GenomeNet

Database: UniProt
Entry: Q923W9
LinkDB: Q923W9
Original site: Q923W9 
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   13-FEB-2019, entry version 143.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   with 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
CC       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
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC       {ECO:0000250}.
DR   EMBL; AB059633; BAB84337.1; -; mRNA.
DR   EMBL; AB059632; BAB84336.1; -; mRNA.
DR   EMBL; AF472524; AAL79834.1; -; mRNA.
DR   EMBL; AL833771; CAM18045.1; -; 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   UniGene; Mm.108550; -.
DR   ProteinModelPortal; Q923W9; -.
DR   SMR; Q923W9; -.
DR   STRING; 10090.ENSMUSP00000105861; -.
DR   MEROPS; M12.244; -.
DR   PhosphoSitePlus; Q923W9; -.
DR   PaxDb; Q923W9; -.
DR   PRIDE; Q923W9; -.
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   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000158971; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q923W9; -.
DR   KO; K08616; -.
DR   OMA; GDCCAHC; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q923W9; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q923W9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027318; Expressed in 106 organ(s), highest expression level in ascending aorta.
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:0042035; P:regulation of cytokine biosynthetic process; 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; IPR013032; EGF-like_CS.
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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   PROPEP       30    204       {ECO:0000250}.
FT                                /FTId=PRO_0000029144.
FT   CHAIN       205    797       Disintegrin and metalloproteinase domain-
FT                                containing protein 33.
FT                                /FTId=PRO_0000029145.
FT   TOPO_DOM     30    702       Extracellular. {ECO:0000255}.
FT   TRANSMEM    703    723       Helical. {ECO:0000255}.
FT   TOPO_DOM    724    797       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      211    410       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      418    504       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      650    682       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       132    139       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    504    649       Cys-rich.
FT   COMPBIAS    767    772       Poly-Pro.
FT   ACT_SITE    347    347       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       134    134       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       346    346       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9BZ11}.
FT   METAL       350    350       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9BZ11}.
FT   METAL       356    356       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:Q9BZ11}.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    277    277       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    408    408       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    449    449       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    321    405       {ECO:0000250|UniProtKB:Q9BZ11}.
FT   DISULFID    361    389       {ECO:0000250|UniProtKB:Q9BZ11}.
FT   DISULFID    362    372       {ECO:0000250|UniProtKB:Q9BZ11}.
FT   DISULFID    476    496       {ECO:0000250}.
FT   DISULFID    654    664       {ECO:0000250}.
FT   DISULFID    658    670       {ECO:0000250}.
FT   DISULFID    672    681       {ECO:0000250}.
FT   VAR_SEQ     637    662       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11814695}.
FT                                /FTId=VSP_005496.
FT   CONFLICT     68     68       L -> P (in Ref. 1; BAB84336/BAB84337).
FT                                {ECO:0000305}.
FT   CONFLICT    319    326       GICRAESS -> DMPRGELSF (in Ref. 5;
FT                                AAK67164). {ECO:0000305}.
FT   CONFLICT    725    725       Missing (in Ref. 5; AAK67164).
FT                                {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
//
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