(data stored in ACNUC30567 zone)

HOGENOM: MOUSE14_PE1374

ID   MOUSE14_PE1374                       STANDARD;      PRT;   793 AA.
AC   MOUSE14_PE1374; Q9JLN6; Q5D070; Q8K5D2; Q8K5D3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein
DE   28; Short=ADAM 28; EC=3.4.24 -;AltName: Full=Thymic epithelial cell-ADAM;
DE   Short=TECADAM;Flags: Precursor; (MOUSE14.PE1374).
GN   Name=Adam28;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE14.PE1374.
CC       Mus musculus chromosome 14 NCBIM37  sequence 1..125194864 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ADA28_MOUSE
CC   -!- FUNCTION: May play a role in organogenesis and organ-specific
CC       functions such as thymic T-cell development.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
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   -!- 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.
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -!- GENE_FAMILY: HOG000230883 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000014725;ENSMUST00000022642;ENSMUSP00000022642.
DR   EMBL; AF153350; - ;
DR   EMBL; AF163290; - ;
DR   EMBL; AF163291; - ;
DR   EMBL; AF163292; - ;
DR   EMBL; AF163293; - ;
DR   EMBL; BC058782; - ;
DR   EMBL; U06146; - ;
DR   UniProtKB/Swiss-Prot; Q9JLN6; Q5D070; Q8K5D2; Q8K5D3; -.
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   IPI; IPI00224974; -.
DR   IPI; IPI00310406; -.
DR   IPI; IPI00402789; -.
DR   RefSeq; NP_001041640.1; NM_001048175.1.
DR   RefSeq; NP_034212.1; NM_010082.2.
DR   RefSeq; NP_899222.1; NM_183366.2.
DR   UniGene; Mm.117450; -.
DR   UniGene; Mm.461069; -.
DR   ProteinModelPortal; Q9JLN6; -.
DR   SMR; Q9JLN6; 201-665.
DR   STRING; Q9JLN6; -.
DR   MEROPS; M12.020; -.
DR   PRIDE; Q9JLN6; -.
DR   Ensembl; ENSMUST00000022642; ENSMUSP00000022642; ENSMUSG00000014725.
DR   Ensembl; ENSMUST00000111072; ENSMUSP00000106701; ENSMUSG00000014725.
DR   GeneID; 13522; -.
DR   KEGG; mmu:13522; -.
DR   UCSC; uc007ult.1; mouse.
DR   UCSC; uc007ulv.1; mouse.
DR   UCSC; uc007ulw.1; mouse.
DR   CTD; 10863; -.
DR   MGI; MGI:105988; Adam28.
DR   GeneTree; ENSGT00590000082827; -.
DR   InParanoid; Q9JLN6; -.
DR   OMA; PTLQEQC; -.
DR   OrthoDB; EOG4PC9RW; -.
DR   PhylomeDB; Q9JLN6; -.
DR   NextBio; 284092; -.
DR   PMAP-CutDB; Q9JLN6; -.
DR   ArrayExpress; Q9JLN6; -.
DR   Bgee; Q9JLN6; -.
DR   CleanEx; MM_ADAM28; -.
DR   Genevestigator; Q9JLN6; -.
DR   GermOnline; ENSMUSG00000014725; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Gene3D; G3DSA:3.40.390.10; G3DSA:3.40.390.10; 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   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; FALSE_NEG.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   HOGENOMDNA; MOUSE14.PE1374; -.
KW   ENSMUSG000000147255old_1320000031; ENSMUSP000000226421old_1320000031;
KW   Q60619_MOUSE; Q71U12_MOUSE; AF153350; AF163290; AF163291; AF163292;
KW   BC058782; U06146;
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.
SQ   SEQUENCE   793 AA;  UNKNOWN MW;  UNKNOWN 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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