Stromelysin-2 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P09238 (MMP10_HUMAN)

Last modified July 7, 2009. Version 110. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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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.

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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.
Cofactor	Binds 2 zinc ions per subunit By similarity. Calcium By similarity.
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.

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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
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	extracellular space Ref.1 Traceable author statement. Source: ProtInc proteinaceous extracellular matrix Ref.1 Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Probable

Propeptide

18 – 98

Activation peptide

PRO_0000028764

Chain

99 – 476

378

Stromelysin-2

PRO_0000028765

Regions

Domain

295 – 337

Hemopexin-like 1

Domain

339 – 382

Hemopexin-like 2

Domain

387 – 434

Hemopexin-like 3

Domain

436 – 476

Hemopexin-like 4

Motif

89 – 96

Cysteine switch By similarity

Sites

Active site

218

By similarity

Metal binding

Zinc; in inhibited form By similarity

Metal binding

217

Zinc; catalytic By similarity

Metal binding

221

Zinc; catalytic By similarity

Metal binding

227

Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond

289 ↔ 476

By similarity

Natural variations

Natural variant

L → V: dbSNP rs17435959. Ref.4

VAR_020949

Natural variant

R → K: dbSNP rs486055. Ref.4 Ref.3

VAR_020950

Natural variant

G → R: dbSNP rs17293607. Ref.4

VAR_020951

Natural variant

142

E → Q in a breast cancer sample; somatic mutation. Ref.6

VAR_036139

Natural variant

226

F → L: dbSNP rs17860971. Ref.4

VAR_020952

Natural variant

282

G → E: dbSNP rs17860973. Ref.4

VAR_020953

Natural variant

440

L → F: dbSNP rs17860996. Ref.4

VAR_020954

Natural variant

475

H → L: dbSNP rs17861009. Ref.4

VAR_020955

Secondary structure

476

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09238-1 [UniParc].

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

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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]	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.
[4]	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.
[5]	"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.
[6]	"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.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

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

IPI

IPI00013405.

PIR

KCHUS2. A28816.

RefSeq

NP_002416.1.

UniGene

Hs.2258

3D structure databases

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

ModBase

Search...

Protein family/group databases

MEROPS

M10.006.

Proteomic databases

PRIDE

P09238.

Genome annotation databases

Ensembl

ENSG00000166670. Homo sapiens. [Contig view]

GeneID

4319.

KEGG

hsa:4319.

UCSC

uc001phg.1. human.

Organism-specific databases

GeneCards

GC11M102146.

H-InvDB

HIX0010066.

HGNC

HGNC:7156. MMP10.

HPA

CAB002159.

MIM

185260. gene.

PharmGKB

PA30868.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09238.

HOVERGEN

P09238.

OMA

P09238. RYFWRRS.

Enzyme and pathway databases

BRENDA

3.4.24.22. 247.

Gene expression databases

ArrayExpress

P09238.

Bgee

P09238.

CleanEx

HS_MMP10.

GermOnline

ENSG00000166670. Homo sapiens.

Family and domain databases

InterPro

IPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR001818. Pept_M10A_M12B.
IPR016293. Pept_M10A_matrix.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Gene3D

G3DSA:2.110.10.10. Hemopexin. 1 hit.

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]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

16993.

SOURCE

Search...

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Entry information

Entry name

MMP10_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	July 7, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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