Stromelysin-2 precursor - Homo sapiens (Human)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Stromelysin-2
Short name=SL-2
EC=3.4.24.22

Alternative name(s):
Matrix metalloproteinase-10
Short name=MMP-10
Transin-2

Gene names

Name:	MMP10
Synonyms:	STMY2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	476 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.8
Cofactor	Binds 2 zinc ions per subunit. Ref.8 Calcium. Ref.8
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
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.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Traceable author statement. Source: ProtInc
Cellular component	extracellular space Traceable author statement. Source: ProtInc proteinaceous extracellular matrix Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Traceable author statement. Source: ProtInc zinc ion binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Probable

Propeptide

18 – 98

81

Activation peptide

PRO_0000028764

Chain

99 – 476

378

Stromelysin-2

PRO_0000028765

Regions

Domain

295 – 337

43

Hemopexin-like 1

Domain

339 – 382

44

Hemopexin-like 2

Domain

387 – 434

48

Hemopexin-like 3

Domain

436 – 476

41

Hemopexin-like 4

Motif

89 – 96

8

Cysteine switch By similarity

Sites

Active site

218

1

Ref.8

Metal binding

91

1

Zinc; in inhibited form By similarity

Metal binding

167

1

Zinc 1

Metal binding

169

1

Zinc 1

Metal binding

182

1

Zinc 1

Metal binding

195

1

Zinc 1

Metal binding

217

1

Zinc 2; catalytic

Metal binding

221

1

Zinc 2; catalytic

Metal binding

227

1

Zinc 2; catalytic

Amino acid modifications

Disulfide bond

289 ↔ 476

By similarity

Natural variations

Natural variant

4

1

L → V. Ref.5
Corresponds to variant rs17435959 [ dbSNP | Ensembl ].

VAR_020949

Natural variant

53

1

R → K. Ref.4 Ref.5
Corresponds to variant rs486055 [ dbSNP | Ensembl ].

VAR_020950

Natural variant

65

1

G → R. Ref.5
Corresponds to variant rs17293607 [ dbSNP | Ensembl ].

VAR_020951

Natural variant

142

1

E → Q in a breast cancer sample; somatic mutation. Ref.9

VAR_036139

Natural variant

226

1

F → L. Ref.5
Corresponds to variant rs17860971 [ dbSNP | Ensembl ].

VAR_020952

Natural variant

282

1

G → E. Ref.5
Corresponds to variant rs17860973 [ dbSNP | Ensembl ].

VAR_020953

Natural variant

440

1

L → F. Ref.5
Corresponds to variant rs17860996 [ dbSNP | Ensembl ].

VAR_020954

Natural variant

475

1

H → L. Ref.5
Corresponds to variant rs17861009 [ dbSNP | Ensembl ].

VAR_020955

Secondary structure

1

.

476

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P09238 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 516DCDDFEF92A0D6
Show »

FASTA

476

54,151

        10         20         30         40         50         60 
MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ FRRKDSNLIV 

        70         80         90        100        110        120 
KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS SFPGMPKWRK THLTYRIVNY 

       130        140        150        160        170        180 
TPDLPRDAVD SAIEKALKVW EEVTPLTFSR LYEGEADIMI SFAVKEHGDF YSFDGPGHSL 

       190        200        210        220        230        240 
AHAYPPGPGL YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN 

       250        260        270        280        290        300 
SFTELAQFRL SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST 

       310        320        330        340        350        360 
LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT VFIFKGNEFW 

       370        380        390        400        410        420 
AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY FFAADKYWRF DENSQSMEQG 

       430        440        450        460        470 
FPRLIADDFP GVEPKVDAVL QAFGFFYFFS GSSQFEFDPN ARMVTHILKS NSWLHC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The collagenase gene family in humans consists of at least four members." Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J., Breathnach R. Biochem. J. 253:187-192(1988) [PubMed: 2844164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Oesophagus.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-53. Tissue: Coronary artery.
[5]	NIEHS SNPs program Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-4; LYS-53; ARG-65; LEU-226; GLU-282; PHE-440 AND LEU-475.
[6]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[8]	"Crystal structure of the catalytic domain of human matrix metalloproteinase 10." Bertini I., Calderone V., Fragai M., Luchinat C., Mangani S., Terni B. J. Mol. Biol. 336:707-716(2004) [PubMed: 15095982] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 99-263, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, CALCIUM-BINDING, ZINC-BINDING SITES.
[9]	"The consensus coding sequences of human breast and colorectal cancers." 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. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-142.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07820 mRNA. Translation: CAA30679.1.
BT007442 mRNA. Translation: AAP36110.1.
AK222601 mRNA. Translation: BAD96321.1.
AK313960 mRNA. Translation: BAG36676.1.
AY744675 Genomic DNA. Translation: AAU21039.1.
CH471065 Genomic DNA. Translation: EAW67029.1.
BC002591 mRNA. Translation: AAH02591.1.

IPI

IPI00013405.

PIR

KCHUS2. A28816.

RefSeq

NP_002416.1. NM_002425.2.

UniGene

Hs.2258.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q3A	X-ray	2.10	A/B/C	99-263	[»]

ProteinModelPortal

P09238.

SMR

P09238. Positions 31-475.

ModBase

Search...

Protein-protein interaction databases

STRING

P09238.

Protein family/group databases

MEROPS

M10.006.

PTM databases

PhosphoSite

P09238.

Polymorphism databases

DMDM

116869.

Proteomic databases

PRIDE

P09238.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000279441; ENSP00000279441; ENSG00000166670.

GeneID

4319.

KEGG

hsa:4319.

UCSC

uc001phg.1. human.

Organism-specific databases

CTD

4319.

GeneCards

GC11M102641.

H-InvDB

HIX0010066.

HGNC

HGNC:7156. MMP10.

HPA

CAB002159.

MIM

185260. gene.

neXtProt

NX_P09238.

PharmGKB

PA30868.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11261.

GeneTree

ENSGT00580000081219.

HOGENOM

HBG747685.

HOVERGEN

HBG052484.

InParanoid

P09238.

OMA

RYFWRRS.

OrthoDB

EOG4KKZ2X.

PhylomeDB

P09238.

Gene expression databases

ArrayExpress

P09238.

Bgee

P09238.

CleanEx

HS_MMP10.

Genevestigator

P09238.

GermOnline

ENSG00000166670. Homo sapiens.

Family and domain databases

InterPro

IPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016293. Pept_M10A_matrix_strom.
IPR021190. Pept_M10A_matrixin.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Gene3D

G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
G3DSA:2.110.10.10. Hemopexin. 1 hit.

KO

K01396.

Pfam

PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001191. Peptidase_M10A_matrix. 1 hit.

PRINTS

PR00138. MATRIXIN.

SMART

SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]

SUPFAM

SSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.

PROSITE

PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

16993.

SOURCE

Search...

Entry information

Entry name

MMP10_HUMAN

Accession

Primary (citable) accession number: P09238
Secondary accession number(s): B2R9X9, Q53HH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.