位置:首页 > 蛋白库 > MMP1_HORSE
MMP1_HORSE
ID   MMP1_HORSE              Reviewed;         469 AA.
AC   Q9XSZ5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Interstitial collagenase;
DE            EC=3.4.24.7;
DE   AltName: Full=Matrix metalloproteinase-1;
DE            Short=MMP-1;
DE   Flags: Precursor;
GN   Name=MMP1;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Richardson D.W.;
RT   "Cloning and expression of equine matrix metalloproteinase 1 (interstitial
RT   collagenase).";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves collagens of types I, II, and III at one site in the
CC       helical domain. Also cleaves collagens of types VII and X.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of the triple helix of collagen at about three-
CC         quarters of the length of the molecule from the N-terminus, at 775-
CC         Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates
CC         and alpha-macroglobulins at bonds where P1' is a hydrophobic
CC         residue.; EC=3.4.24.7;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Can be activated without removal of the activation
CC       peptide.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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: Tyrosine phosphorylated in platelets by PKDCC/VLK.
CC       {ECO:0000250|UniProtKB:P03956}.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF148882; AAD38030.1; -; mRNA.
DR   RefSeq; NP_001075316.1; NM_001081847.2.
DR   AlphaFoldDB; Q9XSZ5; -.
DR   SMR; Q9XSZ5; -.
DR   MEROPS; M10.001; -.
DR   PaxDb; Q9XSZ5; -.
DR   PRIDE; Q9XSZ5; -.
DR   GeneID; 100033896; -.
DR   KEGG; ecb:100033896; -.
DR   CTD; 4312; -.
DR   InParanoid; Q9XSZ5; -.
DR   OrthoDB; 1075463at2759; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00094; HX; 1.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 2.110.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR000585; Hemopexin-like_dom.
DR   InterPro; IPR036375; Hemopexin-like_dom_sf.
DR   InterPro; IPR018487; Hemopexin-like_repeat.
DR   InterPro; IPR018486; Hemopexin_CS.
DR   InterPro; IPR033739; M10A_MMP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR021158; Pept_M10A_Zn_BS.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   Pfam; PF00045; Hemopexin; 4.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR   PRINTS; PR00138; MATRIXIN.
DR   SMART; SM00120; HX; 4.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF50923; SSF50923; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR   PROSITE; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Collagen degradation; Disulfide bond; Extracellular matrix;
KW   Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..99
FT                   /note="Activation peptide"
FT                   /id="PRO_0000028701"
FT   CHAIN           100..469
FT                   /note="Interstitial collagenase"
FT                   /id="PRO_0000028702"
FT   REPEAT          275..324
FT                   /note="Hemopexin 1"
FT   REPEAT          325..371
FT                   /note="Hemopexin 2"
FT   REPEAT          374..422
FT                   /note="Hemopexin 3"
FT   REPEAT          423..466
FT                   /note="Hemopexin 4"
FT   MOTIF           90..97
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         274
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P03956"
FT   MOD_RES         360
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000250|UniProtKB:P03956"
FT   DISULFID        278..466
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  54002 MW;  AEE6760AB2C529CA CRC64;
     MLSLPLLLLL LWGMGSHSFP TVPSETREED VEMVQKYLEN YYNLKSDGEQ IEKQRHRSPV
     VEKLKQMQEF FGLKVTGKPD AETLNVMKQP RCGVPDVAEF VLTEGNPRWE NTHLTYRIEN
     YTPDLPRADV DQAIEKAFQL WSNVSPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
     LAHAFQPGPR IGGDAHFDED ETWTSNFRNY NLYRVAAHEF GHSLGLSHST DIGALMYPNY
     FFTGDVQLSQ DDINGIQAIY GPSQNPIQPI GPQTPEVCDS KLTFDAITTI RGEVMFFKDR
     FYMRINPYYP EAELNFISIF WPQLPNGLQA AYEVSHRDEV RFFKGNKYWA VKGQDVLYGY
     PKDIHRSFGF PSTVKNIDAA VSEEDTGKTY FFVADKYWRY DEYKRSMDAG YPKMIADDFP
     GIGDKVDAVF QKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024