MMP1_PIG
ID MMP1_PIG Reviewed; 469 AA.
AC P21692;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Interstitial collagenase;
DE EC=3.4.24.7;
DE AltName: Full=Matrix metalloproteinase-1;
DE Short=MMP-1;
DE Contains:
DE RecName: Full=18 kDa interstitial collagenase;
DE Flags: Precursor;
GN Name=MMP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1651440; DOI=10.1016/s0934-8832(11)80154-x;
RA Richards C.D., Rafferty J.A., Reynolds J.J., Saklatvala J.;
RT "Porcine collagenase from synovial fibroblasts: cDNA sequence and
RT modulation of expression of RNA in vitro by various cytokines.";
RL Matrix 11:161-167(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-469.
RC TISSUE=Synovial cell;
RX PubMed=2174547; DOI=10.1093/nar/18.22.6703;
RA Clarke N.J., O'Hare M.C., Cawston T.E., Harper G.P.;
RT "Nucleotide sequence of a cDNA for porcine type I collagenase, obtained by
RT PCR.";
RL Nucleic Acids Res. 18:6703-6703(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-469.
RX PubMed=8590015; DOI=10.1016/s0969-2126(01)00188-5;
RA Li J., Brick P., O'Hare M.C., Skarzynski T., Lloyd L.F., Curry V.A.,
RA Clark I.M., Bigg H.F., Hazleman B.L., Cawston T.E., Blow D.M.;
RT "Structure of full-length porcine synovial collagenase reveals a C-terminal
RT domain containing a calcium-linked, four-bladed beta-propeller.";
RL Structure 3:541-549(1995).
RN [4]
RP PROTEIN SEQUENCE OF 100-104 AND 248-282, AND AUTOCATALYTIC CLEAVAGE SITE.
RX PubMed=7840605; DOI=10.1006/abbi.1995.1018;
RA Clark I.M., Mitchell R.E., Powell L.K., Bigg H.F., Cawston T.E.,
RA O'Hare M.C.;
RT "Recombinant porcine collagenase: purification and autolysis.";
RL Arch. Biochem. Biophys. 316:123-127(1995).
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;
CC Note=Binds 4 Ca(2+) ions per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
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: Undergoes autolytic cleavage to produce a N-terminal fragment
CC having reduced collagenolytic activity.
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; X54724; CAA38526.1; -; mRNA.
DR PIR; S15986; KCPGI.
DR RefSeq; NP_001159701.1; NM_001166229.1.
DR PDB; 1FBL; X-ray; 2.50 A; A=100-469.
DR PDBsum; 1FBL; -.
DR AlphaFoldDB; P21692; -.
DR SMR; P21692; -.
DR STRING; 9823.ENSSSCP00000015909; -.
DR MEROPS; M10.001; -.
DR PaxDb; P21692; -.
DR PeptideAtlas; P21692; -.
DR PRIDE; P21692; -.
DR Ensembl; ENSSSCT00000038101; ENSSSCP00000042817; ENSSSCG00000014985.
DR Ensembl; ENSSSCT00015072195; ENSSSCP00015028953; ENSSSCG00015053476.
DR Ensembl; ENSSSCT00025053433; ENSSSCP00025022756; ENSSSCG00025039149.
DR Ensembl; ENSSSCT00035102258; ENSSSCP00035043598; ENSSSCG00035075081.
DR Ensembl; ENSSSCT00040074376; ENSSSCP00040031905; ENSSSCG00040054640.
DR Ensembl; ENSSSCT00045061166; ENSSSCP00045042961; ENSSSCG00045035329.
DR Ensembl; ENSSSCT00050062039; ENSSSCP00050026652; ENSSSCG00050045565.
DR Ensembl; ENSSSCT00055015909; ENSSSCP00055012507; ENSSSCG00055008073.
DR Ensembl; ENSSSCT00065007693; ENSSSCP00065003271; ENSSSCG00065005685.
DR Ensembl; ENSSSCT00070021418; ENSSSCP00070017709; ENSSSCG00070010991.
DR GeneID; 397320; -.
DR KEGG; ssc:397320; -.
DR CTD; 4312; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000159759; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; P21692; -.
DR OrthoDB; 1075463at2759; -.
DR TreeFam; TF315428; -.
DR Reactome; R-SSC-1442490; Collagen degradation.
DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
DR Reactome; R-SSC-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-SSC-210991; Basigin interactions.
DR EvolutionaryTrace; P21692; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000014985; Expressed in duodenum and 17 other tissues.
DR ExpressionAtlas; P21692; baseline and differential.
DR Genevisible; P21692; SS.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Calcium; Collagen degradation;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT PROPEP 20..99
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:7840605"
FT /id="PRO_0000028707"
FT CHAIN 100..469
FT /note="Interstitial collagenase"
FT /id="PRO_0000028708"
FT CHAIN 100..258
FT /note="18 kDa interstitial collagenase"
FT /id="PRO_0000028709"
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 ECO:0000269|PubMed:8590015"
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 BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT SITE 258..259
FT /note="Cleavage; by autolysis"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03956"
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 CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..466
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1FBL"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:1FBL"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:1FBL"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:1FBL"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:1FBL"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1FBL"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:1FBL"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:1FBL"
SQ SEQUENCE 469 AA; 53666 MW; 7952D72B2753F682 CRC64;
MFSLLLLLLL LCNTGSHGFP AATSETQEQD VEIVQKYLKN YYNLNSDGVP VEKKRNSGLV
VEKLKQMQQF FGLKVTGKPD AETLNVMKQP RCGVPDVAEF VLTPGNPRWE NTHLTYRIEN
YTPDLSREDV DRAIEKAFQL WSNVSPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
LAHAFQPGPG IGGDAHFDED ERWTKNFRDY NLYRVAAHEL GHSLGLSHST DIGALMYPNY
IYTGDVQLSQ DDIDGIQAIY GPSENPVQPS GPQTPQVCDS KLTFDAITTL RGELMFFKDR
FYMRTNSFYP EVELNFISVF WPQVPNGLQA AYEIADRDEV RFFKGNKYWA VRGQDVLYGY
PKDIHRSFGF PSTVKNIDAA VFEEDTGKTY FFVAHECWRY DEYKQSMDTG YPKMIAEEFP
GIGNKVDAVF QKDGFLYFFH GTRQYQFDFK TKRILTLQKA NSWFNCRKN
