Disintegrin and metalloproteinase domain-containing protein 15

UniProt data

UniProt name: ADA15_HUMAN (Q13444)

Gene name: ADAM15; Synonyms=MDC15

Organism: Homo sapiens (Human).

Function: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.

Subcellular location: Endomembrane system {ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein {ECO:0000269|PubMed:12243749}. Cell junction, adherens junction {ECO:0000269|PubMed:12243749}. Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity). {ECO:0000250}.

Transmembrane domains:

  1. 697-717, 21 AA, Helical. {ECO:0000255}.

Sequence: 863 AA

10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS 790 800 810 820 830 840 KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA 850 860 GIPPLVVPSR PAPPPPTVSS LYL

CATM prediction

The sequence of ADA15_HUMAN returned 1 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
        700       710       7
 +    |    +    |    +    |		 (Å) (°) (Å) (°)  
Model 1 LTTGLLLSLLVLLVLVMLGASYWYRAR 6.9 -54.9° 1.5 45.1 -17.2

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


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Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 709, VAL, HA A, 708, LEU, O 3.41Å
B, 712, GLY, HA1 A, 709, VAL, O 2.85Å
B, 713, ALA, HA A, 712, GLY, O 3.38Å
A, 709, VAL, HA B, 708, LEU, O 3.41Å
A, 712, GLY, HA1 B, 709, VAL, O 2.85Å
A, 713, ALA, HA B, 712, GLY, O 3.38Å