P50757

PR
Gene name
MMP2
Protein name
72 kDa type IV collagenase
Names
72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100009000
EC number
3.4.24.24: Metalloendopeptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-76 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P50757

Entry ID Method Resolution Chain Position Source
AF-P50757-F1 Predicted AlphaFoldDB

No variants for P50757

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P50757

No associated diseases with P50757

14 regional properties for P50757

Type Name Position InterPro Accession
domain Fibronectin type II domain 226 - 276 IPR000562-1
domain Fibronectin type II domain 284 - 334 IPR000562-2
domain Fibronectin type II domain 342 - 392 IPR000562-3
domain Hemopexin-like domain 468 - 662 IPR000585
domain Peptidase M10, metallopeptidase 118 - 446 IPR001818
domain Peptidoglycan binding-like 48 - 97 IPR002477
domain Peptidase, metallopeptidase 115 - 447 IPR006026
conserved_site Hemopexin, conserved site 608 - 623 IPR018486
repeat Hemopexin-like repeats 474 - 520 IPR018487-1
repeat Hemopexin-like repeats 519 - 565 IPR018487-2
repeat Hemopexin-like repeats 567 - 617 IPR018487-3
repeat Hemopexin-like repeats 616 - 662 IPR018487-4
binding_site Peptidase M10A, cysteine switch, zinc binding site 100 - 107 IPR021158
domain Peptidase M10A, catalytic domain 118 - 446 IPR033739

Functions

Description
EC Number 3.4.24.24 Metalloendopeptidases
Subcellular Localization
  • Secreted, extracellular space, extracellular matrix
  • Membrane
  • Nucleus
  • Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas
  • Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
extracellular matrix A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
cellular response to UV-A Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a UV-A radiation stimulus. UV-A radiation (UV-A light) spans the wavelengths 315 to 400 nm.
collagen catabolic process The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEALGARGAL AGFLRALCVL GCLLGRATAP PSPVIKFPGD VAPKTDKELA VQYLNTFYGC
70 80 90 100 110 120
PKDSCNLFVL KDTLKKMQKF FGLPQTGELD QSTIETMRKP RCGNPDVANY NFFPRKPKWD
130 140 150 160 170 180
KNQITYRIIG YTPDLDPETV DDAFARAFQV WSNVTPLRFS RIHDGEADIM INFGRWEHGD
190 200 210 220 230 240
GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN
250 260 270 280 290 300
GKEYTSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNADGQP CKFPFRFQGT
310 320 330 340 350 360
SYSSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTI GGNSEGAPCV FPFTFLGNKY
370 380 390 400 410 420
ESCTSAGRSD GKMWCATSTN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL
430 440 450 460 470 480
MAPIYTYTKN FRLSQDDIKG IQELYGASPD AGTDAGTGPT PTLGPVTPEI CTQDIVFDGI
490 500 510 520 530 540
AQIRGEIFFF KDRFIWRTVT PGDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN
550 560 570 580 590 600
EYWVYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM
610 620 630 640 650 660
DPGFPRLIAD AWNAIPDHLD AVVDLQGSGH SYFFKGTYYL KLENQSLKSV KVGSIKTDWL
GC