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Database: UniProt
Entry: O35674
LinkDB: O35674
Original site: O35674 
ID   ADA19_MOUSE             Reviewed;         920 AA.
AC   O35674;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   16-JAN-2019, entry version 159.
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   Flags: Precursor;
GN   Name=Adam19; Synonyms=Mltnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Myoblast;
RX   PubMed=9461614; DOI=10.1074/jbc.273.7.4180;
RA   Inoue D., Reid M.S., Lum L., Kraetzschmar J., Weskamp G., Myung Y.M.,
RA   Baron R., Blobel C.P.;
RT   "Cloning and initial characterization of mouse meltrin beta and
RT   analysis of the expression of four metalloprotease-disintegrins in
RT   bone cells.";
RL   J. Biol. Chem. 273:4180-4187(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Myoblast;
RX   PubMed=9622634; DOI=10.1016/S0925-4773(98)00043-4;
RA   Kurisaki T., Masuda A., Osumi N., Nabeshima Y., Fujisawa-Sehara A.;
RT   "Spatially- and temporally-restricted expression of meltrin alpha
RT   (ADAM12) and beta (ADAM19) in mouse embryo.";
RL   Mech. Dev. 73:211-215(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 429-578.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=7566181; DOI=10.1038/377652a0;
RA   Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.,
RA   Fujisawa-Sehara A.;
RT   "A metalloprotease-disintegrin participating in myoblast fusion.";
RL   Nature 377:652-656(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=11116142; DOI=10.1074/jbc.M007913200;
RA   Shirakabe K., Wakatsuki S., Kurisaki T., Fujisawa-Sehara A.;
RT   "Roles of Meltrin beta /ADAM19 in the processing of neuregulin.";
RL   J. Biol. Chem. 276:9352-9358(2001).
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, ECO:0000269|PubMed:11116142}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression
CC       in bone, heart and lung, followed by brain and spleen and
CC       relatively low expression in liver, skeletal muscle, kidney and
CC       testis. In bone, primarily expressed in cell of the osteoblast
CC       lineage and not detected in mature osteoclasts.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the heart and in the tail bud at
CC       8.0 dpc, and then in the cranial and dorsal root ganglia. Also
CC       expressed weakly and transiently in the intestine, lung and in
CC       bone marrow. {ECO:0000269|PubMed:9622634}.
CC   -!- INDUCTION: By calcitriol and during osteoblast differentiation.
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; AF019887; AAC40037.1; -; mRNA.
DR   EMBL; D50410; BAA18923.2; -; mRNA.
DR   CCDS; CCDS24571.1; -.
DR   PIR; PC7067; PC7067.
DR   RefSeq; NP_033746.1; NM_009616.4.
DR   UniGene; Mm.89940; -.
DR   ProteinModelPortal; O35674; -.
DR   SMR; O35674; -.
DR   STRING; 10090.ENSMUSP00000011400; -.
DR   MEROPS; M12.214; -.
DR   iPTMnet; O35674; -.
DR   PhosphoSitePlus; O35674; -.
DR   EPD; O35674; -.
DR   PaxDb; O35674; -.
DR   PeptideAtlas; O35674; -.
DR   PRIDE; O35674; -.
DR   DNASU; 11492; -.
DR   Ensembl; ENSMUST00000011400; ENSMUSP00000011400; ENSMUSG00000011256.
DR   GeneID; 11492; -.
DR   KEGG; mmu:11492; -.
DR   UCSC; uc007iny.2; mouse.
DR   CTD; 8728; -.
DR   MGI; MGI:105377; Adam19.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000158971; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; O35674; -.
DR   KO; K08608; -.
DR   OMA; CNRKELD; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; O35674; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-8941237; Invadopodia formation.
DR   PRO; PR:O35674; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000011256; Expressed in 271 organ(s), highest expression level in decidua.
DR   ExpressionAtlas; O35674; baseline and differential.
DR   Genevisible; O35674; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IMP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:MGI.
DR   GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR   GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS: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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; SH3-binding; Signal;
KW   Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   PROPEP       27    204       {ECO:0000250}.
FT                                /FTId=PRO_0000029104.
FT   CHAIN       205    920       Disintegrin and metalloproteinase domain-
FT                                containing protein 19.
FT                                /FTId=PRO_0000029105.
FT   TOPO_DOM     27    703       Extracellular. {ECO:0000255}.
FT   TRANSMEM    704    724       Helical. {ECO:0000255}.
FT   TOPO_DOM    725    920       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      211    409       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      417    503       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      654    686       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       131    138       Cysteine switch. {ECO:0000250}.
FT   MOTIF       835    846       SH3-binding. {ECO:0000255}.
FT   COMPBIAS    435    438       Poly-Glu.
FT   COMPBIAS    504    653       Cys-rich.
FT   COMPBIAS    616    621       Poly-Glu.
FT   ACT_SITE    347    347
FT   METAL       133    133       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       346    346       Zinc; catalytic.
FT   METAL       350    350       Zinc; catalytic.
FT   METAL       356    356       Zinc; catalytic.
FT   CARBOHYD    145    145       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    445    445       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    649    649       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    321    404       {ECO:0000250}.
FT   DISULFID    361    388       {ECO:0000250}.
FT   DISULFID    362    371       {ECO:0000250}.
FT   DISULFID    475    495       {ECO:0000250}.
FT   DISULFID    658    668       {ECO:0000250}.
FT   DISULFID    662    674       {ECO:0000250}.
FT   DISULFID    676    685       {ECO:0000250}.
SQ   SEQUENCE   920 AA;  100860 MW;  7094FDD4EE547382 CRC64;
     MPGRAGVARF CLLALALQLH WPLAACEPGW TTRGSQEGSP PLQHELIIPQ WRTSESPGRG
     KHPLRAELRV MAEGRELILD LEKNEHLFAP AYTETCYTAS GNPQTSTLKS EDHCFYHGTV
     RDVDESSVTL STCRGIRGLI IVRSNLSYII EPVPNSDSQH RIYRSEHLTL PPGNCGFEHS
     GPTSKDWALQ FTHQTKKQPR RMKREDLHSM KYVELYLVAD YAEFQKNRHD QDATKRKLME
     IANYVDKFYR SLNIRIALVG LEVWTHGDKC EVSENPYSTL WSFLSWRRKL LAQKSHDNAQ
     LITGRSFQGT TIGLAPLMAM CSVYQSGGVS MDHSENAIGV ASTVAHEIGH NFGMSHDSAH
     CCSASAADGG CIMAAATGHP FPKVFSWCNR KELDRYLQTG GGMCLSNMPD TRTLYGGRRC
     GNGYLEDGEE CDCGEEEECK NPCCNASNCT LKEGAECAHG SCCHQCKLVA PGTQCREQVR
     QCDLPEFCTG KSPHCPTNYY QMDGTPCEGG QAYCYNGMCL TYQEQCQQLW GPGARPALDL
     CFERVNAAGD TYGNCGKGLN GQYRKCSPRD AKCGKIQCQS TQARPLESNA VSIDTTITLN
     GRRIHCRGTH VYRGPEEEEG EGDMLDPGLV MTGTKCGHNH ICFEGQCRNT SFFETEGCGK
     KCNGHGVCNN NKNCHCFPGW SPPFCNTPGD GGSVDSGPLP PKSVGPVIAG VFSALFVLAV
     LVLLCHCYRQ SHKLGKPSAL PFKLRHQFSC PFRVSQSGGT GHANPTFKLQ TPQGKRKVTN
     TPESLRKPSH PPPRPPPDYL RVESPPAPLP AHLNRAAGSS PEAGARIERK ESARRPPPSR
     PMPPAPNCLL SQDFSRPRPP QKALPANPVP GQRTGPRSGG TSLLQPPTSG PQPPRPPAVP
     VPKLPEYRSQ RVGAIISSKI
//
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