Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Interstitial collagenase (EC 3.4.24.7) (Matrix metalloproteinase-1) (MMP-1) [Cleaved into: 18 kDa interstitial collagenase]

 MMP1_PIG                Reviewed;         469 AA.
P21692;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
05-DEC-2018, entry version 164.
RecName: Full=Interstitial collagenase;
EC=3.4.24.7;
AltName: Full=Matrix metalloproteinase-1;
Short=MMP-1;
Contains:
RecName: Full=18 kDa interstitial collagenase;
Flags: Precursor;
Name=MMP1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1651440;
Richards C.D., Rafferty J.A., Reynolds J.J., Saklatvala J.;
"Porcine collagenase from synovial fibroblasts: cDNA sequence and
modulation of expression of RNA in vitro by various cytokines.";
Matrix 11:161-167(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-469.
TISSUE=Synovial cell;
PubMed=2174547; DOI=10.1093/nar/18.22.6703;
Clarke N.J., O'Hare M.C., Cawston T.E., Harper G.P.;
"Nucleotide sequence of a cDNA for porcine type I collagenase,
obtained by PCR.";
Nucleic Acids Res. 18:6703-6703(1990).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-469.
PubMed=8590015; DOI=10.1016/S0969-2126(01)00188-5;
Li J., Brick P., O'Hare M.C., Skarzynski T., Lloyd L.F., Curry V.A.,
Clark I.M., Bigg H.F., Hazleman B.L., Cawston T.E., Blow D.M.;
"Structure of full-length porcine synovial collagenase reveals a C-
terminal domain containing a calcium-linked, four-bladed beta-
propeller.";
Structure 3:541-549(1995).
[4]
PROTEIN SEQUENCE OF 100-104 AND 248-282, AND AUTOCATALYTIC CLEAVAGE
SITE.
PubMed=7840605; DOI=10.1006/abbi.1995.1018;
Clark I.M., Mitchell R.E., Powell L.K., Bigg H.F., Cawston T.E.,
O'Hare M.C.;
"Recombinant porcine collagenase: purification and autolysis.";
Arch. Biochem. Biophys. 316:123-127(1995).
-!- FUNCTION: Cleaves collagens of types I, II, and III at one site in
the helical domain. Also cleaves collagens of types VII and X.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of the triple helix of collagen at about three-
quarters of the length of the molecule from the N-terminus, at
775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic
substrates and alpha-macroglobulins at bonds where P1' is a
hydrophobic residue.; EC=3.4.24.7;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 4 Ca(2+) ions per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- ACTIVITY REGULATION: Can be activated without removal of the
activation peptide.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Undergoes autolytic cleavage to produce a N-terminal fragment
having reduced collagenolytic activity.
-!- PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK.
{ECO:0000250|UniProtKB:P03956}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X54724; CAA38526.1; -; mRNA.
PIR; S15986; KCPGI.
RefSeq; NP_001159701.1; NM_001166229.1.
UniGene; Ssc.16013; -.
PDB; 1FBL; X-ray; 2.50 A; A=100-469.
PDBsum; 1FBL; -.
ProteinModelPortal; P21692; -.
SMR; P21692; -.
STRING; 9823.ENSSSCP00000015909; -.
MEROPS; M10.001; -.
PaxDb; P21692; -.
PeptideAtlas; P21692; -.
PRIDE; P21692; -.
Ensembl; ENSSSCT00000038101; ENSSSCP00000042817; ENSSSCG00000014985.
GeneID; 397320; -.
KEGG; ssc:397320; -.
CTD; 4312; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000159759; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P21692; -.
KO; K01388; -.
OMA; FHGTRQY; -.
OrthoDB; EOG091G03DP; -.
TreeFam; TF315428; -.
Reactome; R-SSC-1442490; Collagen degradation.
Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
Reactome; R-SSC-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-SSC-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-SSC-2179392; EGFR Transactivation by Gastrin.
EvolutionaryTrace; P21692; -.
PMAP-CutDB; P21692; -.
Proteomes; UP000008227; Chromosome 9.
Bgee; ENSSSCG00000014985; Expressed in 3 organ(s), highest expression level in lung.
ExpressionAtlas; P21692; baseline and differential.
Genevisible; P21692; SS.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 2.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Collagen degradation;
Complete proteome; Direct protein sequencing; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 19
PROPEP 20 99 Activation peptide.
{ECO:0000269|PubMed:7840605}.
/FTId=PRO_0000028707.
CHAIN 100 469 Interstitial collagenase.
/FTId=PRO_0000028708.
CHAIN 100 258 18 kDa interstitial collagenase.
/FTId=PRO_0000028709.
REPEAT 275 324 Hemopexin 1.
REPEAT 325 371 Hemopexin 2.
REPEAT 374 422 Hemopexin 3.
REPEAT 423 466 Hemopexin 4.
MOTIF 90 97 Cysteine switch. {ECO:0000250}.
ACT_SITE 219 219 {ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:8590015}.
METAL 92 92 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 124 124 Calcium 1.
METAL 158 158 Calcium 2.
METAL 168 168 Zinc 1.
METAL 170 170 Zinc 1.
METAL 175 175 Calcium 3.
METAL 176 176 Calcium 3; via carbonyl oxygen.
METAL 178 178 Calcium 3; via carbonyl oxygen.
METAL 180 180 Calcium 3; via carbonyl oxygen.
METAL 183 183 Zinc 1.
METAL 190 190 Calcium 2; via carbonyl oxygen.
METAL 192 192 Calcium 2; via carbonyl oxygen.
METAL 194 194 Calcium 2.
METAL 196 196 Zinc 1.
METAL 198 198 Calcium 3.
METAL 199 199 Calcium 1.
METAL 201 201 Calcium 3.
METAL 218 218 Zinc 2; catalytic.
METAL 222 222 Zinc 2; catalytic.
METAL 228 228 Zinc 2; catalytic.
METAL 285 285 Calcium 4; via carbonyl oxygen.
METAL 329 329 Calcium 4; via carbonyl oxygen.
METAL 378 378 Calcium 4; via carbonyl oxygen.
METAL 427 427 Calcium 4; via carbonyl oxygen.
SITE 258 259 Cleavage; by autolysis.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P03956}.
MOD_RES 274 274 Phosphothreonine.
{ECO:0000250|UniProtKB:P03956}.
MOD_RES 360 360 Phosphotyrosine; by PKDCC.
{ECO:0000250|UniProtKB:P03956}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 278 466
STRAND 110 118 {ECO:0000244|PDB:1FBL}.
HELIX 127 142 {ECO:0000244|PDB:1FBL}.
STRAND 148 155 {ECO:0000244|PDB:1FBL}.
STRAND 158 164 {ECO:0000244|PDB:1FBL}.
STRAND 169 171 {ECO:0000244|PDB:1FBL}.
STRAND 176 179 {ECO:0000244|PDB:1FBL}.
STRAND 182 184 {ECO:0000244|PDB:1FBL}.
TURN 190 193 {ECO:0000244|PDB:1FBL}.
STRAND 195 198 {ECO:0000244|PDB:1FBL}.
STRAND 204 209 {ECO:0000244|PDB:1FBL}.
HELIX 212 223 {ECO:0000244|PDB:1FBL}.
STRAND 237 239 {ECO:0000244|PDB:1FBL}.
HELIX 250 260 {ECO:0000244|PDB:1FBL}.
STRAND 264 267 {ECO:0000244|PDB:1FBL}.
STRAND 285 290 {ECO:0000244|PDB:1FBL}.
STRAND 293 298 {ECO:0000244|PDB:1FBL}.
STRAND 301 305 {ECO:0000244|PDB:1FBL}.
STRAND 313 316 {ECO:0000244|PDB:1FBL}.
HELIX 317 320 {ECO:0000244|PDB:1FBL}.
STRAND 329 334 {ECO:0000244|PDB:1FBL}.
TURN 335 338 {ECO:0000244|PDB:1FBL}.
STRAND 339 344 {ECO:0000244|PDB:1FBL}.
STRAND 347 352 {ECO:0000244|PDB:1FBL}.
HELIX 364 368 {ECO:0000244|PDB:1FBL}.
STRAND 379 383 {ECO:0000244|PDB:1FBL}.
TURN 384 387 {ECO:0000244|PDB:1FBL}.
STRAND 388 393 {ECO:0000244|PDB:1FBL}.
STRAND 396 401 {ECO:0000244|PDB:1FBL}.
TURN 402 404 {ECO:0000244|PDB:1FBL}.
HELIX 415 418 {ECO:0000244|PDB:1FBL}.
STRAND 427 432 {ECO:0000244|PDB:1FBL}.
STRAND 435 440 {ECO:0000244|PDB:1FBL}.
STRAND 443 448 {ECO:0000244|PDB:1FBL}.
TURN 449 452 {ECO:0000244|PDB:1FBL}.
STRAND 453 459 {ECO:0000244|PDB:1FBL}.
HELIX 462 464 {ECO:0000244|PDB:1FBL}.
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


Related products :

Catalog number Product name Quantity
U0097r CLIA Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
E0097r ELISA Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
E0097r ELISA kit Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
15-288-21115 Interstitial collagenase - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Polyclonal 0.05 mg
15-288-21115 Interstitial collagenase - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Polyclonal 0.1 mg
U0097b CLIA Bos taurus,Bovine,CLG,Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
E0097b ELISA kit Bos taurus,Bovine,CLG,Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
E0097b ELISA Bos taurus,Bovine,CLG,Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
E0097h ELISA kit CLG,Fibroblast collagenase,Homo sapiens,Human,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
E0097h ELISA CLG,Fibroblast collagenase,Homo sapiens,Human,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
U0097h CLIA CLG,Fibroblast collagenase,Homo sapiens,Human,Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1 96T
E0097p ELISA kit Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Pig,Sus scrofa 96T
U0097p CLIA Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Pig,Sus scrofa 96T
E0097p ELISA Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Pig,Sus scrofa 96T
E0097Rb ELISA Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Oryctolagus cuniculus,Rabbit 96T
U0097Rb CLIA Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Oryctolagus cuniculus,Rabbit 96T
EIAAB25010 Interstitial collagenase A,Matrix metalloproteinase-1a,McolA,Mcol-A,Mmp1a,MMP-1a,Mouse,Mus musculus
E0097Rb ELISA kit Interstitial collagenase,Matrix metalloproteinase-1,MMP1,MMP-1,Oryctolagus cuniculus,Rabbit 96T
EIAAB25011 Interstitial collagenase B,Matrix metalloproteinase-1b,McolB,Mcol-B,Mmp1b,MMP-1b,Mouse,Mus musculus
MMP11 MMP1 Gene matrix metallopeptidase 1 (interstitial collagenase)
E1381235 Matrix Metallopeptidase 1 (Interstitial Collagenase) (MMP1) ELISA Kit 1
201-20-3411 MMP1{matrix metallopeptidase 1 (interstitial collagenase)}rabbit.pAb 0.2ml
E1384125 Matrix Metallopeptidase 1 (Interstitial Collagenase) (MMP1) ELISA Kit
GWB-158D95 Anti- MMP1 (matrix metallopeptidase 1 (interstitial collagenase)) Antibody
GWB-DB0BC0 Anti- MMP1 (matrix metallopeptidase 1 (interstitial collagenase)) Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur