ID AD19_HUMAN STANDARD; PRT; 956 AA. AC Q9H013; Q9BZL5; Q9UHP2; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE ADAM 19 precursor (EC 3.4.24.-) (A disintegrin and metalloproteinase DE domain 19) (Meltrin beta) (Metalloprotease and disintegrin dentritic DE antigen marker) (MADDAM) (FKSG34 protein). GN ADAM19 OR MLTNB OR FKSG34. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (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 SEQUENCE FROM N.A. (ISOFORM B). RC TISSUE=Lymph node; RX MEDLINE=20346928; 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 SEQUENCE FROM N.A. (ISOFORM B). RC TISSUE=Dendritic cell; RX MEDLINE=21092672; PubMed=11162584; 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 SEQUENCE OF 100-956 FROM N.A. (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. 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 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Type I membrane 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 organs tissues and CC several cancer cell lines. CC -!- INDUCTION: By 1,25(OH)2VD3 in monocytes. CC -!- PTM: The precursor is cleaved by a furin endopeptidase (By CC similarity). CC -!- SIMILARITY: Belongs to peptidase family M12B. CC -!- SIMILARITY: Contains 1 disintegrin domain. CC -!- SIMILARITY: Contains 1 EGF-like 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; AF326918; AAG50282.1; -. DR EMBL; Y13786; CAC20585.1; -. DR EMBL; AF311317; AAK07852.1; -. DR EMBL; AF134707; AAF22162.1; -. DR HSSP; P18619; 1FVL. DR MEROPS; M12.214; -. DR Genew; HGNC:197; ADAM19. DR MIM; 603640; -. DR InterPro; IPR006586; ADAM_cysteine. DR InterPro; IPR001762; Disintegrin. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR001818; Pept_M10A_M12B. DR InterPro; IPR006025; Pept_M_Zn_BS. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR ProDom; PD000664; Disintegrin; 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; PS50026; EGF_3; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Hydrolase; Metalloprotease; Zinc; Signal; Glycoprotein; Zymogen; KW Transmembrane; EGF-like domain; SH3-binding; Alternative splicing. FT SIGNAL 1 25 Potential. FT PROPEP 26 203 By similarity. FT CHAIN 204 956 ADAM 19. FT DOMAIN 204 700 Extracellular (Potential). FT TRANSMEM 701 721 Potential. FT DOMAIN 722 956 Cytoplasmic (Potential). FT DOMAIN 204 410 Metalloprotease. FT DOMAIN 416 502 Disintegrin-like. FT DOMAIN 435 438 Poly-Glu. FT DOMAIN 503 650 Cys-rich. FT DOMAIN 651 683 EGF-like. FT SITE 834 840 SH3-binding (Potential). FT SITE 839 845 SH3-binding (Potential). FT SITE 133 133 Cysteine switch (Potential). FT METAL 346 346 Zinc (catalytic) (By similarity). FT ACT_SITE 347 347 By similarity. FT METAL 350 350 Zinc (catalytic) (By similarity). FT METAL 356 356 Zinc (catalytic) (By similarity). FT DISULFID 321 404 By similarity. FT DISULFID 361 388 By similarity. FT DISULFID 475 482 Potential. FT DISULFID 655 665 By similarity. FT DISULFID 659 671 By similarity. FT DISULFID 673 682 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 646 646 N-linked (GlcNAc...) (Potential). FT VARSPLIC 903 956 VSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQ FT KPRAKHSCFLVPA -> FPEYRSQRAGGMISSKI (in FT isoform B). FT /FTId=VSP_005481. FT CONFLICT 4 4 G -> S (in Ref. 2). FT CONFLICT 32 33 SK -> R (in Ref. 2 and 3). FT CONFLICT 558 558 V -> D (in Ref. 2 and 3). FT CONFLICT 623 623 N -> D (in Ref. 2 and 3). SQ SEQUENCE 956 AA; 105038 MW; 8373F10FA0418B12 CRC64; MPGGAGAARL CLLAFALQPL RPRAAREPGW TSKGSEEGSP KLQHELIIPQ WKTSESPVRE KHPLKAELRV MAEGRELILD LEKNEQLFAP SYTETHYTSS GNPQTTTRKL EDHCFYHGTV RETELSSVTL STCRGIRGLI TVSSNLSYVI EPLPDSKGQH LIYRSEHLKP PPGNCGFEHS KPTTRDWALQ FTQQTKKRPR RMKREDLNSM KYVELYLVAD YLEFQKNRRD QDATKHKLIE IANYVDKFYR SLNIRIALVG LEVWTHGNMC EVSENPYSTL WSFLSWRRKL LAQKYHDNAQ LITGMSFHGT TIGLAPLMAM CSVYQSGGVN MDHSENAIGV AATMAHEMGH NFGMTHDSAD CCSASAADGG CIMAAATGHP FPKVFNGCNR RELDRYLQSG GGMCLSNMPD TRMLYGGRRC GNGYLEDGEE CDCGEEEECN NPCCNASNCT LRPGAECAHG SCCHQCKLLA PGTLCREQAR QCDLPEFCTG KSPHCPTNFY QMDGTPCEGG QAYCYNGMCL TYQEQCQQLW GPGARPAPDL CFEKVNVAGD TFGNCGKVMN GEHRKCNMRD AKCGKIQCQS SEARPLESNA VPIDTTIIMN GRQIQCRGTH VYRGPEEEGD MLNPGLVMTG TKCGYNHICF EGQCRNTSFF ETEGCGKKCN GHGVCNNNQN CHCLPGWAPP FCNTPGHGGS IDSGPMPPES VGPVVAGVLV AILVLAVLML MYYCCRQNNK LGQLKPSALP SKLRQQFSCP FRVSQNSGTG HANPTFKLQT PQGKRKVINT PEILRKPSQP PPRPPPDYLR GGSPPAPLPA HLSRAARNSP GPGSQIERTE SSRRPPPSRP IPPAPNCIVS QDFSRPRPPQ KALPANPVPG RRSLPRPGGA SPLRPPGAGP QQSRPLAALA PKVSPREALK VKAGTRGLQG GRCRVEKTKQ FMLLVVWTEL PEQKPRAKHS CFLVPA //