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   24-JAN-2024, entry version 168.
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}.
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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   GlyCosmos; Q923W9; 6 sites, No reported glycans.
DR   GlyGen; Q923W9; 6 sites.
DR   PhosphoSitePlus; Q923W9; -.
DR   PaxDb; 10090-ENSMUSP00000105861; -.
DR   ProteomicsDB; 285666; -. [Q923W9-1]
DR   ProteomicsDB; 285667; -. [Q923W9-2]
DR   Antibodypedia; 7461; 200 antibodies from 34 providers.
DR   DNASU; 110751; -.
DR   Ensembl; ENSMUST00000052104.10; ENSMUSP00000052486.4; ENSMUSG00000027318.18. [Q923W9-2]
DR   Ensembl; ENSMUST00000110232.9; ENSMUSP00000105861.3; ENSMUSG00000027318.18. [Q923W9-1]
DR   Ensembl; ENSMUST00000183552.8; ENSMUSP00000139344.2; ENSMUSG00000027318.18. [Q923W9-1]
DR   GeneID; 110751; -.
DR   KEGG; mmu:110751; -.
DR   UCSC; uc008mkm.2; mouse. [Q923W9-1]
DR   AGR; MGI:1341813; -.
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; MGAQCAH; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q923W9; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-9762292; Regulation of CDH11 function.
DR   BioGRID-ORCS; 110751; 3 hits in 79 CRISPR screens.
DR   PRO; PR:Q923W9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q923W9; Protein.
DR   Bgee; ENSMUSG00000027318; Expressed in ascending aorta and 97 other cell types or tissues.
DR   ExpressionAtlas; Q923W9; baseline and differential.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 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   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF38; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 33; 1.
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; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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.
DR   Genevisible; Q923W9; MM.
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
//