MMP1_RABIT
ID MMP1_RABIT Reviewed; 468 AA.
AC P13943;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Synovial cell;
RX PubMed=2825772; DOI=10.1021/bi00393a032;
RA Fini M.E., Plucinska I.M., Mayer A.S., Gross R.H., Brinckerhoff C.E.;
RT "A gene for rabbit synovial cell collagenase: member of a family of
RT metalloproteinases that degrade the connective tissue matrix.";
RL Biochemistry 26:6156-6165(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 449-468.
RC STRAIN=New Zealand white;
RX PubMed=3021384; DOI=10.1016/s0174-173x(86)80009-7;
RA Fini M.E., Austin S.D., Holt P.T., Ruby P.L., Gross R.H., White H.D.,
RA Brinckerhoff C.E.;
RT "Homology between exon-containing portions of rabbit genomic clones for
RT synovial cell collagenase and human foreskin and synovial cell mRNAs.";
RL Coll. Relat. Res. 6:239-248(1986).
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}.
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DR EMBL; M17823; AAB88016.1; -; Genomic_DNA.
DR EMBL; M17820; AAB88016.1; JOINED; Genomic_DNA.
DR EMBL; M17821; AAB88016.1; JOINED; Genomic_DNA.
DR EMBL; M17822; AAB88016.1; JOINED; Genomic_DNA.
DR EMBL; M19240; AAB88016.1; JOINED; mRNA.
DR EMBL; M25663; AAA31203.1; -; mRNA.
DR PIR; A27500; KCRBI.
DR RefSeq; NP_001164610.1; NM_001171139.2.
DR AlphaFoldDB; P13943; -.
DR SMR; P13943; -.
DR STRING; 9986.ENSOCUP00000015428; -.
DR MEROPS; M10.001; -.
DR PRIDE; P13943; -.
DR Ensembl; ENSOCUT00000017958; ENSOCUP00000015428; ENSOCUG00000017958.
DR GeneID; 100009110; -.
DR KEGG; ocu:100009110; -.
DR CTD; 4312; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000154907; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P13943; -.
DR OMA; FRNYNLY; -.
DR OrthoDB; 1075463at2759; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000017958; Expressed in zone of skin and 6 other tissues.
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 Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..98
FT /note="Activation peptide"
FT /id="PRO_0000028710"
FT CHAIN 99..468
FT /note="Interstitial collagenase"
FT /id="PRO_0000028711"
FT REPEAT 274..323
FT /note="Hemopexin 1"
FT REPEAT 324..370
FT /note="Hemopexin 2"
FT REPEAT 373..421
FT /note="Hemopexin 3"
FT REPEAT 422..465
FT /note="Hemopexin 4"
FT MOTIF 89..96
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 91
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 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT MOD_RES 359
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000250|UniProtKB:P03956"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..465
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 53740 MW; DA90538919952B8C CRC64;
MPGLPLLLLL LWGVGSHGFP AASETQEQDV EMVQKYLENY YNLKDDWRKI PKQRGNGLAV
EKLKQMQEFF GLKVTGKPDA ETLKMMKQPR CGVPDVAQFV LTPGNPRWEQ THLTYRIENY
TPDLSRADVD NAIEKAFQLW SNVTPLTFTK VSKGQADIMI SFVRGDHRDN SPFDGPEGQL
AHAFQPGLGI GGDVHFDEDD RWTKDFRNYN LYRVAAHELG HSLGLSHSTD IGALMYPNYM
FSGDVQLAQD DIDGIQAIYG PSQNPSQPVG PQTPKVCDSK LTFDAITTIR GEIMFFKDRF
YMRANPYYSE VELNFISVFW PHLPNGLQAA YEVAHRDEIL FFKGNKYWTV QGQNELPGYP
KDIHSSFGFP RSVNHIDAAV SEEDTGKTYF FVANKYWRYD EYKRSMDAGY PKMIEYDFPG
IGNKVDAVFK KDGFFYFFHG TRQYKFDPKT KRILTLQKAN SWFNCRKN
