ADA33_MOUSE
ID ADA33_MOUSE Reviewed; 797 AA.
AC Q923W9; Q8R5G5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 33;
DE Short=ADAM 33;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adam33;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=11814695; DOI=10.1016/s0378-1119(01)00818-6;
RA Yoshinaka T., Nishii K., Yamada K., Sawada H., Nishiwaki E., Smith K.,
RA Yoshino K., Ishiguro H., Higashiyama S.;
RT "Identification and characterization of novel mouse and human ADAM33s with
RT potential metalloprotease activity.";
RL Gene 282:227-236(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=NMRI;
RA Karkkainen I., Liehu M.A., Huovila A.-P.J.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 113-797 (ISOFORM 1).
RC STRAIN=Swiss Webster / NIH;
RA Smith K.M., Alfandari D., White J.M., Sutherland A.E., DeSimone D.W.;
RT "M-ADAM33 cloned from mouse embryo day 11 cDNA library.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 562-570 AND 780-797, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9BZ11};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9BZ11};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q923W9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923W9-2; Sequence=VSP_005496;
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
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; AB059633; BAB84337.1; -; mRNA.
DR EMBL; AB059632; BAB84336.1; -; mRNA.
DR EMBL; AF472524; AAL79834.1; -; mRNA.
DR EMBL; AL833771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28296.1; -; Genomic_DNA.
DR EMBL; AF386072; AAK67164.1; -; mRNA.
DR CCDS; CCDS16753.1; -. [Q923W9-1]
DR CCDS; CCDS50716.1; -. [Q923W9-2]
DR RefSeq; NP_291093.2; NM_033615.3. [Q923W9-1]
DR AlphaFoldDB; Q923W9; -.
DR SMR; Q923W9; -.
DR STRING; 10090.ENSMUSP00000105861; -.
DR MEROPS; M12.244; -.
DR GlyGen; Q923W9; 6 sites.
DR PhosphoSitePlus; Q923W9; -.
DR PaxDb; Q923W9; -.
DR PRIDE; Q923W9; -.
DR ProteomicsDB; 285666; -. [Q923W9-1]
DR ProteomicsDB; 285667; -. [Q923W9-2]
DR Antibodypedia; 7461; 195 antibodies from 34 providers.
DR DNASU; 110751; -.
DR Ensembl; ENSMUST00000052104; ENSMUSP00000052486; ENSMUSG00000027318. [Q923W9-2]
DR Ensembl; ENSMUST00000110232; ENSMUSP00000105861; ENSMUSG00000027318. [Q923W9-1]
DR Ensembl; ENSMUST00000183552; ENSMUSP00000139344; ENSMUSG00000027318. [Q923W9-1]
DR GeneID; 110751; -.
DR KEGG; mmu:110751; -.
DR UCSC; uc008mkm.2; mouse. [Q923W9-1]
DR CTD; 80332; -.
DR MGI; MGI:1341813; Adam33.
DR VEuPathDB; HostDB:ENSMUSG00000027318; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158971; -.
DR HOGENOM; CLU_012714_7_2_1; -.
DR InParanoid; Q923W9; -.
DR OMA; ETHYTTD; -.
DR PhylomeDB; Q923W9; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 110751; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q923W9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q923W9; protein.
DR Bgee; ENSMUSG00000027318; Expressed in ascending aorta and 95 other tissues.
DR ExpressionAtlas; Q923W9; baseline and differential.
DR Genevisible; Q923W9; MM.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; NAS:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; 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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
KW Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..204
FT /evidence="ECO:0000250"
FT /id="PRO_0000029144"
FT CHAIN 205..797
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 33"
FT /id="PRO_0000029145"
FT TOPO_DOM 30..702
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 211..410
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 418..504
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 650..682
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 766..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..139
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..405
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT DISULFID 361..389
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT DISULFID 362..372
FT /evidence="ECO:0000250|UniProtKB:Q9BZ11"
FT DISULFID 476..496
FT /evidence="ECO:0000250"
FT DISULFID 654..664
FT /evidence="ECO:0000250"
FT DISULFID 658..670
FT /evidence="ECO:0000250"
FT DISULFID 672..681
FT /evidence="ECO:0000250"
FT VAR_SEQ 637..662
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11814695"
FT /id="VSP_005496"
FT CONFLICT 68
FT /note="L -> P (in Ref. 1; BAB84336/BAB84337)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..326
FT /note="GICRAESS -> DMPRGELSF (in Ref. 5; AAK67164)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="Missing (in Ref. 5; AAK67164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 797 AA; 86971 MW; B332EA909514E626 CRC64;
MGSRCGRPGG SPVLLLLPLL LPSCPLRSAR MFPGNAHGEL VTPHWILEGR LWLKVTLEEP
ILKPDSVLVA LEAEGQDLLL ELEKKHKLLA PGYTETHYRP DGHPVVLSPN HTDHCQYHGR
VRGFRESWVV LSTCSGMSGL IVLSSKVSYY LQPRTPGDTK DFPTHEIFRM EQLFTWRGVQ
RDKNSQYKAG MASLPHVPQS RVRREARRSP RYLELYIVAD HTLFLLQHQN LNHTRQRLLE
VANCVDQILR TLDIQLVLTG LEVWTEQDLS RITQDANETL WAFLQWRRGV WARRPHDSTQ
LLTGRTFQGT TVGLAPVEGI CRAESSGGVS TDHSELPIGT AATMAHEIGH SLGLHHDPEG
CCVQADAEQG GCVMEAATGH PFPRVFSACS RRQLRTFFRK GGGPCLSNTS APGLLVLPSR
CGNGFLEAGE ECDCGSGQKC PDPCCFAHNC SLRAGAQCAH GDCCARCLLK SAGTPCRPAA
TDCDLPEFCT GTSPYCPADV YLLDGSPCAE GRGYCLDGWC PTLEQQCQQL WGPGSKPAPE
PCFQQMNSMG NSQGNCGQDH KGSFLPCAQR DALCGKLLCQ GGEPNPLVPH IVTMDSTILL
EGREVVCRGA FVLPDSHLDQ LDLGLVEPGT GCGPRMVCQD RHCQNATSQE LERCLTACHN
GGVCNSNRNC HCAAGWAPPF CDKPGLGGSV DSGPAQSANR DAFPLAMLLS FLLPLLPGAG
LAWCYYQLPT FCHRRGLCCR RDPLWNRDIP LGSVHPVEFG SIITGEPSPP PPWTSCQQRS
HPPSLDLLSD PANSELT
