(data stored in ACNUC3659 zone)

HOVERGEN: MCPT1_MOUSE

ID   MCPT1_MOUSE             Reviewed;         246 AA.
AC   P11034;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-NOV-2009, entry version 88.
DE   RecName: Full=Mast cell protease 1;
DE            EC=3.4.21.-;
DE   AltName: Full=MMCP-1;
DE   Flags: Precursor;
GN   Name=Mcpt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92388686; PubMed=1517575;
RA   Ghildyal N., McNeil H.P., Stechschulte S., Austen K.F.,
RA   Silberstein D., Gurish M.F., Somerville L.L., Stevens R.L.;
RT   "IL-10 induces transcription of the gene for mouse mast cell protease-
RT   1, a serine protease preferentially expressed in mucosal mast cells of
RT   Trichinella spiralis-infected mice.";
RL   J. Immunol. 149:2123-2129(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=91285010; PubMed=2060576; DOI=10.1002/eji.1830210706;
RA   Huang R., Blom T., Hellman L.;
RT   "Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three
RT   mouse mast cell-specific serine proteases.";
RL   Eur. J. Immunol. 21:1611-1621(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-246.
RX   MEDLINE=89207558; PubMed=2706264; DOI=10.1021/bi00427a054;
RA   le Trong H., Newlands G.F.J., Miller H.R.P., Charbonneau H.,
RA   Neurath H., Woodbury R.G.;
RT   "Amino acid sequence of a mouse mucosal mast cell protease.";
RL   Biochemistry 28:391-395(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-49.
RX   MEDLINE=93371351; PubMed=8363563;
RA   Newlands G.F.J., Knox D.P., Pirie-Shepherd S.R., Miller H.R.P.;
RT   "Biochemical and immunological characterization of multiple glycoforms
RT   of mouse mast cell protease 1: comparison with an isolated murine
RT   serosal mast cell protease (MMCP-4).";
RL   Biochem. J. 294:127-135(1993).
CC   -!- FUNCTION: Has a chymotrypsin-like activity.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule.
CC       Note=Secretory granules.
CC   -!- TISSUE SPECIFICITY: Mucosal mast cells.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; S44609; AAB23194.1; -; mRNA.
DR   EMBL; X68803; CAA48703.1; -; Genomic_DNA.
DR   IPI; IPI00111387; -.
DR   PIR; A46504; A46504.
DR   RefSeq; NP_032596.1; -.
DR   UniGene; Mm.201549; -.
DR   HSSP; P00770; 3RP2.
DR   STRING; P11034; -.
DR   MEROPS; S01.458; -.
DR   PRIDE; P11034; -.
DR   Ensembl; ENSMUST00000022836; ENSMUSP00000022836; ENSMUSG00000022227; Mus musculus.
DR   GeneID; 17224; -.
DR   KEGG; mmu:17224; -.
DR   UCSC; uc007ubi.1; mouse.
DR   CTD; 17224; -.
DR   MGI; MGI:96937; Mcpt1.
DR   HOGENOM; P11034; -.
DR   HOVERGEN; P11034; -.
DR   OMA; CKGREIT; -.
DR   NextBio; 291636; -.
DR   ArrayExpress; P11034; -.
DR   Bgee; P11034; -.
DR   CleanEx; MM_MCPT1; -.
DR   Genevestigator; P11034; -.
DR   GermOnline; ENSMUSG00000022227; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P11034.
DR   SWISS-2DPAGE; P11034.
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Zymogen.
FT   DOMAIN        1     65       PRODOM:2005.1:PD474467  1445
FT   DOMAIN       71    114       PRODOM:2005.1:PD331626  438
FT   DOMAIN      115    151       PRODOM:2005.1:PD701657  461
FT   DOMAIN      152    190       PRODOM:2005.1:PD887239  32
FT   DOMAIN      200    240       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     18
FT   PROPEP       19     20       Activation peptide.
FT                                /FTId=PRO_0000027449.
FT   CHAIN        21    246       Mast cell protease 1.
FT                                /FTId=PRO_0000027450.
FT   DOMAIN       21    244       Peptidase S1.
FT   ACT_SITE     65     65       Charge relay system (By similarity).
FT   ACT_SITE    109    109       Charge relay system (By similarity).
FT   ACT_SITE    202    202       Charge relay system (By similarity).
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Probable).
FT   DISULFID     50     66       By similarity.
FT   DISULFID    143    208       By similarity.
FT   DISULFID    174    187       By similarity.
SQ   SEQUENCE   246 AA;  27013 MW;  26E112E8C580154B CRC64;
     MQALLFLMAL LLPSGAGAEE IIGGVEARPH SRPYMAHLKI ITDRGSEDRC GGFLIAPQFV
     LTAAHCKGRE ITVTLGAHDV SKSESTQQRI KVEKQIIHKN YNVSFNLYDI MLLKLEEKAE
     LTPTVDVIPL PGPSDFIDPG KMCWTAGWGK TGEKEPTSET LREVELRIMD KEACKMYKHY
     DYNFQVCVGS STKLKTAYMG DSGGPLLCAG VAHGIVSYGD SHGKPPAVFT RISAYVPWIK
     TVINGK
//

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