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Disintegrin and metalloproteinase domain-containing protein 19 (ADAM 19) (EC 3.4.24.-) (Meltrin-beta) (Metalloprotease and disintegrin dendritic antigen marker) (MADDAM)

 ADA19_HUMAN             Reviewed;         955 AA.
Q9H013; Q9BZL5; Q9UHP2;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
12-SEP-2018, entry version 172.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 19;
Short=ADAM 19;
EC=3.4.24.-;
AltName: Full=Meltrin-beta;
AltName: Full=Metalloprotease and disintegrin dendritic antigen marker;
Short=MADDAM;
Flags: Precursor;
Name=ADAM19; Synonyms=MLTNB; ORFNames=FKSG34;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Wang Y.-G., Gong L.;
"Identification of FKSG34, a novel human gene encoding for
metalloprotease-disintegrin meltrin beta.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT SER-4.
TISSUE=Lymph node;
PubMed=10887142;
Fritsche J., Moser M., Faust S., Peuker A., Buettner R., Andreesen R.,
Kreutz M.;
"Molecular cloning and characterization of a human metalloprotease
disintegrin a novel marker for dendritic cell differentiation.";
Blood 96:732-739(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Dendritic cell;
PubMed=11162584; DOI=10.1006/bbrc.2000.4200;
Wei P., Zhao Y.-G., Zhuang L., Ruben S., Sang Q.-X.A.;
"Expression and enzymatic activity of human disintegrin and
metalloproteinase ADAM19/meltrin beta.";
Biochem. Biophys. Res. Commun. 280:744-755(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-955 (ISOFORM A).
Xu R., Cai J., Ying B., Wang F., Xu T., Zhao S., Li C.;
"Partial sequence of Homo sapiens ADAM19.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH SH3PXD2A.
PubMed=12615925; DOI=10.1074/jbc.M300267200;
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M.,
Courtneidge S.A.;
"The adaptor protein fish associates with members of the ADAMs family
and localizes to podosomes of Src-transformed cells.";
J. Biol. Chem. 278:16844-16851(2003).
[7]
VARIANTS [LARGE SCALE ANALYSIS] GLN-133 AND THR-298.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[8]
VARIANT [LARGE SCALE ANALYSIS] GLN-609.
PubMed=18772397; DOI=10.1126/science.1164368;
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B.,
Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T.,
Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D.,
Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C.,
Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N.,
Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.;
"Core signaling pathways in human pancreatic cancers revealed by
global genomic analyses.";
Science 321:1801-1806(2008).
-!- FUNCTION: Participates in the proteolytic processing of beta-type
neuregulin isoforms which are involved in neurogenesis and
synaptogenesis, suggesting a regulatory role in glial cell. Also
cleaves alpha-2 macroglobulin. May be involved in osteoblast
differentiation and/or osteoblast activity in bone (By
similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with SH3PXD2A. {ECO:0000269|PubMed:12615925}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q9H013-1; Sequence=Displayed;
Name=B;
IsoId=Q9H013-2; Sequence=VSP_005481;
-!- TISSUE SPECIFICITY: Expressed in many normal organ tissues and
several cancer cell lines.
-!- INDUCTION: By 1,25(OH)2VD3 in monocytes.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
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EMBL; AF326918; AAG50282.1; -; mRNA.
EMBL; Y13786; CAC20585.1; -; mRNA.
EMBL; AF311317; AAK07852.1; -; mRNA.
EMBL; AC008676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF134707; AAF22162.1; -; mRNA.
CCDS; CCDS4338.1; -. [Q9H013-2]
RefSeq; NP_150377.1; NM_033274.4. [Q9H013-2]
RefSeq; XP_005266060.1; XM_005266003.2. [Q9H013-1]
UniGene; Hs.483944; -.
ProteinModelPortal; Q9H013; -.
SMR; Q9H013; -.
BioGrid; 114267; 3.
IntAct; Q9H013; 3.
MINT; Q9H013; -.
STRING; 9606.ENSP00000257527; -.
MEROPS; M12.214; -.
iPTMnet; Q9H013; -.
PhosphoSitePlus; Q9H013; -.
DMDM; 302393821; -.
MaxQB; Q9H013; -.
PaxDb; Q9H013; -.
PeptideAtlas; Q9H013; -.
PRIDE; Q9H013; -.
ProteomicsDB; 80195; -.
ProteomicsDB; 80196; -. [Q9H013-2]
DNASU; 8728; -.
Ensembl; ENST00000257527; ENSP00000257527; ENSG00000135074. [Q9H013-2]
Ensembl; ENST00000517905; ENSP00000428654; ENSG00000135074. [Q9H013-1]
GeneID; 8728; -.
KEGG; hsa:8728; -.
UCSC; uc003lwz.5; human. [Q9H013-1]
CTD; 8728; -.
DisGeNET; 8728; -.
EuPathDB; HostDB:ENSG00000135074.15; -.
GeneCards; ADAM19; -.
HGNC; HGNC:197; ADAM19.
HPA; HPA055537; -.
MIM; 603640; gene.
neXtProt; NX_Q9H013; -.
OpenTargets; ENSG00000135074; -.
PharmGKB; PA24514; -.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144014; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9H013; -.
KO; K08608; -.
OMA; GGMCLSN; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q9H013; -.
TreeFam; TF314733; -.
Reactome; R-HSA-8941237; Invadopodia formation.
SABIO-RK; Q9H013; -.
SIGNOR; Q9H013; -.
ChiTaRS; ADAM19; human.
GeneWiki; ADAM19; -.
GenomeRNAi; 8728; -.
PRO; PR:Q9H013; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000135074; Expressed in 209 organ(s), highest expression level in blood.
CleanEx; HS_ADAM19; -.
ExpressionAtlas; Q9H013; baseline and differential.
Genevisible; Q9H013; HS.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IEP:UniProtKB.
GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR033596; ADAM19.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
PANTHER; PTHR11905:SF19; PTHR11905:SF19; 1.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Polymorphism; Protease; Reference proteome;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 202 {ECO:0000250}.
/FTId=PRO_0000029102.
CHAIN 203 955 Disintegrin and metalloproteinase domain-
containing protein 19.
/FTId=PRO_0000029103.
TOPO_DOM 203 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 720 Helical. {ECO:0000255}.
TOPO_DOM 721 955 Cytoplasmic. {ECO:0000255}.
DOMAIN 210 408 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 416 502 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 650 682 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 130 137 Cysteine switch. {ECO:0000250}.
MOTIF 833 844 SH3-binding. {ECO:0000255}.
COMPBIAS 434 437 Poly-Glu.
COMPBIAS 502 649 Cys-rich.
ACT_SITE 346 346 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 132 132 Zinc; in inhibited form. {ECO:0000250}.
METAL 345 345 Zinc; catalytic. {ECO:0000250}.
METAL 349 349 Zinc; catalytic. {ECO:0000250}.
METAL 355 355 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 320 403 {ECO:0000250}.
DISULFID 360 387 {ECO:0000250}.
DISULFID 361 370 {ECO:0000250}.
DISULFID 474 494 {ECO:0000250}.
DISULFID 654 664 {ECO:0000250}.
DISULFID 658 670 {ECO:0000250}.
DISULFID 672 681 {ECO:0000250}.
VAR_SEQ 902 955 VSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQ
KPRAKHSCFLVPA -> FPEYRSQRAGGMISSKI (in
isoform B). {ECO:0000303|PubMed:10887142,
ECO:0000303|PubMed:11162584}.
/FTId=VSP_005481.
VARIANT 4 4 G -> S (in dbSNP:rs11465228).
{ECO:0000269|PubMed:10887142}.
/FTId=VAR_057066.
VARIANT 133 133 R -> Q (in a colorectal cancer sample;
somatic mutation; dbSNP:rs200894535).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036146.
VARIANT 298 298 A -> T (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036147.
VARIANT 609 609 H -> Q (in a pancreatic ductal
adenocarcinoma sample; somatic mutation).
{ECO:0000269|PubMed:18772397}.
/FTId=VAR_062670.
CONFLICT 32 32 R -> SK (in Ref. 1; AAG50282).
{ECO:0000305}.
CONFLICT 557 557 D -> V (in Ref. 1; AAG50282 and 5;
AAF22162). {ECO:0000305}.
CONFLICT 622 622 D -> N (in Ref. 1; AAG50282 and 5;
AAF22162). {ECO:0000305}.
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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