GenomeNet

Database: UniProt
Entry: Q9JLN6
LinkDB: Q9JLN6
Original site: Q9JLN6 
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   13-FEB-2019, entry version 150.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION, AND
RP   MUTAGENESIS 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
RT   pro-domain removal and for cell surface localization of mature
RT   ADAM28.";
RL   Biochem. J. 348:21-27(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in organogenesis and organ-specific
CC       functions 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
CC       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
CC       and developmentally related tissues including the trachea,
CC       thyroid, lung and stomach, but not in lymphocytes. Expressed at
CC       high levels also in epididymis. In contrast with human is not
CC       expressed in immature or mature lymphocyte populations of
CC       thymocytes, lymph node, spleen, and bone marrow.
CC       {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
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: Pro-domain removal and maturation may be, at least in part,
CC       autocatalytic.
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   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   UniGene; Mm.117450; -.
DR   ProteinModelPortal; Q9JLN6; -.
DR   SMR; Q9JLN6; -.
DR   STRING; 10090.ENSMUSP00000022642; -.
DR   MEROPS; M12.020; -.
DR   iPTMnet; Q9JLN6; -.
DR   PhosphoSitePlus; Q9JLN6; -.
DR   PaxDb; Q9JLN6; -.
DR   PRIDE; Q9JLN6; -.
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   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000156716; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9JLN6; -.
DR   KO; K08614; -.
DR   OMA; YYQGHII; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9JLN6; -.
DR   TreeFam; TF314733; -.
DR   PMAP-CutDB; Q9JLN6; -.
DR   PRO; PR:Q9JLN6; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000014725; Expressed in 118 organ(s), highest expression level in skeletal muscle tissue.
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: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   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; Complete proteome; 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     20       {ECO:0000255}.
FT   PROPEP       21    195       {ECO:0000250}.
FT                                /FTId=PRO_0000029132.
FT   CHAIN       196    793       Disintegrin and metalloproteinase domain-
FT                                containing protein 28.
FT                                /FTId=PRO_0000029133.
FT   TOPO_DOM    196    668       Extracellular. {ECO:0000255}.
FT   TRANSMEM    669    689       Helical. {ECO:0000255}.
FT   TOPO_DOM    690    793       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      206    402       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      410    496       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      628    660       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       169    176       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    497    631       Cys-rich.
FT   COMPBIAS    760    765       Poly-Pro.
FT   ACT_SITE    343    343       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       171    171       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       342    342       Zinc; catalytic. {ECO:0000250}.
FT   METAL       346    346       Zinc; catalytic. {ECO:0000250}.
FT   METAL       352    352       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD     91     91       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    272    272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    277    277       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    531    531       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    551    551       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    605    605       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    631    631       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    317    397       {ECO:0000250}.
FT   DISULFID    357    381       {ECO:0000250}.
FT   DISULFID    359    364       {ECO:0000250}.
FT   DISULFID    468    488       {ECO:0000250}.
FT   DISULFID    632    642       {ECO:0000250}.
FT   DISULFID    636    648       {ECO:0000250}.
FT   DISULFID    650    659       {ECO:0000250}.
FT   VAR_SEQ     769    793       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11867223}.
FT                                /FTId=VSP_005488.
FT   VAR_SEQ     769    771       TGR -> DPN (in isoform 3).
FT                                {ECO:0000303|PubMed:10794709,
FT                                ECO:0000303|PubMed:11867223,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_005489.
FT   VAR_SEQ     775    793       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10794709,
FT                                ECO:0000303|PubMed:11867223,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_005490.
FT   MUTAGEN     343    343       E->A: Abolishes prodomain removal.
FT                                {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
//
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