Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9GLE5

Entry ID Method Resolution Chain Position Source
AF-Q9GLE5-F1 Predicted AlphaFoldDB

No variants for Q9GLE5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9GLE5

No associated diseases with Q9GLE5

14 regional properties for Q9GLE5

Type Name Position InterPro Accession
domain Fibronectin type II domain 227 - 277 IPR000562-1
domain Fibronectin type II domain 285 - 335 IPR000562-2
domain Fibronectin type II domain 343 - 393 IPR000562-3
domain Hemopexin-like domain 467 - 661 IPR000585
domain Peptidase M10, metallopeptidase 119 - 447 IPR001818
domain Peptidoglycan binding-like 50 - 98 IPR002477
domain Peptidase, metallopeptidase 116 - 448 IPR006026
conserved_site Hemopexin, conserved site 607 - 622 IPR018486
repeat Hemopexin-like repeats 469 - 519 IPR018487-1
repeat Hemopexin-like repeats 518 - 564 IPR018487-2
repeat Hemopexin-like repeats 566 - 616 IPR018487-3
repeat Hemopexin-like repeats 615 - 661 IPR018487-4
binding_site Peptidase M10A, cysteine switch, zinc binding site 101 - 108 IPR021158
domain Peptidase M10A, catalytic domain 119 - 447 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.

17 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SZV7 HPX Hemopexin Bos taurus (Bovine) PR
O77656 MMP13 Collagenase 3 Bos taurus (Bovine) PR
Q90611 MMP2 72 kDa type IV collagenase Gallus gallus (Chicken) PR
Q8MPP3 Mmp2 Matrix metalloproteinase-2 Drosophila melanogaster (Fruit fly) PR
P04004 VTN Vitronectin Homo sapiens (Human) PR
P45452 MMP13 Collagenase 3 Homo sapiens (Human) PR
Q99542 MMP19 Matrix metalloproteinase-19 Homo sapiens (Human) PR
Q9NPA2 MMP25 Matrix metalloproteinase-25 Homo sapiens (Human) PR
Q9H239 MMP28 Matrix metalloproteinase-28 Homo sapiens (Human) PR
P34960 Mmp12 Macrophage metalloelastase Mus musculus (Mouse) PR
P33435 Mmp13 Collagenase 3 Mus musculus (Mouse) PR
P28862 Mmp3 Stromelysin-1 Mus musculus (Mouse) PR
P33434 Mmp2 72 kDa type IV collagenase Mus musculus (Mouse) PR
P23097 Mmp13 Collagenase 3 Rattus norvegicus (Rat) PR
Q63341 Mmp12 Macrophage metalloelastase Rattus norvegicus (Rat) PR
P33436 Mmp2 72 kDa type IV collagenase Rattus norvegicus (Rat) PR
Q6PHG2 hpx Hemopexin Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MTEARVSRGA LAALLRALCA LGCLLGRAAA APSPIIKFPG DVAPKTDKEL AVQYLNTFYG
70 80 90 100 110 120
CPKESCNLFV LKDTLKKMQK FFGLPQTGEL DQSTIETMRK PRCGNPDVAN YNFFPRKPKW
130 140 150 160 170 180
DKNQITYRII GYTPDLDPQT VDDAFARAFQ VWSDVTPLRF SRIHDGEADI MINFGRWEHG
190 200 210 220 230 240
DGYPFDGKDG LLAHAFAPGP GVGGDSHFDD DELRTLGEGQ VVRVKYGNAD GEYCKFPFRF
250 260 270 280 290 300
NGKEYTSCTD TGRSDGFLWC STTYNFDKDG KYGFCPHEAL FTMGGNADGQ PCKFPFRFQG
310 320 330 340 350 360
TSYDSCTTEG RTDGYRWCGT TEDYDRDKEY GFCPETAMST VGGNSEGAPC VLPFTFLGNK
370 380 390 400 410 420
HESCTSAGRS DGKLWCATTS NYDDDRKWGF CPDQGYSLFL VAAHEFGHAM GLEHSQDPGA
430 440 450 460 470 480
LMAPIYTYTK NFRLSHDDIQ GIQELYGASP DIDTGTGPTP TLGPVTPELC KQDIVFDGIS
490 500 510 520 530 540
QIRGEIFFFK DRFIWRTVTP RDKPTGPLLV ATFWPELPEK IDAVYEDPQE EKAVFFAGNE
550 560 570 580 590 600
YWVYSASTLE RGYPKPLTSL GLPPGVQKVD AAFNWSKNKK TYIFAGDKFW RYNEVKKKMD
610 620 630 640 650 660
PGFPKLIADA WNAIPDNLDA VVDLQGGGHS YFFKGAYYLK LENQSLKSVK FGSIKSDWLG
C