -!- INTERACTION:
CC Q9NQC1; Q8WYH8: ING5; NbExp=4; IntAct=EBI-2796167, EBI-488533;
CC Q9NQC1-2; P01100: FOS; NbExp=3; IntAct=EBI-10311936, EBI-852851;
CC Q9NQC1-2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-10311936, EBI-739467;
CC Q9NQC1-2; P62993: GRB2; NbExp=3; IntAct=EBI-10311936, EBI-401755;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQC1-2; Sequence=VSP_021051;
CC Name=3;
CC IsoId=Q9NQC1-3; Sequence=VSP_021050;
CC -!- DOMAIN: The first PHD domain is essential for its E3 ubiquitin ligase
CC activity. {ECO:0000269|PubMed:25018020}.
CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13245.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84949.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB94935.1; Type=Erroneous initiation; Note=Truncated 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; D87076; BAA13245.2; ALT_INIT; mRNA.
DR EMBL; AK074123; BAB84949.1; ALT_FRAME; mRNA.
DR EMBL; BC009307; AAH09307.2; -; mRNA.
DR EMBL; BC021962; AAH21962.2; -; mRNA.
DR EMBL; AC005355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62253.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62254.1; -; Genomic_DNA.
DR EMBL; AJ251833; CAB94935.1; ALT_INIT; mRNA.
DR EMBL; BN000288; CAE30501.1; -; mRNA.
DR CCDS; CCDS4176.1; -. [Q9NQC1-1]
DR RefSeq; NP_001276913.1; NM_001289984.1.
DR RefSeq; NP_001276914.1; NM_001289985.1.
DR RefSeq; NP_001295072.1; NM_001308143.1.
DR RefSeq; NP_056103.4; NM_015288.5. [Q9NQC1-1]
DR AlphaFoldDB; Q9NQC1; -.
DR SMR; Q9NQC1; -.
DR BioGRID; 116924; 49.
DR ComplexPortal; CPX-719; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-722; HBO1-5.2 histone acetyltransferase complex.
DR CORUM; Q9NQC1; -.
DR IntAct; Q9NQC1; 31.
DR MINT; Q9NQC1; -.
DR STRING; 9606.ENSP00000354425; -.
DR iPTMnet; Q9NQC1; -.
DR PhosphoSitePlus; Q9NQC1; -.
DR BioMuta; JADE2; -.
DR DMDM; 116242597; -.
DR EPD; Q9NQC1; -.
DR jPOST; Q9NQC1; -.
DR MassIVE; Q9NQC1; -.
DR MaxQB; Q9NQC1; -.
DR PaxDb; Q9NQC1; -.
DR PeptideAtlas; Q9NQC1; -.
DR PRIDE; Q9NQC1; -.
DR ProteomicsDB; 12749; -.
DR ProteomicsDB; 82130; -. [Q9NQC1-1]
DR ProteomicsDB; 82131; -. [Q9NQC1-2]
DR ProteomicsDB; 82132; -. [Q9NQC1-3]
DR Antibodypedia; 14678; 48 antibodies from 12 providers.
DR DNASU; 23338; -.
DR Ensembl; ENST00000395003.5; ENSP00000378451.1; ENSG00000043143.22. [Q9NQC1-1]
DR Ensembl; ENST00000430087.2; ENSP00000396026.2; ENSG00000043143.22. [Q9NQC1-3]
DR GeneID; 23338; -.
DR KEGG; hsa:23338; -.
DR UCSC; uc003kzm.3; human. [Q9NQC1-1]
DR CTD; 23338; -.
DR DisGeNET; 23338; -.
DR GeneCards; JADE2; -.
DR HGNC; HGNC:22984; JADE2.
DR HPA; ENSG00000043143; Low tissue specificity.
DR MIM; 610515; gene.
DR neXtProt; NX_Q9NQC1; -.
DR OpenTargets; ENSG00000043143; -.
DR PharmGKB; PA128394627; -.
DR VEuPathDB; HostDB:ENSG00000043143; -.
DR eggNOG; KOG0954; Eukaryota.
DR GeneTree; ENSGT00940000158570; -.
DR HOGENOM; CLU_016215_2_0_1; -.
DR InParanoid; Q9NQC1; -.
DR OrthoDB; 1235709at2759; -.
DR PhylomeDB; Q9NQC1; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; Q9NQC1; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9NQC1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23338; 19 hits in 1089 CRISPR screens.
DR ChiTaRS; JADE2; human.
DR GenomeRNAi; 23338; -.
DR Pharos; Q9NQC1; Tbio.
DR PRO; PR:Q9NQC1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NQC1; protein.
DR Bgee; ENSG00000043143; Expressed in palpebral conjunctiva and 183 other tissues.
DR ExpressionAtlas; Q9NQC1; baseline and differential.
DR Genevisible; Q9NQC1; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15705; ePHD_JADE2; 1.
DR CDD; cd15680; PHD_JADE2; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR039549; JADE2_ePHD.
DR InterPro; IPR039548; JADE2_PHD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PF10513; EPL1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..790
FT /note="E3 ubiquitin-protein ligase Jade-2"
FT /id="PRO_0000059308"
FT ZN_FING 199..249
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 251..285
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 309..365
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQF7"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 518..790
FT /note="GLSTSFPIDGTFFNSWLAQSVQITAENMAMSEWPLNNGHREDPAPGLLSEEL
FT LQDEETLLSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKT
FT WGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASV
FT AADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFD
FT TETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS -> ERSGRRAKGKK
FT SDSKRKGCEGSKGSTEKKEKVKAGPDSVLGQLGE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_021050"
FT VAR_SEQ 518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9039502"
FT /id="VSP_021051"
FT VARIANT 581
FT /note="R -> G (in dbSNP:rs34200923)"
FT /id="VAR_053778"
FT MUTAGEN 202
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity
FT on KDM1A."
FT /evidence="ECO:0000269|PubMed:25018020"
FT MUTAGEN 243
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity
FT on KDM1A."
FT /evidence="ECO:0000269|PubMed:25018020"
FT CONFLICT 331
FT /note="T -> I (in Ref. 1; BAA13245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 87466 MW; 22C1B1A0360BC1AE CRC64;
MEEKRRKYSI SSDNSDTTDS HATSTSASRC SKLPSSTKSG WPRQNEKKPS EVFRTDLITA
MKIPDSYQLS PDDYYILADP WRQEWEKGVQ VPAGAEAIPE PVVRILPPLE GPPAQASPSS
TMLGEGSQPD WPGGSRYDLD EIDAYWLELI NSELKEMERP ELDELTLERV LEELETLCHQ
NMARAIETQE GLGIEYDEDV VCDVCRSPEG EDGNEMVFCD KCNVCVHQAC YGILKVPTGS
WLCRTCALGV QPKCLLCPKR GGALKPTRSG TKWVHVSCAL WIPEVSIGCP EKMEPITKIS
HIPASRWALS CSLCKECTGT CIQCSMPSCV TAFHVTCAFD HGLEMRTILA DNDEVKFKSF
CQEHSDGGPR NEPTSEPTEP SQAGEDLEKV TLRKQRLQQL EEDFYELVEP AEVAERLDLA
EALVDFIYQY WKLKRKANAN QPLLTPKTDE VDNLAQQEQD VLYRRLKLFT HLRQDLERVR
NLCYMVTRRE RTKHAICKLQ EQIFHLQMKL IEQDLCRGLS TSFPIDGTFF NSWLAQSVQI
TAENMAMSEW PLNNGHREDP APGLLSEELL QDEETLLSFM RDPSLRPGDP ARKARGRTRL
PAKKKPPPPP PQDGPGSRTT PDKAPKKTWG QDAGSGKGGQ GPPTRKPPRR TSSHLPSSPA
AGDCPILATP ESPPPLAPET PDEAASVAAD SDVQVPGPAA SPKPLGRLRP PRESKVTRRL
PGARPDAGMG PPSAVAERPK VSLHFDTETD GYFSDGEMSD SDVEAEDGGV QRGPREAGAE
EVVRMGVLAS
