ID   ADA19_HUMAN             Reviewed;         955 AA.
AC   Q9H013; Q9BZL5; Q9UHP2;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 3.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 19;
DE            Short=ADAM 19;
DE            EC=3.4.24.-;
DE   AltName: Full=Meltrin-beta;
DE   AltName: Full=Metalloprotease and disintegrin dendritic antigen marker;
DE            Short=MADDAM;
DE   Flags: Precursor;
GN   Name=ADAM19; Synonyms=MLTNB; ORFNames=FKSG34;
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 [MRNA] (ISOFORM A).
RA   Wang Y.-G., Gong L.;
RT   "Identification of FKSG34, a novel human gene encoding for metalloprotease-
RT   disintegrin meltrin beta.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT SER-4.
RC   TISSUE=Lymph node;
RX   PubMed=10887142;
RA   Fritsche J., Moser M., Faust S., Peuker A., Buettner R., Andreesen R.,
RA   Kreutz M.;
RT   "Molecular cloning and characterization of a human metalloprotease
RT   disintegrin a novel marker for dendritic cell differentiation.";
RL   Blood 96:732-739(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC   TISSUE=Dendritic cell;
RX   PubMed=11162584; DOI=10.1006/bbrc.2000.4200;
RA   Wei P., Zhao Y.-G., Zhuang L., Ruben S., Sang Q.-X.A.;
RT   "Expression and enzymatic activity of human disintegrin and
RT   metalloproteinase ADAM19/meltrin beta.";
RL   Biochem. Biophys. Res. Commun. 280:744-755(2001).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 99-955 (ISOFORM A).
RA   Xu R., Cai J., Ying B., Wang F., Xu T., Zhao S., Li C.;
RT   "Partial sequence of Homo sapiens ADAM19.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH SH3PXD2A.
RX   PubMed=12615925; DOI=10.1074/jbc.m300267200;
RA   Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M.,
RA   Courtneidge S.A.;
RT   "The adaptor protein fish associates with members of the ADAMs family and
RT   localizes to podosomes of Src-transformed cells.";
RL   J. Biol. Chem. 278:16844-16851(2003).
RN   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLN-133 AND THR-298.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-609.
RX   PubMed=18772397; DOI=10.1126/science.1164368;
RA   Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA   Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA   Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA   Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA   Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA   Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA   Velculescu V.E., Kinzler K.W.;
RT   "Core signaling pathways in human pancreatic cancers revealed by global
RT   genomic analyses.";
RL   Science 321:1801-1806(2008).
CC   -!- FUNCTION: Participates in the proteolytic processing of beta-type
CC       neuregulin isoforms which are involved in neurogenesis and
CC       synaptogenesis, suggesting a regulatory role in glial cell. Also
CC       cleaves alpha-2 macroglobulin. May be involved in osteoblast
CC       differentiation and/or osteoblast activity in bone (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with SH3PXD2A. {ECO:0000269|PubMed:12615925}.
CC   -!- INTERACTION:
CC       Q9H013; Q8TE68: EPS8L1; NbExp=2; IntAct=EBI-8567699, EBI-7487998;
CC       Q9H013; O95153: TSPOAP1; NbExp=2; IntAct=EBI-8567699, EBI-5915931;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q9H013-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q9H013-2; Sequence=VSP_005481;
CC   -!- TISSUE SPECIFICITY: Expressed in many normal organ tissues and several
CC       cancer cell lines.
CC   -!- INDUCTION: By 1,25(OH)2VD3 in monocytes.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
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DR   EMBL; AF326918; AAG50282.1; -; mRNA.
DR   EMBL; Y13786; CAC20585.1; -; mRNA.
DR   EMBL; AF311317; AAK07852.1; -; mRNA.
DR   EMBL; AC008676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF134707; AAF22162.1; -; mRNA.
DR   CCDS; CCDS4338.1; -. [Q9H013-2]
DR   RefSeq; NP_150377.1; NM_033274.4. [Q9H013-2]
DR   RefSeq; XP_005266060.1; XM_005266003.2.
DR   AlphaFoldDB; Q9H013; -.
DR   SMR; Q9H013; -.
DR   BioGRID; 114267; 50.
DR   IntAct; Q9H013; 18.
DR   MINT; Q9H013; -.
DR   STRING; 9606.ENSP00000257527; -.
DR   MEROPS; M12.214; -.
DR   GlyCosmos; Q9H013; 4 sites, No reported glycans.
DR   GlyGen; Q9H013; 8 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9H013; -.
DR   PhosphoSitePlus; Q9H013; -.
DR   SwissPalm; Q9H013; -.
DR   BioMuta; ADAM19; -.
DR   DMDM; 302393821; -.
DR   EPD; Q9H013; -.
DR   jPOST; Q9H013; -.
DR   MassIVE; Q9H013; -.
DR   MaxQB; Q9H013; -.
DR   PaxDb; 9606-ENSP00000257527; -.
DR   PeptideAtlas; Q9H013; -.
DR   ProteomicsDB; 80195; -. [Q9H013-1]
DR   ProteomicsDB; 80196; -. [Q9H013-2]
DR   Antibodypedia; 16547; 275 antibodies from 36 providers.
DR   DNASU; 8728; -.
DR   Ensembl; ENST00000257527.9; ENSP00000257527.5; ENSG00000135074.16. [Q9H013-2]
DR   Ensembl; ENST00000517905.1; ENSP00000428654.1; ENSG00000135074.16. [Q9H013-1]
DR   GeneID; 8728; -.
DR   KEGG; hsa:8728; -.
DR   MANE-Select; ENST00000257527.9; ENSP00000257527.5; NM_033274.5; NP_150377.1. [Q9H013-2]
DR   UCSC; uc003lwz.5; human. [Q9H013-1]
DR   AGR; HGNC:197; -.
DR   CTD; 8728; -.
DR   DisGeNET; 8728; -.
DR   GeneCards; ADAM19; -.
DR   HGNC; HGNC:197; ADAM19.
DR   HPA; ENSG00000135074; Low tissue specificity.
DR   MIM; 603640; gene.
DR   neXtProt; NX_Q9H013; -.
DR   OpenTargets; ENSG00000135074; -.
DR   PharmGKB; PA24514; -.
DR   VEuPathDB; HostDB:ENSG00000135074; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000159624; -.
DR   HOGENOM; CLU_012714_7_0_1; -.
DR   InParanoid; Q9H013; -.
DR   OMA; HGMMSPR; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q9H013; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q9H013; -.
DR   Reactome; R-HSA-8941237; Invadopodia formation.
DR   Reactome; R-HSA-9762292; Regulation of CDH11 function.
DR   SABIO-RK; Q9H013; -.
DR   SignaLink; Q9H013; -.
DR   SIGNOR; Q9H013; -.
DR   BioGRID-ORCS; 8728; 9 hits in 1148 CRISPR screens.
DR   ChiTaRS; ADAM19; human.
DR   GeneWiki; ADAM19; -.
DR   GenomeRNAi; 8728; -.
DR   Pharos; Q9H013; Tbio.
DR   PRO; PR:Q9H013; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9H013; Protein.
DR   Bgee; ENSG00000135074; Expressed in oocyte and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9H013; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
DR   GO; GO:1902945; F:metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IMP:ARUK-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0042987; P:amyloid precursor protein catabolic process; IMP:ARUK-UCL.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR   GO; GO:0001890; P:placenta development; IEP:UniProtKB.
DR   GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IMP:ARUK-UCL.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF19; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 19; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q9H013; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; SH3-binding; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..202
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029102"
FT   CHAIN           203..955
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 19"
FT                   /id="PRO_0000029103"
FT   TOPO_DOM        203..699
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        700..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        721..955
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          210..408
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          416..502
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          650..682
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          753..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           130..137
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   MOTIF           833..844
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        753..775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..802
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        645
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        320..403
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..387
FT                   /evidence="ECO:0000250"
FT   DISULFID        361..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        474..494
FT                   /evidence="ECO:0000250"
FT   DISULFID        654..664
FT                   /evidence="ECO:0000250"
FT   DISULFID        658..670
FT                   /evidence="ECO:0000250"
FT   DISULFID        672..681
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         902..955
FT                   /note="VSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQKPRAKHSCFLV
FT                   PA -> FPEYRSQRAGGMISSKI (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:10887142,
FT                   ECO:0000303|PubMed:11162584"
FT                   /id="VSP_005481"
FT   VARIANT         4
FT                   /note="G -> S (in dbSNP:rs11465228)"
FT                   /evidence="ECO:0000269|PubMed:10887142"
FT                   /id="VAR_057066"
FT   VARIANT         133
FT                   /note="R -> Q (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs200894535)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036146"
FT   VARIANT         298
FT                   /note="A -> T (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs1178207005)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036147"
FT   VARIANT         609
FT                   /note="H -> Q (in a pancreatic ductal adenocarcinoma
FT                   sample; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:18772397"
FT                   /id="VAR_062670"
FT   CONFLICT        32
FT                   /note="R -> SK (in Ref. 1; AAG50282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="D -> V (in Ref. 1; AAG50282 and 5; AAF22162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622
FT                   /note="D -> N (in Ref. 1; AAG50282 and 5; AAF22162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   955 AA;  104997 MW;  9C9D42BED18BF7F9 CRC64;
     MPGGAGAARL CLLAFALQPL RPRAAREPGW TRGSEEGSPK LQHELIIPQW KTSESPVREK
     HPLKAELRVM AEGRELILDL EKNEQLFAPS YTETHYTSSG NPQTTTRKLE DHCFYHGTVR
     ETELSSVTLS TCRGIRGLIT VSSNLSYVIE PLPDSKGQHL IYRSEHLKPP PGNCGFEHSK
     PTTRDWALQF TQQTKKRPRR MKREDLNSMK YVELYLVADY LEFQKNRRDQ DATKHKLIEI
     ANYVDKFYRS LNIRIALVGL EVWTHGNMCE VSENPYSTLW SFLSWRRKLL AQKYHDNAQL
     ITGMSFHGTT IGLAPLMAMC SVYQSGGVNM DHSENAIGVA ATMAHEMGHN FGMTHDSADC
     CSASAADGGC IMAAATGHPF PKVFNGCNRR ELDRYLQSGG GMCLSNMPDT RMLYGGRRCG
     NGYLEDGEEC DCGEEEECNN PCCNASNCTL RPGAECAHGS CCHQCKLLAP GTLCREQARQ
     CDLPEFCTGK SPHCPTNFYQ MDGTPCEGGQ AYCYNGMCLT YQEQCQQLWG PGARPAPDLC
     FEKVNVAGDT FGNCGKDMNG EHRKCNMRDA KCGKIQCQSS EARPLESNAV PIDTTIIMNG
     RQIQCRGTHV YRGPEEEGDM LDPGLVMTGT KCGYNHICFE GQCRNTSFFE TEGCGKKCNG
     HGVCNNNQNC HCLPGWAPPF CNTPGHGGSI DSGPMPPESV GPVVAGVLVA ILVLAVLMLM
     YYCCRQNNKL GQLKPSALPS KLRQQFSCPF RVSQNSGTGH ANPTFKLQTP QGKRKVINTP
     EILRKPSQPP PRPPPDYLRG GSPPAPLPAH LSRAARNSPG PGSQIERTES SRRPPPSRPI
     PPAPNCIVSQ DFSRPRPPQK ALPANPVPGR RSLPRPGGAS PLRPPGAGPQ QSRPLAALAP
     KVSPREALKV KAGTRGLQGG RCRVEKTKQF MLLVVWTELP EQKPRAKHSC FLVPA
//