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Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Thymic epithelial cell-ADAM) (TECADAM)

 ADA28_MOUSE             Reviewed;         793 AA.
Q9JLN6; Q5D070; Q8K5D2; Q8K5D3;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
12-FEB-2003, sequence version 3.
05-DEC-2018, entry version 148.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28;
Short=ADAM 28;
EC=3.4.24.-;
AltName: Full=Thymic epithelial cell-ADAM;
Short=TECADAM;
Flags: Precursor;
Name=Adam28;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION, AND
MUTAGENESIS OF GLU-343.
TISSUE=Lung;
PubMed=10794709; DOI=10.1042/bj3480021;
Howard L., Maciewicz R.A., Blobel C.P.;
"Cloning and characterization of ADAM28: evidence for autocatalytic
pro-domain removal and for cell surface localization of mature
ADAM28.";
Biochem. J. 348:21-27(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
SPECIFICITY.
TISSUE=Thymus;
PubMed=11867223; DOI=10.1016/S0378-1119(01)00871-X;
Haidl I.D., Huber G., Eichmann K.;
"An ADAM family member with expression in thymic epithelial cells and
related tissues.";
Gene 283:163-170(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: May play a role in organogenesis and organ-specific
functions such as thymic T-cell development.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9JLN6-1; Sequence=Displayed;
Name=2;
IsoId=Q9JLN6-2; Sequence=VSP_005488;
Name=3;
IsoId=Q9JLN6-3; Sequence=VSP_005489, VSP_005490;
-!- TISSUE SPECIFICITY: Strong expression in thymic epithelial cells
and developmentally related tissues including the trachea,
thyroid, lung and stomach, but not in lymphocytes. Expressed at
high levels also in epididymis. In contrast with human is not
expressed in immature or mature lymphocyte populations of
thymocytes, lymph node, spleen, and bone marrow.
{ECO:0000269|PubMed:11867223}.
-!- DEVELOPMENTAL STAGE: The expression patterns in adult and day 15.5
embryos are similar.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Pro-domain removal and maturation may be, at least in part,
autocatalytic.
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EMBL; AF153350; AAF71993.1; -; mRNA.
EMBL; AF163290; AAM21935.1; -; mRNA.
EMBL; AF163291; AAM21936.1; -; mRNA.
EMBL; AF163292; AAM21937.1; -; mRNA.
EMBL; BC058782; AAH58782.1; -; mRNA.
CCDS; CCDS36964.1; -. [Q9JLN6-3]
CCDS; CCDS36965.1; -. [Q9JLN6-1]
RefSeq; NP_001041640.1; NM_001048175.2. [Q9JLN6-3]
RefSeq; NP_034212.1; NM_010082.2. [Q9JLN6-1]
RefSeq; NP_899222.1; NM_183366.3. [Q9JLN6-2]
UniGene; Mm.117450; -.
ProteinModelPortal; Q9JLN6; -.
SMR; Q9JLN6; -.
STRING; 10090.ENSMUSP00000022642; -.
MEROPS; M12.020; -.
iPTMnet; Q9JLN6; -.
PhosphoSitePlus; Q9JLN6; -.
PaxDb; Q9JLN6; -.
PRIDE; Q9JLN6; -.
Ensembl; ENSMUST00000022642; ENSMUSP00000022642; ENSMUSG00000014725. [Q9JLN6-1]
Ensembl; ENSMUST00000111072; ENSMUSP00000106701; ENSMUSG00000014725. [Q9JLN6-3]
Ensembl; ENSMUST00000224039; ENSMUSP00000153354; ENSMUSG00000014725. [Q9JLN6-2]
GeneID; 13522; -.
KEGG; mmu:13522; -.
UCSC; uc007ult.2; mouse. [Q9JLN6-3]
UCSC; uc007ulv.1; mouse. [Q9JLN6-1]
CTD; 10863; -.
MGI; MGI:105988; Adam28.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00940000156716; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9JLN6; -.
KO; K08614; -.
OMA; YYQGHII; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q9JLN6; -.
TreeFam; TF314733; -.
PMAP-CutDB; Q9JLN6; -.
PRO; PR:Q9JLN6; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000014725; Expressed in 118 organ(s), highest expression level in skeletal muscle tissue.
CleanEx; MM_ADAM28; -.
Genevisible; Q9JLN6; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 195 {ECO:0000250}.
/FTId=PRO_0000029132.
CHAIN 196 793 Disintegrin and metalloproteinase domain-
containing protein 28.
/FTId=PRO_0000029133.
TOPO_DOM 196 668 Extracellular. {ECO:0000255}.
TRANSMEM 669 689 Helical. {ECO:0000255}.
TOPO_DOM 690 793 Cytoplasmic. {ECO:0000255}.
DOMAIN 206 402 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 410 496 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 628 660 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 169 176 Cysteine switch. {ECO:0000250}.
COMPBIAS 497 631 Cys-rich.
COMPBIAS 760 765 Poly-Pro.
ACT_SITE 343 343 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 171 171 Zinc; in inhibited form. {ECO:0000250}.
METAL 342 342 Zinc; catalytic. {ECO:0000250}.
METAL 346 346 Zinc; catalytic. {ECO:0000250}.
METAL 352 352 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 631 631 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 317 397 {ECO:0000250}.
DISULFID 357 381 {ECO:0000250}.
DISULFID 359 364 {ECO:0000250}.
DISULFID 468 488 {ECO:0000250}.
DISULFID 632 642 {ECO:0000250}.
DISULFID 636 648 {ECO:0000250}.
DISULFID 650 659 {ECO:0000250}.
VAR_SEQ 769 793 Missing (in isoform 2).
{ECO:0000303|PubMed:11867223}.
/FTId=VSP_005488.
VAR_SEQ 769 771 TGR -> DPN (in isoform 3).
{ECO:0000303|PubMed:10794709,
ECO:0000303|PubMed:11867223,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005489.
VAR_SEQ 775 793 Missing (in isoform 3).
{ECO:0000303|PubMed:10794709,
ECO:0000303|PubMed:11867223,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005490.
MUTAGEN 343 343 E->A: Abolishes prodomain removal.
{ECO:0000269|PubMed:10794709}.
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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