ID   JADE1_MOUSE             Reviewed;         834 AA.
AC   Q6ZPI0; Q6IE84; Q8C7S6; Q8CFM2; Q8R362;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Protein Jade-1;
DE   AltName: Full=Jade family PHD finger protein 1;
DE   AltName: Full=PHD finger protein 17;
GN   Name=Jade1; Synonyms=Kiaa1807, Phf17;
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 1).
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 MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
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 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   IDENTIFICATION, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12169691; DOI=10.1074/jbc.m205040200;
RA   Zhou M.I., Wang H., Ross J.J., Kuzmin I., Xu C., Cohen H.T.;
RT   "The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain
RT   protein Jade-1.";
RL   J. Biol. Chem. 277:39887-39898(2002).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC       H4 acetyltransferase activity. Plays a key role in HBO1 complex by
CC       directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac,
CC       H4K8ac and H4K12ac), regulating DNA replication initiation, regulating
CC       DNA replication initiation. May also promote acetylation of nucleosomal
CC       histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor
CC       suppressor. Negatively regulates canonical Wnt signaling; at least in
CC       part, cooperates with NPHP4 in this function.
CC       {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or
CC       ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts
CC       with NPHP4. {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IE81}.
CC       Chromosome {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q6IE81}. Note=Localizes to the ciliary
CC       transition zone. {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Jade1L;
CC         IsoId=Q6ZPI0-1; Sequence=Displayed;
CC       Name=2; Synonyms=Jade1S;
CC         IsoId=Q6ZPI0-2; Sequence=VSP_021048, VSP_021049;
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney. Also present in liver
CC       (at protein level). {ECO:0000269|PubMed:12169691}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 6.5 dpc. From 12.5 to 15.5 dpc,
CC       expressed in the nervous system and developing muscles.
CC       {ECO:0000269|PubMed:14612400}.
CC   -!- DOMAIN: The 2 PHD-type zinc fingers are required for transcriptional
CC       activity. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, and show no visible
CC       phenotype. {ECO:0000269|PubMed:14612400}.
CC   -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC98255.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK129445; BAC98255.1; ALT_INIT; mRNA.
DR   EMBL; AK049332; BAC33688.1; -; mRNA.
DR   EMBL; AK147466; BAE27932.1; -; mRNA.
DR   EMBL; BC020316; AAH20316.1; -; mRNA.
DR   EMBL; BC026471; AAH26471.1; ALT_INIT; mRNA.
DR   EMBL; BN000282; CAE30497.1; -; mRNA.
DR   EMBL; BN000281; CAE30496.1; -; mRNA.
DR   CCDS; CCDS17331.1; -. [Q6ZPI0-1]
DR   RefSeq; NP_001123656.1; NM_001130184.1. [Q6ZPI0-1]
DR   RefSeq; NP_001123657.1; NM_001130185.1. [Q6ZPI0-1]
DR   RefSeq; NP_001123658.1; NM_001130186.1. [Q6ZPI0-1]
DR   RefSeq; NP_758507.3; NM_172303.4. [Q6ZPI0-1]
DR   AlphaFoldDB; Q6ZPI0; -.
DR   SMR; Q6ZPI0; -.
DR   BioGRID; 234652; 10.
DR   ComplexPortal; CPX-794; HBO1-4.1 histone acetyltransferase complex.
DR   ComplexPortal; CPX-797; HBO1-5.1 histone acetyltransferase complex.
DR   IntAct; Q6ZPI0; 6.
DR   STRING; 10090.ENSMUSP00000128152; -.
DR   iPTMnet; Q6ZPI0; -.
DR   PhosphoSitePlus; Q6ZPI0; -.
DR   EPD; Q6ZPI0; -.
DR   jPOST; Q6ZPI0; -.
DR   MaxQB; Q6ZPI0; -.
DR   PaxDb; 10090-ENSMUSP00000128152; -.
DR   PeptideAtlas; Q6ZPI0; -.
DR   ProteomicsDB; 269356; -. [Q6ZPI0-1]
DR   ProteomicsDB; 269357; -. [Q6ZPI0-2]
DR   Pumba; Q6ZPI0; -.
DR   Antibodypedia; 16094; 209 antibodies from 28 providers.
DR   DNASU; 269424; -.
DR   Ensembl; ENSMUST00000026865.15; ENSMUSP00000026865.9; ENSMUSG00000025764.15. [Q6ZPI0-1]
DR   Ensembl; ENSMUST00000163764.8; ENSMUSP00000128152.2; ENSMUSG00000025764.15. [Q6ZPI0-1]
DR   Ensembl; ENSMUST00000168086.7; ENSMUSP00000131441.2; ENSMUSG00000025764.15. [Q6ZPI0-1]
DR   Ensembl; ENSMUST00000170711.8; ENSMUSP00000127113.2; ENSMUSG00000025764.15. [Q6ZPI0-1]
DR   Ensembl; ENSMUST00000191952.2; ENSMUSP00000141499.2; ENSMUSG00000025764.15. [Q6ZPI0-2]
DR   GeneID; 269424; -.
DR   KEGG; mmu:269424; -.
DR   UCSC; uc008pcj.2; mouse. [Q6ZPI0-1]
DR   AGR; MGI:1925835; -.
DR   CTD; 79960; -.
DR   MGI; MGI:1925835; Jade1.
DR   VEuPathDB; HostDB:ENSMUSG00000025764; -.
DR   eggNOG; KOG0954; Eukaryota.
DR   GeneTree; ENSGT00940000158247; -.
DR   HOGENOM; CLU_016215_0_0_1; -.
DR   InParanoid; Q6ZPI0; -.
DR   OMA; SSTCWSQ; -.
DR   PhylomeDB; Q6ZPI0; -.
DR   TreeFam; TF316118; -.
DR   Reactome; R-MMU-3214847; HATs acetylate histones.
DR   BioGRID-ORCS; 269424; 4 hits in 84 CRISPR screens.
DR   ChiTaRS; Jade1; mouse.
DR   PRO; PR:Q6ZPI0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q6ZPI0; Protein.
DR   Bgee; ENSMUSG00000025764; Expressed in lacrimal gland and 243 other cell types or tissues.
DR   ExpressionAtlas; Q6ZPI0; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR   GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR   GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd15671; ePHD_JADE; 1.
DR   CDD; cd15679; PHD_JADE1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR039546; Jade-1_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   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   PANTHER; PTHR13793:SF79; PROTEIN JADE-1; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   Genevisible; Q6ZPI0; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Apoptosis; Cell projection;
KW   Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..834
FT                   /note="Protein Jade-1"
FT                   /id="PRO_0000253530"
FT   ZN_FING         204..254
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         256..290
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         314..370
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..81
FT                   /note="Interaction with KAT7/HBO1 and histones"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   REGION          81..189
FT                   /note="Interaction with histones"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   REGION          367..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   MOD_RES         609
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         704
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   CROSSLNK        573
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT   VAR_SEQ         504..510
FT                   /note="RNLTYMV -> MIDTDTL (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_021048"
FT   VAR_SEQ         511..834
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_021049"
FT   CONFLICT        190
FT                   /note="A -> D (in Ref. 2; BAC33688)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   834 AA;  93897 MW;  43388FC7103D97D6 CRC64;
     MKRGRLPSSS EDSDDNGSLS TTWSQHSRSQ HGRSSTCSRP EDRKPSEVFR TDLITAMKLH
     DSYQLNPDDY YVLADPWRQE WEKGVQVPVS PGTIPQPVAR VVSEEKSLMF IRPKKYIASS
     GSEPPALGYV DIRTLADSVC RYDLNDMDAA WLEVTNEEFK EMGMPELDEY TMERVLEEFE
     QRCYDNMNHA IETEEGLGIE YDEDVVCDVC QSPDGEDGNE MVFCDKCNIC VHQACYGILK
     VPEGSWLCRT CALGVQPKCL LCPKKGGAMK PTRSGTKWVH VSCALWIPEV SIGSPEKMEP
     ITKVSHIPSS RWALVCSLCN EKFGASIQCS VKNCRTAFHV TCAFDRGLEM KTILAENDEV
     KFKSYCPKHS SHRKPEEGLG EGAAQENGAP ESSPQSPLEP YGSLEPNREE AHRVSVRKQK
     LQQLEDEFYT FVNLLDVARA LRLPEEVVDF LYQYWKLKRK INFNKPLITP KKDEEDNLAK
     REQDVLFRRL QLFTHLRQDL ERVRNLTYMV TRREKIKRSV CKVQEQIFTQ YTKLLEQEKV
     SGVPSSCSSA LENMLFFNSP SVGPNAPKIE DLKWHSAFFR KQMGTSLVHP LKKSHKRDAV
     QNSSGTEGKT SHKQPGLCGR REGLEVSESL LSLEKTFAEA RLLSSAQQKN GVVTPDHGKR
     RDNRFHCDLV KGDLKDKSFK QSHKPLRSTD TSQRHLDNTR AATSPGVGQS APGTRKEIVP
     KCNGSLVKVP ITPASPVKSW GGFRIPKKGE RQQQGEAHDG ACHQHSDCSH LGVSRAPAKE
     RAKSRLRADS ENDGYAPDGE MSDSESEASE KKCIHASSTI SRRTDIIRRS ILAS
//