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 12-SEP-2018, entry version 155. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; ENSGT00910000144014; -. DR HOGENOM; HOG000230883; -. DR HOVERGEN; HBG006978; -. DR InParanoid; O35674; -. DR KO; K08608; -. DR OMA; GGMCLSN; -. DR OrthoDB; EOG091G01NX; -. 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:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI. 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; IEA:Ensembl. DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. 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 //