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

72 kDa type IV collagenase (EC 3.4.24.24) (72 kDa gelatinase) (Gelatinase A) (Matrix metalloproteinase-2) (MMP-2)

 MMP2_CHICK              Reviewed;         663 AA.
Q90611;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
28-FEB-2018, entry version 146.
RecName: Full=72 kDa type IV collagenase;
EC=3.4.24.24;
AltName: Full=72 kDa gelatinase;
AltName: Full=Gelatinase A;
AltName: Full=Matrix metalloproteinase-2;
Short=MMP-2;
Flags: Precursor;
Name=MMP2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=8010954; DOI=10.1042/bj3000729;
Aimes R.T., French D.L., Quigley J.P.;
"Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from
chicken embryo fibroblasts using gene family PCR: expression of the
gelatinase increases upon malignant transformation.";
Biochem. J. 300:729-736(1994).
[2]
PROTEIN SEQUENCE OF 27-41 AND 107-122.
PubMed=1848240;
Chen J.-M., Aimes R.T., Ward G.R., Youngleib G.L., Quigley J.P.;
"Isolation and characterization of a 70-kDa metalloprotease
(gelatinase) that is elevated in Rous sarcoma virus-transformed
chicken embryo fibroblasts.";
J. Biol. Chem. 266:5113-5121(1991).
-!- CATALYTIC ACTIVITY: Cleavage of gelatin type I and collagen types
IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-
Ile-Ala-Gly-Gln.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 4 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};
-!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- TISSUE SPECIFICITY: Produced by normal skin fibroblasts.
-!- 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: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-
MMP3). {ECO:0000250}.
-!- 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; U07775; AAA19596.1; -; mRNA.
PIR; S46492; S46492.
RefSeq; NP_989751.1; NM_204420.2.
UniGene; Gga.3199; -.
ProteinModelPortal; Q90611; -.
SMR; Q90611; -.
STRING; 9031.ENSGALP00000005656; -.
MEROPS; M10.003; -.
PaxDb; Q90611; -.
PRIDE; Q90611; -.
Ensembl; ENSGALT00000005666; ENSGALP00000005656; ENSGALG00000003580.
GeneID; 386583; -.
KEGG; gga:386583; -.
CTD; 4313; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00910000144034; -.
HOGENOM; HOG000217926; -.
HOVERGEN; HBG052484; -.
InParanoid; Q90611; -.
KO; K01398; -.
OMA; HESCTSA; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q90611; -.
TreeFam; TF315428; -.
Reactome; R-GGA-1442490; Collagen degradation.
Reactome; R-GGA-1474228; Degradation of the extracellular matrix.
Reactome; R-GGA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
PRO; PR:Q90611; -.
Proteomes; UP000000539; Chromosome 11.
Bgee; ENSGALG00000003580; -.
GO; GO:0005604; C:basement membrane; IDA:AgBase.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0031012; C:extracellular matrix; IDA:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:AgBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl.
GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:AgBase.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:1904932; P:negative regulation of cartilage condensation; IMP:AgBase.
GO; GO:0061037; P:negative regulation of cartilage development; IMP:AgBase.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:AgBase.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:AgBase.
GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0043408; P:regulation of MAPK cascade; IMP:AgBase.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
CDD; cd00062; FN2; 3.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.10.10.10; -; 3.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 2.
InterPro; IPR028708; 72kDa_collagenase.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR013806; Kringle-like.
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:SF29; PTHR10201:SF29; 4.
Pfam; PF00040; fn2; 3.
Pfam; PF00045; Hemopexin; 3.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00059; FN2; 3.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
SUPFAM; SSF57440; SSF57440; 3.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00023; FN2_1; 3.
PROSITE; PS51092; FN2_2; 3.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Calcium; Collagen degradation; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 26 {ECO:0000269|PubMed:1848240}.
PROPEP 27 106 Activation peptide.
{ECO:0000269|PubMed:1848240}.
/FTId=PRO_0000028722.
CHAIN 107 663 72 kDa type IV collagenase.
/FTId=PRO_0000028723.
DOMAIN 225 273 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 283 331 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 341 389 Fibronectin type-II 3.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 475 519 Hemopexin 1.
REPEAT 520 566 Hemopexin 2.
REPEAT 568 616 Hemopexin 3.
REPEAT 617 663 Hemopexin 4.
REGION 107 218 Collagenase-like 1.
REGION 219 393 Collagen-binding.
REGION 394 468 Collagenase-like 2.
MOTIF 97 104 Cysteine switch. {ECO:0000250}.
ACT_SITE 401 401 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 99 99 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 131 131 Calcium 1. {ECO:0000250}.
METAL 165 165 Calcium 2. {ECO:0000250}.
METAL 175 175 Zinc 1. {ECO:0000250}.
METAL 177 177 Zinc 1. {ECO:0000250}.
METAL 182 182 Calcium 3. {ECO:0000250}.
METAL 183 183 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 190 190 Zinc 1. {ECO:0000250}.
METAL 197 197 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 199 199 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 201 201 Calcium 2. {ECO:0000250}.
METAL 203 203 Zinc 1. {ECO:0000250}.
METAL 205 205 Calcium 3. {ECO:0000250}.
METAL 206 206 Calcium 1. {ECO:0000250}.
METAL 208 208 Calcium 3. {ECO:0000250}.
METAL 400 400 Zinc 2; catalytic. {ECO:0000250}.
METAL 404 404 Zinc 2; catalytic. {ECO:0000250}.
METAL 410 410 Zinc 2; catalytic. {ECO:0000250}.
METAL 479 479 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 524 524 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 572 572 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 621 621 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
DISULFID 230 256 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 244 271 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 288 314 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 302 329 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 346 372 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 360 387 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 472 663 {ECO:0000255|PROSITE-ProRule:PRU00479}.
CONFLICT 40 40 P -> Q (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 W -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 122 122 T -> I (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 663 AA; 74941 MW; 8D6FDA4E67C3EBCA CRC64;
MKTHSVFGFF FKVLLIQVYL FNKTLAAPSP IIKFPGDSTP KTDKELAVQY LNKYYGCPKD
NCNLFVLKDT LKKMQKFFGL PETGDLDQNT IETMKKPRCG NPDVANYNFF PRKPKWEKNH
ITYRIIGYTP DLDPETVDDA FARAFKVWSD VTPLRFNRIN DGEADIMINF GRWEHGDGYP
FDGKDGLLAH AFAPGPGIGG DSHFDDDELW TLGEGQVVRV KYGNADGEYC KFPFWFNGKE
YNSCTDAGRN DGFLWCSTTK DFDADGKYGF CPHESLFTMG GNGDGQPCKF PFKFQGQSYD
QCTTEGRTDG YRWCGTTEDY DRDKKYGFCP ETAMSTVGGN SEGAPCVFPF IFLGNKYDSC
TSAGRNDGKL WCASTSSYDD DRKWGFCPDQ GYSLFLVAAH EFGHAMGLEH SEDPGALMAP
IYTYTKNFRL SQDDIKGIQE LYEVSPDVEP GPGPGPGPGP RPTLGPVTPE LCKHDIVFDG
VAQIRGEIFF FKDRFMWRTV NPRGKPTGPL LVATFWPDLP EKIDAVYESP QDEKAVFFAG
NEYWVYTASN LDRGYPKKLT SLGLPPDVQR IDAAFNWGRN KKTYIFSGDR YWKYNEEKKK
MELATPKFIA DSWNGVPDNL DAVLGLTDSG YTYFFKDQYY LQMEDKSLKI VKIGKISSDW
LGC


Related products :

Catalog number Product name Quantity
18-003-42334 Matrix metalloproteinase-9 - EC 3.4.24.35; MMP-9; 92 kDa type IV collagenase; 92 kDa gelatinase; Gelatinase B; GELB Polyclonal 0.1 mg Protein A
15-288-21116 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.1 mg
15-288-21116 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.05 mg
18-003-42982 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.1 mg Protein A
U0100m CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
U0100r CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
E0100m ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
E0100r ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
E0100m ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
E0100r ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
U0553b CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
E0553r ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
E0553b ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
E0553b ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Bos taurus,Bovine,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
U0553r CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
E0100Rb ELISA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0553r ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Rat,Rattus norvegicus 96T
U0100Rb CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0100Rb ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,MMP2,MMP-2,Oryctolagus cuniculus,Rabbit 96T
E0100h ELISA 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
U0100h CLIA 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
E0100h ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,CLG4A,Gelatinase A,Homo sapiens,Human,Matrix metalloproteinase-2,MMP2,MMP-2,TBE-1 96T
U0553Rb CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9,Oryctolagus cuniculus,Rabbit 96T
E0553m ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Clg4b,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Mouse,Mus musculus 96T
U0553m CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Clg4b,Gelatinase B,GELB,Matrix metalloproteinase-9,Mmp9,MMP-9,Mouse,Mus musculus 96T


 

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