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Stromelysin-2 (SL-2) (EC 3.4.24.22) (Matrix metalloproteinase-10) (MMP-10) (Transin-2)

 MMP10_HUMAN             Reviewed;         476 AA.
P09238; B2R9X9; Q53HH9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
28-FEB-2018, entry version 185.
RecName: Full=Stromelysin-2;
Short=SL-2;
EC=3.4.24.22;
AltName: Full=Matrix metalloproteinase-10;
Short=MMP-10;
AltName: Full=Transin-2;
Flags: Precursor;
Name=MMP10; Synonyms=STMY2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2844164; DOI=10.1042/bj2530187;
Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J.,
Breathnach R.;
"The collagenase gene family in humans consists of at least four
members.";
Biochem. J. 253:187-192(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-53.
TISSUE=Coronary artery;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-4; LYS-53; ARG-65;
LEU-226; GLU-282; PHE-440 AND LEU-475.
NIEHS SNPs program;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 99-263, CATALYTIC ACTIVITY,
ACTIVE SITE, COFACTOR, CALCIUM-BINDING, AND ZINC-BINDING SITES.
PubMed=15095982; DOI=10.1016/j.jmb.2003.12.033;
Bertini I., Calderone V., Fragai M., Luchinat C., Mangani S.,
Terni B.;
"Crystal structure of the catalytic domain of human matrix
metalloproteinase 10.";
J. Mol. Biol. 336:707-716(2004).
[9]
VARIANT [LARGE SCALE ANALYSIS] GLN-142.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV,
and V; weakly collagens III, IV, and V. Activates procollagenase.
-!- CATALYTIC ACTIVITY: Similar to stromelysin 1, but action on
collagen types III, IV and V is weak.
{ECO:0000269|PubMed:15095982}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:15095982};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:15095982};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15095982};
-!- 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}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp10/";
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EMBL; X07820; CAA30679.1; -; mRNA.
EMBL; BT007442; AAP36110.1; -; mRNA.
EMBL; AK222601; BAD96321.1; -; mRNA.
EMBL; AK313960; BAG36676.1; -; mRNA.
EMBL; AY744675; AAU21039.1; -; Genomic_DNA.
EMBL; CH471065; EAW67029.1; -; Genomic_DNA.
EMBL; BC002591; AAH02591.1; -; mRNA.
CCDS; CCDS8321.1; -.
PIR; A28816; KCHUS2.
RefSeq; NP_002416.1; NM_002425.2.
UniGene; Hs.2258; -.
PDB; 1Q3A; X-ray; 2.10 A; A/B/C=99-263.
PDB; 3V96; X-ray; 1.90 A; B=99-263.
PDB; 4ILW; X-ray; 2.10 A; D/F=99-263.
PDBsum; 1Q3A; -.
PDBsum; 3V96; -.
PDBsum; 4ILW; -.
ProteinModelPortal; P09238; -.
SMR; P09238; -.
BioGrid; 110462; 15.
STRING; 9606.ENSP00000279441; -.
BindingDB; P09238; -.
ChEMBL; CHEMBL4270; -.
DrugBank; DB00786; Marimastat.
DrugBank; DB08271; N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID.
GuidetoPHARMACOLOGY; 1634; -.
MEROPS; M10.006; -.
iPTMnet; P09238; -.
PhosphoSitePlus; P09238; -.
BioMuta; MMP10; -.
DMDM; 116869; -.
PaxDb; P09238; -.
PeptideAtlas; P09238; -.
PRIDE; P09238; -.
TopDownProteomics; P09238; -.
DNASU; 4319; -.
Ensembl; ENST00000279441; ENSP00000279441; ENSG00000166670.
GeneID; 4319; -.
KEGG; hsa:4319; -.
UCSC; uc001phg.3; human.
CTD; 4319; -.
DisGeNET; 4319; -.
EuPathDB; HostDB:ENSG00000166670.9; -.
GeneCards; MMP10; -.
HGNC; HGNC:7156; MMP10.
HPA; CAB002159; -.
MIM; 185260; gene.
neXtProt; NX_P09238; -.
OpenTargets; ENSG00000166670; -.
PharmGKB; PA30868; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P09238; -.
KO; K01396; -.
OMA; MEQGFPR; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P09238; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.22; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
SIGNOR; P09238; -.
EvolutionaryTrace; P09238; -.
GeneWiki; MMP10; -.
GenomeRNAi; 4319; -.
PRO; PR:P09238; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166670; -.
CleanEx; HS_MMP10; -.
ExpressionAtlas; P09238; baseline and differential.
Genevisible; P09238; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
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; 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; Calcium; Collagen degradation; Complete proteome;
Disulfide bond; Extracellular matrix; Hydrolase; Metal-binding;
Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000305}.
PROPEP 18 98 Activation peptide.
/FTId=PRO_0000028764.
CHAIN 99 476 Stromelysin-2.
/FTId=PRO_0000028765.
REPEAT 286 335 Hemopexin 1.
REPEAT 336 382 Hemopexin 2.
REPEAT 384 432 Hemopexin 3.
REPEAT 433 476 Hemopexin 4.
MOTIF 89 96 Cysteine switch. {ECO:0000250}.
ACT_SITE 218 218 {ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:15095982}.
METAL 91 91 Zinc; in inhibited form. {ECO:0000250}.
METAL 167 167 Zinc 1.
METAL 169 169 Zinc 1.
METAL 182 182 Zinc 1.
METAL 195 195 Zinc 1.
METAL 217 217 Zinc 2; catalytic.
METAL 221 221 Zinc 2; catalytic.
METAL 227 227 Zinc 2; catalytic.
DISULFID 289 476 {ECO:0000250}.
VARIANT 4 4 L -> V (in dbSNP:rs17435959).
{ECO:0000269|Ref.5}.
/FTId=VAR_020949.
VARIANT 53 53 R -> K (in dbSNP:rs486055).
{ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_020950.
VARIANT 65 65 G -> R (in dbSNP:rs17293607).
{ECO:0000269|Ref.5}.
/FTId=VAR_020951.
VARIANT 142 142 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036139.
VARIANT 226 226 F -> L (in dbSNP:rs17860971).
{ECO:0000269|Ref.5}.
/FTId=VAR_020952.
VARIANT 282 282 G -> E (in dbSNP:rs17860973).
{ECO:0000269|Ref.5}.
/FTId=VAR_020953.
VARIANT 440 440 L -> F (in dbSNP:rs17860996).
{ECO:0000269|Ref.5}.
/FTId=VAR_020954.
VARIANT 475 475 H -> L (in dbSNP:rs17861009).
{ECO:0000269|Ref.5}.
/FTId=VAR_020955.
STRAND 111 117 {ECO:0000244|PDB:3V96}.
HELIX 126 141 {ECO:0000244|PDB:3V96}.
STRAND 147 150 {ECO:0000244|PDB:3V96}.
STRAND 152 154 {ECO:0000244|PDB:3V96}.
STRAND 157 163 {ECO:0000244|PDB:3V96}.
STRAND 168 171 {ECO:0000244|PDB:3V96}.
STRAND 175 183 {ECO:0000244|PDB:3V96}.
STRAND 186 188 {ECO:0000244|PDB:3V96}.
TURN 189 192 {ECO:0000244|PDB:3V96}.
STRAND 194 197 {ECO:0000244|PDB:3V96}.
STRAND 202 210 {ECO:0000244|PDB:3V96}.
HELIX 211 223 {ECO:0000244|PDB:3V96}.
STRAND 231 233 {ECO:0000244|PDB:1Q3A}.
STRAND 237 239 {ECO:0000244|PDB:3V96}.
HELIX 242 247 {ECO:0000244|PDB:3V96}.
HELIX 252 262 {ECO:0000244|PDB:3V96}.
SEQUENCE 476 AA; 54151 MW; 516DCDDFEF92A0D6 CRC64;
MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ FRRKDSNLIV
KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS SFPGMPKWRK THLTYRIVNY
TPDLPRDAVD SAIEKALKVW EEVTPLTFSR LYEGEADIMI SFAVKEHGDF YSFDGPGHSL
AHAYPPGPGL YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN
SFTELAQFRL SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST
LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT VFIFKGNEFW
AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY FFAADKYWRF DENSQSMEQG
FPRLIADDFP GVEPKVDAVL QAFGFFYFFS GSSQFEFDPN ARMVTHILKS NSWLHC


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