ADEC1_HUMAN
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 03-AUG-2022, entry version 162.
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 GlyGen; O15204; 4 sites, 24 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; O15204; -.
DR PeptideAtlas; O15204; -.
DR PRIDE; O15204; -.
DR ProteomicsDB; 48507; -. [O15204-1]
DR ProteomicsDB; 48508; -. [O15204-2]
DR Antibodypedia; 22827; 172 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 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 PhylomeDB; O15204; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; O15204; -.
DR SignaLink; O15204; -.
DR BioGRID-ORCS; 27299; 7 hits in 1072 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 tissues.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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
