ID AD19_MOUSE STANDARD; PRT; 920 AA. AC O35674; DT 01-MAR-2002 (Rel. 41, Created) DT 01-MAR-2002 (Rel. 41, Last sequence update) DT 01-MAR-2002 (Rel. 41, Last annotation update) DE ADAM 19 precursor (EC 3.4.24.-) (A disintegrin and metalloproteinase DE domain 19) (Meltrin beta). GN ADAM19 OR MLTNB. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Myoblasts; RX MEDLINE=98129833; PubMed=9461614; 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 SEQUENCE FROM N.A., AND DEVELOPMENTAL STAGE. RC TISSUE=Myoblasts; RX MEDLINE=98288128; PubMed=9622634; RA Kurisaki T., Masuda A., Osumi N., Nabeshima Y.-I., 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 SEQUENCE OF 429-578 FROM N.A. RC TISSUE=Embryonic fibroblast; RX MEDLINE=96026308; PubMed=7566181; RA Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.-I., 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; 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 DIFFERENCIATION AND/OR OSTEOBLAST ACTIVITY IN BONE (BY CC SIMILARITY). CC -!- COFACTOR: BINDS ONE ZINC ION (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE 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. CC -!- INDUCTION: BY CALCITRIOL AND DURING OSTEOBLAST DIFFERENTIATION. CC -!- PTM: THE PRECURSOR IS CLEAVED BY A FURIN ENDOPEPTIDASE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M12B. CC -!- SIMILARITY: CONTAINS 1 EGF-LIKE DOMAIN. CC -!- SIMILARITY: CONTAINS 1 DISINTEGRIN DOMAIN. 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; -. DR EMBL; D50410; BAA18923.2; -. DR HSSP; P18619; 1FVL. DR MEROPS; M12.214; -. DR MGD; MGI:105377; Adam19. DR InterPro; IPR001762; Disintegrin. DR InterPro; IPR000561; EGF-like. DR InterPro; IPR002870; Pep_M12B_propep. DR InterPro; IPR001590; Reprolysin. DR InterPro; IPR000130; Zn_MTpeptdse. DR Pfam; PF00200; disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR ProDom; PD000664; Disintegrin; 1. DR SMART; SM00050; DISIN; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; FALSE_NEG. DR PROSITE; PS00427; DISINTEGRIN_1; FALSE_NEG. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Hydrolase; Metalloprotease; Zinc; Signal; Glycoprotein; Zymogen; KW Transmembrane; EGF-like domain; SH3-binding. FT SIGNAL 1 26 POTENTIAL. FT PROPEP 27 204 BY SIMILARITY. FT CHAIN 205 920 ADAM 19. FT DOMAIN 27 703 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 704 724 POTENTIAL. FT DOMAIN 725 920 CYTOPLASMIC (POTENTIAL). FT DOMAIN 211 409 METALLOPROTEASE. FT DOMAIN 417 503 DISINTEGRIN-LIKE. FT DOMAIN 435 438 POLY-GLU. FT DOMAIN 504 653 CYS-RICH. FT DOMAIN 654 686 EGF-LIKE. FT DOMAIN 616 621 POLY-GLU. FT SITE 835 841 SH3-BINDING (POTENTIAL). FT SITE 840 846 SH3-BINDING (POTENTIAL). FT SITE 133 133 CYSTEINE SWITCH (POTENTIAL). FT METAL 346 346 ZINC (CATALYTIC). FT ACT_SITE 347 347 FT METAL 350 350 ZINC (CATALYTIC). FT METAL 356 356 ZINC (CATALYTIC). FT DISULFID 321 404 BY SIMILARITY. FT DISULFID 361 388 BY SIMILARITY. FT DISULFID 466 488 POTENTIAL. FT DISULFID 658 668 BY SIMILARITY. FT DISULFID 662 674 BY SIMILARITY. FT DISULFID 676 685 BY SIMILARITY. FT CARBOHYD 145 145 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 445 445 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 448 448 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 649 649 N-LINKED (GLCNAC...) (POTENTIAL). 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 //