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Interstitial collagenase A (EC 3.4.24.7) (Matrix metalloproteinase-1a) (MMP-1a) (Mcol-A)

 MMP1A_MOUSE             Reviewed;         464 AA.
Q9EPL5; Q149J4;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 127.
RecName: Full=Interstitial collagenase A;
EC=3.4.24.7;
AltName: Full=Matrix metalloproteinase-1a;
Short=MMP-1a;
AltName: Full=Mcol-A;
Flags: Precursor;
Name=Mmp1a; Synonyms=McolA;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11113146; DOI=10.1074/jbc.M009586200;
Balbin M., Fueyo A., Knauper V., Lopez J.M., Alvarez J., Sanchez L.M.,
Quesada V., Bordallo J., Murphy G., Lopez-Otin C.;
"Identification and enzymatic characterization of two diverging murine
counterparts of human interstitial collagenase (MMP-1) expressed at
sites of embryo implantation.";
J. Biol. Chem. 276:10253-10262(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129/SvJ;
Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
Nagaraja R.;
"Genomic sequence analysis in the mouse T-complex region.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Cleaves collagens of types I, II, and III at one site in
the helical domain. Also cleaves collagens of types VII and X (By
similarity). Able to degrade synthetic peptides and type I and II
fibrillar collagen. {ECO:0000250}.
-!- 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; 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};
-!- ACTIVITY REGULATION: Can be activated without removal of the
activation peptide. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- 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.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ278462; CAC18880.1; -; mRNA.
EMBL; AK049552; BAC33807.1; -; mRNA.
EMBL; AY211543; AAO37582.1; -; Genomic_DNA.
EMBL; BC117756; AAI17757.1; -; mRNA.
RefSeq; NP_114395.1; NM_032006.3.
UniGene; Mm.156952; -.
ProteinModelPortal; Q9EPL5; -.
SMR; Q9EPL5; -.
STRING; 10090.ENSMUSP00000034492; -.
MEROPS; M10.033; -.
PhosphoSitePlus; Q9EPL5; -.
PaxDb; Q9EPL5; -.
PRIDE; Q9EPL5; -.
GeneID; 83995; -.
KEGG; mmu:83995; -.
UCSC; uc009ocp.1; mouse.
CTD; 83995; -.
MGI; MGI:1933846; Mmp1a.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9EPL5; -.
KO; K01388; -.
PhylomeDB; Q9EPL5; -.
PRO; PR:Q9EPL5; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
GO; GO:0032461; P:positive regulation of protein oligomerization; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
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.
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; 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;
Autocatalytic cleavage; Calcium; Collagen degradation;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 96 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000042645.
CHAIN 97 464 Interstitial collagenase A.
/FTId=PRO_0000042646.
REPEAT 273 322 Hemopexin 1.
REPEAT 323 369 Hemopexin 2.
REPEAT 372 420 Hemopexin 3.
REPEAT 421 464 Hemopexin 4.
REGION 95 274 Metalloprotease.
MOTIF 87 94 Cysteine switch. {ECO:0000250}.
ACT_SITE 216 216 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 89 89 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 155 155 Calcium 2. {ECO:0000250}.
METAL 165 165 Zinc 1. {ECO:0000250}.
METAL 167 167 Zinc 1. {ECO:0000250}.
METAL 172 172 Calcium 3. {ECO:0000250}.
METAL 173 173 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 180 180 Zinc 1. {ECO:0000250}.
METAL 187 187 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 189 189 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 191 191 Calcium 2. {ECO:0000250}.
METAL 193 193 Zinc 1. {ECO:0000250}.
METAL 195 195 Calcium 3. {ECO:0000250}.
METAL 198 198 Calcium 3. {ECO:0000250}.
METAL 215 215 Zinc 2; catalytic. {ECO:0000250}.
METAL 219 219 Zinc 2; catalytic. {ECO:0000250}.
METAL 225 225 Zinc 2; catalytic. {ECO:0000250}.
METAL 283 283 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 376 376 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 425 425 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 276 464 {ECO:0000250}.
SEQUENCE 464 AA; 53488 MW; 09FFC0470E5F9948 CRC64;
MPSLPLLLLL WAASSYSFPV FHNGDRQNVE TVWKYLENYY NLGKNMQAKN VNGKEMMAEK
LRQMQQLFGL KVTGNSDPET LRAMKKPRCG VPDVAPYAIT HNNPRWTKTH LTYSILNYTP
YLPKAVVEDA IARAFRVWSD VTPLTFQRVF EEEGDIVLSF HRGDHGDNNP FDGPNYKLAH
TFQPGPGLGG DVHYDLDETW TNSSENFNLF YVTAHELGHS LGLTHSSDIG ALMFPSYTWY
TEDFVLNQDD INRIQDLYGP SPNPIQPTGA TTPHPCNGDL TFDAITTFRG EVFFFKGRFY
IRVNRFMPEP ELNLIGILWP NLPVKLDAAY EASMIDQVRY FKGSKVWAVQ EQSVLRGFPR
DIHSFFGFPS NVTHIDAAVC EEETGKTYFF VDHMYWRYDE NTQSMDPGYP RLTAEDFPGI
DDKVDDVFQK GENFYFFHQS VQHRFNLQIR RVDDSRDSST WFNC


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