ADEC1_MOUSE
ID ADEC1_MOUSE Reviewed; 467 AA.
AC Q9R0X2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, 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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11673514; DOI=10.4049/jimmunol.167.9.5052;
RA Mueller C.G.F., Cremer I., Paulet P.E., Niida S., Maeda N., Lebeque S.,
RA Fridman W.H., Sautes-Fridman C.;
RT "Mannose receptor ligand-positive cells express the metalloprotease decysin
RT in the B cell follicle.";
RL J. Immunol. 167:5052-5060(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12606478; DOI=10.1095/biolreprod.102.009761;
RA Baran N., Kelly P.A., Binart N.;
RT "Decysin, a new member of the metalloproteinase family, is regulated by
RT prolactin and steroids during mouse pregnancy.";
RL Biol. Reprod. 68:1787-1792(2003).
CC -!- FUNCTION: May play an important role in the control of the immune
CC response and during pregnancy.
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.
CC -!- TISSUE SPECIFICITY: Expressed highly in uterus during pregnancy.
CC -!- DEVELOPMENTAL STAGE: From the prepubertal period to day 5.5 of
CC pregnancy is weakly expressed. From day 5.5 of pregnancy, an increase
CC of expression is observed. At day 12.5 expression is higher.
CC {ECO:0000269|PubMed:12606478}.
CC -!- INDUCTION: Induced by immunization in mature dendritic cells (DC), in
CC marginal zone (MZ) metallophils, in follicular DC (FDC) and tingible
CC body macrophages of germinal center. Down-regulated by steroid hormones
CC and PRL. {ECO:0000269|PubMed:12606478}.
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DR EMBL; AJ242912; CAB54557.1; -; mRNA.
DR EMBL; BC046324; AAH46324.1; -; mRNA.
DR CCDS; CCDS49532.1; -.
DR RefSeq; NP_067450.1; NM_021475.2.
DR AlphaFoldDB; Q9R0X2; -.
DR SMR; Q9R0X2; -.
DR STRING; 10090.ENSMUSP00000022641; -.
DR MEROPS; M12.219; -.
DR GlyGen; Q9R0X2; 2 sites.
DR iPTMnet; Q9R0X2; -.
DR PhosphoSitePlus; Q9R0X2; -.
DR CPTAC; non-CPTAC-3557; -.
DR MaxQB; Q9R0X2; -.
DR PaxDb; Q9R0X2; -.
DR PeptideAtlas; Q9R0X2; -.
DR PRIDE; Q9R0X2; -.
DR ProteomicsDB; 281938; -.
DR Antibodypedia; 22827; 172 antibodies from 29 providers.
DR DNASU; 58860; -.
DR Ensembl; ENSMUST00000022641; ENSMUSP00000022641; ENSMUSG00000022057.
DR GeneID; 58860; -.
DR KEGG; mmu:58860; -.
DR UCSC; uc007uls.1; mouse.
DR CTD; 27299; -.
DR MGI; MGI:1917650; Adamdec1.
DR VEuPathDB; HostDB:ENSMUSG00000022057; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00900000141143; -.
DR HOGENOM; CLU_012714_8_0_1; -.
DR InParanoid; Q9R0X2; -.
DR OMA; ITKPVCG; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R0X2; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 58860; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9R0X2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9R0X2; protein.
DR Bgee; ENSMUSG00000022057; Expressed in right colon and 55 other tissues.
DR ExpressionAtlas; Q9R0X2; baseline and differential.
DR Genevisible; Q9R0X2; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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 PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..208
FT /evidence="ECO:0000255"
FT /id="PRO_0000029148"
FT CHAIN 209..467
FT /note="ADAM DEC1"
FT /id="PRO_0000029149"
FT DOMAIN 217..411
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 418..467
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 361
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 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 327..406
FT /evidence="ECO:0000250"
FT DISULFID 368..373
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 52956 MW; 12A0FF346BAD70E2 CRC64;
MLPGTSRLPT EASMSWVLLS VLWLIIQIQV IDATLTPELK PHEIVRPKKL PISQKRGLEN
NQTERYGKEE KYAPEVQYQI ILNGEEIVFH LKRTKHLLGP DYTETSYSPR GEESTRHSQD
VKPCYYEGHI QNARGSLARI STCDGLRGYF THRDQRYQIK PLQSTDEGEH AVLPYSWKGQ
DTVHDKDAEK QVVRKRSHLR TSRSLKNPNE DLLQGQKYIG LFLVLDNAYY KLYNGNVTQM
RTFLFKVLNL LNMIYKTINI QVSLVGMEIW SDQDKIKVEP NLGATFTHFM RWHYSNLGKR
IHNHAQLLSG ASFRHGRVGM AAGNSFCTTS SVSVIEAKKK NNVALVALMS HELGHALGMK
DVPYYTKCPS GSCVMNQYLS SKFPKDFSTV SRSHFQGFLS SRNARCLLLA PDPKNIIKPT
CGNQVLDVGE ECDCGSPEEC TNLCCEPLTC RLKSQPDCSE ASNHITE
