GenomeNet

Database: UniProt
Entry: Q9H013
LinkDB: Q9H013
Original site: Q9H013 
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   13-FEB-2019, entry version 176.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   metalloprotease-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.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   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
RT   and 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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   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.,
RA   Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
RA   Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
RA   Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
RA   Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
RA   Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
RT   "Core signaling pathways in human pancreatic cancers revealed by
RT   global 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
CC       similarity). {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   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       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
CC       several cancer cell lines.
CC   -!- INDUCTION: By 1,25(OH)2VD3 in monocytes.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC       {ECO:0000250}.
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. [Q9H013-1]
DR   UniGene; Hs.483944; -.
DR   ProteinModelPortal; Q9H013; -.
DR   SMR; Q9H013; -.
DR   BioGrid; 114267; 3.
DR   IntAct; Q9H013; 3.
DR   MINT; Q9H013; -.
DR   STRING; 9606.ENSP00000257527; -.
DR   MEROPS; M12.214; -.
DR   iPTMnet; Q9H013; -.
DR   PhosphoSitePlus; Q9H013; -.
DR   BioMuta; ADAM19; -.
DR   DMDM; 302393821; -.
DR   jPOST; Q9H013; -.
DR   MaxQB; Q9H013; -.
DR   PaxDb; Q9H013; -.
DR   PeptideAtlas; Q9H013; -.
DR   PRIDE; Q9H013; -.
DR   ProteomicsDB; 80195; -.
DR   ProteomicsDB; 80196; -. [Q9H013-2]
DR   DNASU; 8728; -.
DR   Ensembl; ENST00000257527; ENSP00000257527; ENSG00000135074. [Q9H013-2]
DR   Ensembl; ENST00000517905; ENSP00000428654; ENSG00000135074. [Q9H013-1]
DR   GeneID; 8728; -.
DR   KEGG; hsa:8728; -.
DR   UCSC; uc003lwz.5; human. [Q9H013-1]
DR   CTD; 8728; -.
DR   DisGeNET; 8728; -.
DR   EuPathDB; HostDB:ENSG00000135074.15; -.
DR   GeneCards; ADAM19; -.
DR   HGNC; HGNC:197; ADAM19.
DR   HPA; HPA055537; -.
DR   MIM; 603640; gene.
DR   neXtProt; NX_Q9H013; -.
DR   OpenTargets; ENSG00000135074; -.
DR   PharmGKB; PA24514; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000159624; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9H013; -.
DR   KO; K08608; -.
DR   OMA; CNRKELD; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9H013; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-HSA-8941237; Invadopodia formation.
DR   SABIO-RK; Q9H013; -.
DR   SIGNOR; Q9H013; -.
DR   ChiTaRS; ADAM19; human.
DR   GeneWiki; ADAM19; -.
DR   GenomeRNAi; 8728; -.
DR   PRO; PR:Q9H013; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000135074; Expressed in 209 organ(s), highest expression level in blood.
DR   ExpressionAtlas; Q9H013; baseline and differential.
DR   Genevisible; Q9H013; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:InterPro.
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   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR033596; ADAM19.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
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:SF19; PTHR11905:SF19; 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; SSF57552; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Polymorphism; Protease; Reference proteome;
KW   SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc;
KW   Zymogen.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   PROPEP       26    202       {ECO:0000250}.
FT                                /FTId=PRO_0000029102.
FT   CHAIN       203    955       Disintegrin and metalloproteinase domain-
FT                                containing protein 19.
FT                                /FTId=PRO_0000029103.
FT   TOPO_DOM    203    699       Extracellular. {ECO:0000255}.
FT   TRANSMEM    700    720       Helical. {ECO:0000255}.
FT   TOPO_DOM    721    955       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      210    408       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      416    502       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      650    682       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       130    137       Cysteine switch. {ECO:0000250}.
FT   MOTIF       833    844       SH3-binding. {ECO:0000255}.
FT   COMPBIAS    434    437       Poly-Glu.
FT   COMPBIAS    502    649       Cys-rich.
FT   ACT_SITE    346    346       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       132    132       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       345    345       Zinc; catalytic. {ECO:0000250}.
FT   METAL       349    349       Zinc; catalytic. {ECO:0000250}.
FT   METAL       355    355       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    444    444       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    447    447       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    320    403       {ECO:0000250}.
FT   DISULFID    360    387       {ECO:0000250}.
FT   DISULFID    361    370       {ECO:0000250}.
FT   DISULFID    474    494       {ECO:0000250}.
FT   DISULFID    654    664       {ECO:0000250}.
FT   DISULFID    658    670       {ECO:0000250}.
FT   DISULFID    672    681       {ECO:0000250}.
FT   VAR_SEQ     902    955       VSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQ
FT                                KPRAKHSCFLVPA -> FPEYRSQRAGGMISSKI (in
FT                                isoform B). {ECO:0000303|PubMed:10887142,
FT                                ECO:0000303|PubMed:11162584}.
FT                                /FTId=VSP_005481.
FT   VARIANT       4      4       G -> S (in dbSNP:rs11465228).
FT                                {ECO:0000269|PubMed:10887142}.
FT                                /FTId=VAR_057066.
FT   VARIANT     133    133       R -> Q (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs200894535).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036146.
FT   VARIANT     298    298       A -> T (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs1178207005).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036147.
FT   VARIANT     609    609       H -> Q (in a pancreatic ductal
FT                                adenocarcinoma sample; somatic mutation).
FT                                {ECO:0000269|PubMed:18772397}.
FT                                /FTId=VAR_062670.
FT   CONFLICT     32     32       R -> SK (in Ref. 1; AAG50282).
FT                                {ECO:0000305}.
FT   CONFLICT    557    557       D -> V (in Ref. 1; AAG50282 and 5;
FT                                AAF22162). {ECO:0000305}.
FT   CONFLICT    622    622       D -> N (in Ref. 1; AAG50282 and 5;
FT                                AAF22162). {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
//
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