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

Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)

 MMP13_HORSE             Reviewed;         472 AA.
O18927;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-FEB-2018, entry version 119.
RecName: Full=Collagenase 3;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase-13;
Short=MMP-13;
Flags: Precursor;
Name=MMP13;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Richardson D.W.;
"Dose dependent effects of corticosteroids on the expression of matrix
related genes in equine articular chondrocytes.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays a role in the degradation of extracellular matrix
proteins including fibrillar collagen, fibronectin, TNC and ACAN.
Cleaves triple helical collagens, including type I, type II and
type III collagen, but has the highest activity with soluble type
II collagen. Can also degrade collagen type IV, type XIV and type
X. May also function by activating or degrading key regulatory
proteins, such as TGFB1 and CTGF. Plays a role in wound healing,
tissue remodeling, cartilage degradation, bone development, bone
mineralization and ossification. Required for normal embryonic
bone development and ossification. Plays a role in the healing of
bone fractures via endochondral ossification. Plays a role in
wound healing, probably by a mechanism that involves proteolytic
activation of TGFB1 and degradation of CTGF. Plays a role in
keratinocyte migration during wound healing. May play a role in
cell migration and in tumor cell invasion (By similarity).
{ECO:0000250}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}. Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Seems to be specific to breast carcinomas.
-!- DOMAIN: The C-terminal region binds to collagen. {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 (By similarity).
{ECO:0000250}.
-!- PTM: The proenzyme is activated by removal of the propeptide; this
cleavage can be effected by other matrix metalloproteinases, such
as MMP2, MMP3 and MMP14 and may involve several cleavage steps.
Cleavage can also be autocatalytic, after partial maturation by
another protease or after treatment with 4-aminophenylmercuric
acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000250|UniProtKB:P45452}.
-!- 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-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF034087; AAB86893.1; -; mRNA.
RefSeq; NP_001075273.1; NM_001081804.1.
UniGene; Eca.13058; -.
ProteinModelPortal; O18927; -.
SMR; O18927; -.
STRING; 9796.ENSECAP00000005084; -.
MEROPS; M10.013; -.
PaxDb; O18927; -.
GeneID; 100009711; -.
KEGG; ecb:100009711; -.
CTD; 4322; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; O18927; -.
KO; K07994; -.
BRENDA; 3.4.24.B4; 2120.
Proteomes; UP000002281; Unplaced.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; ISS:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; ISS:UniProtKB.
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; IPR028711; Collagenase_3.
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.
PANTHER; PTHR10201:SF165; PTHR10201:SF165; 1.
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.
2: Evidence at transcript level;
Calcium; Collagen degradation; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 104 Activation peptide. {ECO:0000255}.
/FTId=PRO_0000028786.
CHAIN 105 472 Collagenase 3.
/FTId=PRO_0000028787.
REPEAT 282 331 Hemopexin 1.
REPEAT 332 378 Hemopexin 2.
REPEAT 380 428 Hemopexin 3.
REPEAT 429 472 Hemopexin 4.
REGION 177 247 Interaction with TIMP2. {ECO:0000250}.
REGION 269 472 Interaction with collagen. {ECO:0000250}.
MOTIF 95 102 Cysteine switch. {ECO:0000250}.
ACT_SITE 224 224 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 97 97 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 129 129 Calcium 1. {ECO:0000250}.
METAL 163 163 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 173 173 Zinc 1; via tele nitrogen. {ECO:0000250}.
METAL 175 175 Zinc 1. {ECO:0000250}.
METAL 180 180 Calcium 3. {ECO:0000250}.
METAL 181 181 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 183 183 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 185 185 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 188 188 Zinc 1; via tele nitrogen. {ECO:0000250}.
METAL 195 195 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 197 197 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 199 199 Calcium 2. {ECO:0000250}.
METAL 201 201 Zinc 1; via pros nitrogen. {ECO:0000250}.
METAL 203 203 Calcium 3. {ECO:0000250}.
METAL 204 204 Calcium 1. {ECO:0000250}.
METAL 206 206 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 206 206 Calcium 3. {ECO:0000250}.
METAL 223 223 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 227 227 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 233 233 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 241 241 Zinc 2; via carbonyl oxygen; catalytic.
{ECO:0000250}.
METAL 292 292 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 294 294 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 336 336 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 338 338 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 384 384 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 386 386 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 433 433 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 435 435 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
MOD_RES 367 367 Phosphotyrosine; by PKDCC.
{ECO:0000250|UniProtKB:P45452}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 285 472 {ECO:0000250}.
SEQUENCE 472 AA; 54226 MW; 92B2697583F016D1 CRC64;
MHPGVLAAFL FLSWTRCWSL PVPNDDDDDD DMSEEDFQLA ERYLKSYYYP LNPAGILKKT
AANSVVDRLR EMQSFFGLEV TGKLDDNTLD IMKKPRCGVP DVGEYNVFPR TLKWPKMNLT
YRIVNYTPDL THSEVEKAFK KAFKVWSDVT PLNFTRLYNG TADIMISFGT KEHGDFYPFD
GPSGLLAHAF PPGPNYGGDA HFDDDETWTS SSKGYNLFLV AAHEFGHSLG LDHSKDPGAL
MFPIYTYTGK SHFVLPDDDV QGIQYLYGPG DEDPNPKHPK TPDKCDPSLS LDAITSLRGE
TMVFKDRFFW RLHPQLVDAE LFLTKSFWPE LPNRIDAAYE HPSKDLIFIF RGRKFWALNG
YDILEGYPQK ISELGFPKDV KKISAAVHFE DTGKTLFFSG NQVWRYDDTN RMMDKDYPRL
IEEDFPGIGD KVDAVYEKNG YIYFFNGPIQ FEYSIWSNRI VRVMPTNSLL WC


Related products :

Catalog number Product name Quantity
E0097r ELISA kit 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
U0097r CLIA 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 0.1 mg
15-288-21115 Interstitial collagenase - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Polyclonal 0.05 mg
20-783-73156 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
U0103m CLIA Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
20-783-73157 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
E0103m ELISA Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
20-783-73158 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
E0103m ELISA kit Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
U0097b CLIA 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
E0097b ELISA kit 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
20-783-71861 RAT ANTI MOUSE CD147 RPE - NEUROTHELIN; Leukocyte activation antigen M6; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7; Tumor cell-derived collagenase st 100 TESTS
E0103h ELISA CLG1,Homo sapiens,Human,Matrix metalloproteinase-8,MMP8,MMP-8,Neutrophil collagenase,PMNL collagenase,PMNL-CL 96T
E0103h ELISA kit CLG1,Homo sapiens,Human,Matrix metalloproteinase-8,MMP8,MMP-8,Neutrophil collagenase,PMNL collagenase,PMNL-CL 96T
U0103h CLIA CLG1,Homo sapiens,Human,Matrix metalloproteinase-8,MMP8,MMP-8,Neutrophil collagenase,PMNL collagenase,PMNL-CL 96T
20-783-71858 RAT ANTI MOUSE CD147 FITC - NEUROTHELIN; Leukocyte activation antigen M6; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7; Tumor cell-derived collagenase s 0.1 mg
20-783-71103 MOUSE ANTI HUMAN CD147 RPE - NEUROTHELIN; Leukocyte activation antigen M6; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7; Tumor cell-derived collagenase 100 TESTS
20-783-72459 MOUSE ANTI RAT CD147 - NEUROTHELIN; Leukocyte activation antigen M6; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7; Tumor cell-derived collagenase stimul 2 ml
20-783-71856 RAT ANTI MOUSE CD147 - NEUROTHELIN; Leukocyte activation antigen M6; Collagenase stimulatory factor; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7; Tumor cell-derived collagenase stimul 0.25 mg


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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