ID ADEC1_HUMAN Reviewed; 470 AA. AC O15204; B7ZAK5; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 2. DT 13-FEB-2019, entry version 145. DE RecName: Full=ADAM DEC1; DE EC=3.4.24.-; DE AltName: Full=A disintegrin and metalloproteinase domain-like protein decysin-1; DE Short=ADAM-like protein decysin-1; DE Flags: Precursor; GN Name=ADAMDEC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP INDUCTION. RX PubMed=9271581; DOI=10.1084/jem.186.5.655; RA Mueller C.G.F., Rissoan M.C., Salinas B., Ait-Yahia S., Ravel O., RA Bridon J.-M., Briere F., Lebecque S., Liu Y.J.; RT "Polymerase chain reaction selects a novel disintegrin proteinase from RT CD40-activated germinal center dendritic cells."; RL J. Exp. Med. 186:655-663(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=14632642; DOI=10.1111/j.1365-2567.2003.01754.x; RA Fritsche J., Muller A., Hausmann M., Rogler G., Andreesen R., RA Kreutz M.; RT "Inverse regulation of the ADAM-family members, decysin and RT MADDAM/ADAM19 during monocyte differentiation."; RL Immunology 110:450-457(2003). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-237. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP GLYCOSYLATION AT ASN-184. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). CC -!- FUNCTION: May play an important role in the control of the immune CC response and during pregnancy. {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O15204-1; Sequence=Displayed; CC Name=2; CC IsoId=O15204-2; Sequence=VSP_043124; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed highly in the small intestine and CC appendix, moderately in lymph node, mucosal lining of the colon, CC thymus, spleen and very weakly in the bone marrow. Predominantly CC expressed in dendritic cells (DC) of the germinal center. Weakly CC expressed in monocyte and highly expressed in macrophage. Absent CC in immature DC. {ECO:0000269|PubMed:14632642, CC ECO:0000269|PubMed:9271581}. CC -!- INDUCTION: Induced during DC maturation and up-regulated in CC response to T-cell signals. In macrophage up-regulated by CC bacterial lipopolysaccharides (LPS). Up-regulated by 1-alpha,25- CC dihydroxyvitamin D3 during differentiation of primary monocyte CC into macrophage. {ECO:0000269|PubMed:14632642, CC ECO:0000269|PubMed:9271581}. 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; Y13323; CAA73764.2; -; mRNA. DR EMBL; AK316320; BAH14691.1; -; mRNA. DR EMBL; AK316322; BAH14693.1; -; mRNA. DR EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069582; AAH69582.1; -; mRNA. DR EMBL; BC074877; AAH74877.1; -; mRNA. DR EMBL; BC074878; AAH74878.1; -; mRNA. DR CCDS; CCDS55212.1; -. [O15204-2] DR CCDS; CCDS6044.1; -. [O15204-1] DR RefSeq; NP_001138743.1; NM_001145271.1. [O15204-2] DR RefSeq; NP_001138744.1; NM_001145272.1. [O15204-2] DR RefSeq; NP_055294.1; NM_014479.3. [O15204-1] DR UniGene; Hs.521459; -. DR UniGene; Hs.688686; -. DR ProteinModelPortal; O15204; -. DR SMR; O15204; -. DR IntAct; O15204; 1. DR STRING; 9606.ENSP00000256412; -. DR MEROPS; M12.219; -. DR GlyConnect; 1910; -. DR iPTMnet; O15204; -. DR PhosphoSitePlus; O15204; -. DR BioMuta; ADAMDEC1; -. DR EPD; O15204; -. DR jPOST; O15204; -. DR PaxDb; O15204; -. DR PeptideAtlas; O15204; -. DR PRIDE; O15204; -. DR ProteomicsDB; 48507; -. DR ProteomicsDB; 48508; -. [O15204-2] DR Ensembl; ENST00000256412; ENSP00000256412; ENSG00000134028. [O15204-1] DR Ensembl; ENST00000522298; ENSP00000428993; ENSG00000134028. [O15204-2] DR GeneID; 27299; -. DR KEGG; hsa:27299; -. DR UCSC; uc003xdz.2; human. [O15204-1] DR CTD; 27299; -. DR DisGeNET; 27299; -. DR EuPathDB; HostDB:ENSG00000134028.14; -. DR GeneCards; ADAMDEC1; -. DR HGNC; HGNC:16299; ADAMDEC1. DR MIM; 606393; gene. DR neXtProt; NX_O15204; -. DR OpenTargets; ENSG00000134028; -. DR PharmGKB; PA24535; -. DR eggNOG; KOG3607; Eukaryota. DR eggNOG; ENOG410XX2M; LUCA. DR GeneTree; ENSGT00900000141143; -. DR HOGENOM; HOG000230883; -. DR HOVERGEN; HBG106501; -. DR InParanoid; O15204; -. DR KO; K08634; -. DR OMA; LRGYFTH; -. DR OrthoDB; 162519at2759; -. DR PhylomeDB; O15204; -. DR TreeFam; TF314733; -. DR ChiTaRS; ADAMDEC1; human. DR GenomeRNAi; 27299; -. DR PRO; PR:O15204; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000134028; Expressed in 112 organ(s), highest expression level in small intestine. DR ExpressionAtlas; O15204; baseline and differential. DR Genevisible; O15204; HS. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0004222; F:metalloendopeptidase activity; NAS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS: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; IPR033613; ADAMDEC1. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. 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:SF125; PTHR11905:SF125; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; SSF57552; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein; KW Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; KW Reference proteome; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1 30 {ECO:0000255}. FT PROPEP 31 205 {ECO:0000255}. FT /FTId=PRO_0000029146. FT CHAIN 206 470 ADAM DEC1. FT /FTId=PRO_0000029147. FT DOMAIN 218 412 Peptidase M12B. {ECO:0000255|PROSITE- FT ProRule:PRU00276}. FT DOMAIN 420 470 Disintegrin. {ECO:0000255|PROSITE- FT ProRule:PRU00068}. FT ACT_SITE 353 353 {ECO:0000255|PROSITE-ProRule:PRU00276, FT ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 352 352 Zinc; catalytic. {ECO:0000250}. FT METAL 356 356 Zinc; catalytic. {ECO:0000250}. FT METAL 362 362 Zinc; catalytic. {ECO:0000255}. FT CARBOHYD 61 61 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 184 184 N-linked (GlcNAc...) (complex) FT asparagine. FT {ECO:0000269|PubMed:19139490}. FT CARBOHYD 237 237 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 466 466 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 328 407 {ECO:0000250}. FT DISULFID 369 374 {ECO:0000250}. FT VAR_SEQ 1 79 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043124. FT VARIANT 121 121 M -> T (in dbSNP:rs7007084). FT /FTId=VAR_024598. FT VARIANT 444 444 N -> S (in dbSNP:rs3765124). FT /FTId=VAR_021848. SQ SEQUENCE 470 AA; 52775 MW; 35A454DD8A6A7E53 CRC64; MLRGISQLPA VATMSWVLLP VLWLIVQTQA IAIKQTPELT LHEIVCPKKL HILHKREIKN NQTEKHGKEE RYEPEVQYQM ILNGEEIILS LQKTKHLLGP DYTETLYSPR GEEITTKPEN MEHCYYKGNI LNEKNSVASI STCDGLRGYF THHHQRYQIK PLKSTDEKEH AVFTSNQEEQ DPANHTCGVK STDGKQGPIR ISRSLKSPEK EDFLRAQKYI DLYLVLDNAF YKNYNENLTL IRSFVFDVMN LLNVIYNTID VQVALVGMEI WSDGDKIKVV PSASTTFDNF LRWHSSNLGK KIHDHAQLLS GISFNNRRVG LAASNSLCSP SSVAVIEAKK KNNVALVGVM SHELGHVLGM PDVPFNTKCP SGSCVMNQYL SSKFPKDFST SCRAHFERYL LSQKPKCLLQ APIPTNIMTT PVCGNHLLEV GEDCDCGSPK ECTNLCCEAL TCKLKPGTDC GGDAPNHTTE //