MMP1 (11q22.2) sinkistä riippuva MMP, ZnMc matrilysiini domeenin ja HX propellin omaava. Hemopexiinitoistoa 4-siipi propellina

1. ORIGIN 1 mqeffglkvt gkpdaetlkv MkqPRCGVPD vaqfvltegn prweqthlty rienytpdlp
   

          61 radvdhaiek afqlwsnvtp ltftkvsegq adimisfvrg dhrdnspfdg pggnlahafq
         121 pgpgiggdah fdederwtnn freynlhrva aHElgHslgl sHstdigalm ypsytfsgdv
         181 qlaqddidgi qaiygrsqnp vqpigpqtpk acdskltfda ittirgevmf fkdrfymrtn
         241 pfypevelnf isvfwpqlpn gleaayefad rdevrffkgn kywavqgqnv lhgypkdiys
         301 sfgfprtvkh idaalseent gktyffvank ywrydeykrs mdpgypkmia hdfpgighkv
         361 davfmkdgff yffhgtrqyk fdpktkrilt lqkanswfnc rkn
   //

    (Tästä mtixmetalloproteiinista on useita  artikkeleita PubMed lähteestä vuodelta 2019. Nyt katson nitä MMP- molekyylejäuudestaan. ne ovat sinkistä riippuvaisia. Katalyyttisessä kohdassa on  Zn ja Hemopexiinipropelli koordinoi  Zn tai Calsiumia.
   Signaalipeptidin jälkeen  oleva propeptidio on n 80 aminoappoa ja siinä on tunnusomaista konservatiivinen sekvenssi PRCG(C/N)PD, tässä  peptidissä se on 24..30  kohdalla. Siinä näkyvä cysteiini(C)  kiinnitty katalyyttisen domeenin Zn metalliin ja pitää täten yllä  MMP-proteiinin latenssitilaa , propeptidimuotoa (pro-MMP). 
   Katalyyttinen kohta on 42..195, " ZnMc_MMP.  Siinä on sinkkiä sitova kohta jakson keskellä motiivissa HEXXHXUGUXH, (U tarkoittaa hydrofobista bulk-aminohappoa) .  
   H152, E153, H156, H162.  
   C-terminaalissa päin oleva hemopexiini moduli (HX toistoja 4) , 4-siipinen propelli, jota sitoutuneet metallit pitävät koossa  2-siipinen  propelli,   sinkkia tai  kalsiumia metallina.  
    (Hemopexin-like superfamily- tunnus)
   NM_001145938.2 → NP_001139410.1  interstitial collagenase isoform 2
   See identical proteins and their annotated locations for NP_001139410.1
   
   Status: REVIEWED

   Description

   Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 5' coding region and uses a downstream start codon compared to variant 1. The resulting protein (isoform 2) has a shorter N-terminus compared to isoform 1.

   Source sequence(s)

   AK297723, AP000619

   UniProtKB/TrEMBL

   B4DN15

   Conserved Domains (4) summary

   cd00094
   Location:209 → 400

   HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of  metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.

    

   cd04278
   Location:42 → 195

   weqthlty rienytpdlp
          61 radvdhaiek afqlwsnvtp ltftkvsegq adimisfvrg dhrdnspfdg pggnlahafq
         121 pgpgiggdah fdederwtnn freynlhrva ahelghslgl shstdigalm ypsytfsgdv
         181 qlaqddidgi qaiyg

   ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ..specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).

   Feature 1:active site [active site]

   Evidence:

   • Comment:consensus motif: HEXXHXUGUXH U= bulky hydrophobic
   • Comment:coordinates zinc, contains catalytic Glu
   • Citation:PMID 8253063
   • Structure:1BQQ: Human type-1 matrix metalloprotease coordinates zinc
     - View structure with Cn3D
   • Citation:PMID 9724659

    

    

   pfam00413

    
   Location:42 → 195

   Peptidase_M10; MatrixinThe members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.

   pfam01471
   Location:1 → 21

   PG_binding_1; Putative peptidoglycan binding domainThis domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. .. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.