ADA28_MOUSE
ID ADA28_MOUSE Reviewed; 793 AA.
AC Q9JLN6; Q5D070; Q8K5D2; Q8K5D3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28;
DE Short=ADAM 28;
DE EC=3.4.24.-;
DE AltName: Full=Thymic epithelial cell-ADAM;
DE Short=TECADAM;
DE Flags: Precursor;
GN Name=Adam28;
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] (ISOFORM 3), CHARACTERIZATION, AND MUTAGENESIS
RP OF GLU-343.
RC TISSUE=Lung;
RX PubMed=10794709; DOI=10.1042/bj3480021;
RA Howard L., Maciewicz R.A., Blobel C.P.;
RT "Cloning and characterization of ADAM28: evidence for autocatalytic pro-
RT domain removal and for cell surface localization of mature ADAM28.";
RL Biochem. J. 348:21-27(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=11867223; DOI=10.1016/s0378-1119(01)00871-x;
RA Haidl I.D., Huber G., Eichmann K.;
RT "An ADAM family member with expression in thymic epithelial cells and
RT related tissues.";
RL Gene 283:163-170(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Olfactory epithelium;
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).
CC -!- FUNCTION: May play a role in organogenesis and organ-specific functions
CC such as thymic T-cell development.
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: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9JLN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JLN6-2; Sequence=VSP_005488;
CC Name=3;
CC IsoId=Q9JLN6-3; Sequence=VSP_005489, VSP_005490;
CC -!- TISSUE SPECIFICITY: Strong expression in thymic epithelial cells and
CC developmentally related tissues including the trachea, thyroid, lung
CC and stomach, but not in lymphocytes. Expressed at high levels also in
CC epididymis. In contrast with human is not expressed in immature or
CC mature lymphocyte populations of thymocytes, lymph node, spleen, and
CC bone marrow. {ECO:0000269|PubMed:11867223}.
CC -!- DEVELOPMENTAL STAGE: The expression patterns in adult and day 15.5
CC embryos are similar.
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: Pro-domain removal and maturation may be, at least in part,
CC autocatalytic.
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DR EMBL; AF153350; AAF71993.1; -; mRNA.
DR EMBL; AF163290; AAM21935.1; -; mRNA.
DR EMBL; AF163291; AAM21936.1; -; mRNA.
DR EMBL; AF163292; AAM21937.1; -; mRNA.
DR EMBL; BC058782; AAH58782.1; -; mRNA.
DR CCDS; CCDS36964.1; -. [Q9JLN6-3]
DR CCDS; CCDS36965.1; -. [Q9JLN6-1]
DR CCDS; CCDS88698.1; -. [Q9JLN6-2]
DR RefSeq; NP_001041640.1; NM_001048175.2. [Q9JLN6-3]
DR RefSeq; NP_034212.1; NM_010082.2. [Q9JLN6-1]
DR RefSeq; NP_899222.1; NM_183366.3. [Q9JLN6-2]
DR AlphaFoldDB; Q9JLN6; -.
DR SMR; Q9JLN6; -.
DR BioGRID; 199330; 13.
DR STRING; 10090.ENSMUSP00000022642; -.
DR MEROPS; M12.020; -.
DR GlyGen; Q9JLN6; 7 sites.
DR iPTMnet; Q9JLN6; -.
DR PhosphoSitePlus; Q9JLN6; -.
DR PaxDb; Q9JLN6; -.
DR PRIDE; Q9JLN6; -.
DR ProteomicsDB; 285550; -. [Q9JLN6-1]
DR ProteomicsDB; 285551; -. [Q9JLN6-2]
DR ProteomicsDB; 285552; -. [Q9JLN6-3]
DR Antibodypedia; 58742; 202 antibodies from 24 providers.
DR DNASU; 13522; -.
DR Ensembl; ENSMUST00000022642; ENSMUSP00000022642; ENSMUSG00000014725. [Q9JLN6-1]
DR Ensembl; ENSMUST00000111072; ENSMUSP00000106701; ENSMUSG00000014725. [Q9JLN6-3]
DR Ensembl; ENSMUST00000224039; ENSMUSP00000153354; ENSMUSG00000014725. [Q9JLN6-2]
DR GeneID; 13522; -.
DR KEGG; mmu:13522; -.
DR UCSC; uc007ult.2; mouse. [Q9JLN6-3]
DR UCSC; uc007ulv.1; mouse. [Q9JLN6-1]
DR CTD; 10863; -.
DR MGI; MGI:105988; Adam28.
DR VEuPathDB; HostDB:ENSMUSG00000014725; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156716; -.
DR HOGENOM; CLU_012714_7_1_1; -.
DR InParanoid; Q9JLN6; -.
DR OMA; ICVMDRA; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9JLN6; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 13522; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Adam28; mouse.
DR PRO; PR:Q9JLN6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JLN6; protein.
DR Bgee; ENSMUSG00000014725; Expressed in superior surface of tongue and 91 other tissues.
DR ExpressionAtlas; Q9JLN6; baseline and differential.
DR Genevisible; Q9JLN6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
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; 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; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..195
FT /evidence="ECO:0000250"
FT /id="PRO_0000029132"
FT CHAIN 196..793
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 28"
FT /id="PRO_0000029133"
FT TOPO_DOM 196..668
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 206..402
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 410..496
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 628..660
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 699..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..176
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 703..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 171
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 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
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 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..397
FT /evidence="ECO:0000250"
FT DISULFID 357..381
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 468..488
FT /evidence="ECO:0000250"
FT DISULFID 632..642
FT /evidence="ECO:0000250"
FT DISULFID 636..648
FT /evidence="ECO:0000250"
FT DISULFID 650..659
FT /evidence="ECO:0000250"
FT VAR_SEQ 769..793
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867223"
FT /id="VSP_005488"
FT VAR_SEQ 769..771
FT /note="TGR -> DPN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10794709,
FT ECO:0000303|PubMed:11867223, ECO:0000303|PubMed:15489334"
FT /id="VSP_005489"
FT VAR_SEQ 775..793
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10794709,
FT ECO:0000303|PubMed:11867223, ECO:0000303|PubMed:15489334"
FT /id="VSP_005490"
FT MUTAGEN 343
FT /note="E->A: Abolishes prodomain removal."
FT /evidence="ECO:0000269|PubMed:10794709"
SQ SEQUENCE 793 AA; 88671 MW; 7715E71456D4403B CRC64;
MQQWSLLVVS FLLSPVPVSA IKELPKAKKY EVVYPIRLHP LRKRETQEPE PKETFETELR
YKMTVNGKVA VLYLKKNNKL LAPDYSETYY NSSGNKVTTS PQIMDSCYYQ GHIVNEKVSA
ASISTCQGLR GYISQGDEKY FIEPLSSENL DEQAHALFKD DSNEDQEKSN CGVDDALWLQ
GLHQDVALPA TRLIKLNDGM VQEPKKYIEY YVVLDNGEFK KYNKNLAEIR KIVLEMANYI
NMLYNKLDAH VALVGVEIWT DGDKIKITPD ANTTLENFSK WRGNDLLKRK HHDIAQLISS
TDFSGSTVGL AFMSSMCSPY HSVGIVQDHS NYHLRVAGTM AHEMGHNLGM IHDYLSCKCP
SEVCVMEQSL RFHMPTDFSS CSRVNYKQFL EEKLSHCLFN SPLPSDIIST PVCGNQLLEM
NEDCDCGTPK ECTNKCCDAR TCKIKAGFQC ALGECCEKCQ LKKPGVVCRA AKDECDLPEV
CDGKSSHCPG DRFRVNGSPC QNGHGYCLKG KCPTLQQQCM DMWGPGTKVA NTSCYKQNEG
GTKYGYCHVE NGTHMPCKAK DAMCGKLFCE GGSGDLPWKG LTISFLTCKL FDPEDTSQGV
DMVANGTKCG TNKVCINAEC VDMEKTYKSA NCSSKCKGHA VCDHELQCQC KEGWAPPDCE
NSATVFHFSI VVGVLFPLAV IFVVVAIVIQ RQSARRKQRR VQRLPSTKDA KLHNQKCRPQ
KVKDVQPQEM SQMKKLHVSD LPSEEPEPPP DVLITKPNFP PPPIPVSLTG RAKVPFVKTP
HPFSQQIGRV YLK
