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   24-JAN-2024, entry version 170.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND 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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., 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., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., 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 project:
RT   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., Kreutz M.;
RT   "Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19
RT   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., Moore R.J.,
RA   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., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   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   -!- 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 in
CC       immature DC. {ECO:0000269|PubMed:14632642, ECO:0000269|PubMed:9271581}.
CC   -!- INDUCTION: Induced during DC maturation and up-regulated in response to
CC       T-cell signals. In macrophage up-regulated by bacterial
CC       lipopolysaccharides (LPS). Up-regulated by 1-alpha,25-dihydroxyvitamin
CC       D3 during differentiation of primary monocyte into macrophage.
CC       {ECO:0000269|PubMed:14632642, ECO:0000269|PubMed:9271581}.
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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   AlphaFoldDB; O15204; -.
DR   SMR; O15204; -.
DR   IntAct; O15204; 1.
DR   STRING; 9606.ENSP00000256412; -.
DR   MEROPS; M12.219; -.
DR   GlyConnect; 1910; 19 N-Linked glycans (2 sites).
DR   GlyCosmos; O15204; 4 sites, 25 glycans.
DR   GlyGen; O15204; 4 sites, 25 N-linked glycans (2 sites).
DR   iPTMnet; O15204; -.
DR   PhosphoSitePlus; O15204; -.
DR   BioMuta; ADAMDEC1; -.
DR   EPD; O15204; -.
DR   jPOST; O15204; -.
DR   MassIVE; O15204; -.
DR   PaxDb; 9606-ENSP00000256412; -.
DR   PeptideAtlas; O15204; -.
DR   ProteomicsDB; 48507; -. [O15204-1]
DR   ProteomicsDB; 48508; -. [O15204-2]
DR   Antibodypedia; 22827; 188 antibodies from 29 providers.
DR   DNASU; 27299; -.
DR   Ensembl; ENST00000256412.8; ENSP00000256412.4; ENSG00000134028.14. [O15204-1]
DR   Ensembl; ENST00000522298.1; ENSP00000428993.1; ENSG00000134028.14. [O15204-2]
DR   GeneID; 27299; -.
DR   KEGG; hsa:27299; -.
DR   MANE-Select; ENST00000256412.8; ENSP00000256412.4; NM_014479.3; NP_055294.1.
DR   UCSC; uc003xdz.2; human. [O15204-1]
DR   AGR; HGNC:16299; -.
DR   CTD; 27299; -.
DR   DisGeNET; 27299; -.
DR   GeneCards; ADAMDEC1; -.
DR   HGNC; HGNC:16299; ADAMDEC1.
DR   HPA; ENSG00000134028; Tissue enriched (intestine).
DR   MIM; 606393; gene.
DR   neXtProt; NX_O15204; -.
DR   OpenTargets; ENSG00000134028; -.
DR   PharmGKB; PA24535; -.
DR   VEuPathDB; HostDB:ENSG00000134028; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00900000141143; -.
DR   HOGENOM; CLU_012714_8_0_1; -.
DR   InParanoid; O15204; -.
DR   OMA; ITKPVCG; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; O15204; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; O15204; -.
DR   SignaLink; O15204; -.
DR   BioGRID-ORCS; 27299; 8 hits in 1149 CRISPR screens.
DR   ChiTaRS; ADAMDEC1; human.
DR   GenomeRNAi; 27299; -.
DR   Pharos; O15204; Tbio.
DR   PRO; PR:O15204; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O15204; Protein.
DR   Bgee; ENSG00000134028; Expressed in jejunal mucosa and 111 other cell types or tissues.
DR   ExpressionAtlas; O15204; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
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; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF125; ADAM DEC1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; O15204; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..205
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000029146"
FT   CHAIN           206..470
FT                   /note="ADAM DEC1"
FT                   /id="PRO_0000029147"
FT   DOMAIN          218..412
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          420..470
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   REGION          173..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19139490"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        466
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        328..407
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..374
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..79
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043124"
FT   VARIANT         121
FT                   /note="M -> T (in dbSNP:rs7007084)"
FT                   /id="VAR_024598"
FT   VARIANT         444
FT                   /note="N -> S (in dbSNP:rs3765124)"
FT                   /id="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
//