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 P25723

Entry ID Method Resolution Chain Position Source
AF-P25723-F1 Predicted AlphaFoldDB

No variants for P25723

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P25723

No associated diseases with P25723

16 regional properties for P25723

Type Name Position InterPro Accession
ptm EGF-type aspartate/asparagine hydroxylation site 606 - 617 IPR000152-1
ptm EGF-type aspartate/asparagine hydroxylation site 768 - 779 IPR000152-2
domain EGF-like domain 591 - 631 IPR000742-1
domain EGF-like domain 753 - 793 IPR000742-2
domain CUB domain 340 - 477 IPR000859-1
domain CUB domain 478 - 591 IPR000859-2
domain CUB domain 634 - 753 IPR000859-3
domain CUB domain 797 - 909 IPR000859-4
domain CUB domain 910 - 1026 IPR000859-5
domain Peptidase M12A 136 - 338 IPR001506
domain EGF-like calcium-binding domain 591 - 631 IPR001881-1
domain EGF-like calcium-binding domain 753 - 793 IPR001881-2
domain Peptidase, metallopeptidase 142 - 286 IPR006026
conserved_site EGF-like calcium-binding, conserved site 591 - 615 IPR018097-1
conserved_site EGF-like calcium-binding, conserved site 753 - 777 IPR018097-2
domain Tolloid/BMP1 peptidase domain 137 - 338 IPR034036

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

4 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
collagen binding Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
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).

9 GO annotations of biological process

Name Definition
amnioserosa formation Formation of the amnioserosa, an epithelium that occupies a hole in the embryonic dorsal epidermis. This occurs by the transformation of a narrow strip of cells at the dorsal midline of the blastoderm from columnar to squamous cells, accompanied by a lateral shift.
dorsal/ventral pattern formation The regionalization process in which the areas along the dorsal/ventral axis are established that will lead to differences in cell differentiation. The dorsal/ventral axis is defined by a line that runs orthogonal to both the anterior/posterior and left/right axes. The dorsal end is defined by the upper or back side of an organism. The ventral end is defined by the lower or front side of an organism.
imaginal disc-derived wing vein morphogenesis The process in which anatomical structures of the veins on an imaginal disc-derived wing are generated and organized.
maternal specification of dorsal/ventral axis, oocyte, soma encoded Polarization of the oocyte along the dorsal-ventral axis, by a gene product encoded by somatic cells. An example of this is found in Drosophila melanogaster.
positive regulation of activin receptor signaling pathway Any process that activates or increases the frequency, rate or extent of the activity of any activin receptor signaling pathway.
positive regulation of BMP signaling pathway Any process that activates or increases the frequency, rate or extent of BMP signaling pathway activity.
protein processing Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
R8 cell fate specification The process in which a cell becomes capable of differentiating autonomously into an R8 cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.

19 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9DER7 TLL1 Tolloid-like protein 1 Gallus gallus (Chicken) PR
P98066 TNFAIP6 Tumor necrosis factor-inducible gene 6 protein Homo sapiens (Human) PR
Q9Y6L7 TLL2 Tolloid-like protein 2 Homo sapiens (Human) PR
P13497 BMP1 Bone morphogenetic protein 1 Homo sapiens (Human) PR
O43897 TLL1 Tolloid-like protein 1 Homo sapiens (Human) PR
Q6HA09 Astl Astacin-like metalloendopeptidase Mus musculus (Mouse) PR
O08859 Tnfaip6 Tumor necrosis factor-inducible gene 6 protein Mus musculus (Mouse) PR
P98063 Bmp1 Bone morphogenetic protein 1 Mus musculus (Mouse) PR
Q9WVM6 Tll2 Tolloid-like protein 2 Mus musculus (Mouse) PR
Q62381 Tll1 Tolloid-like protein 1 Mus musculus (Mouse) PR
Q9U3S9 nas-6 Zinc metalloproteinase nas-6 Caenorhabditis elegans PR
P55112 nas-4 Zinc metalloproteinase nas-4 Caenorhabditis elegans PR
P55113 nas-7 Zinc metalloproteinase nas-7 Caenorhabditis elegans PR
Q18439 nas-8 Zinc metalloproteinase nas-8 Caenorhabditis elegans PR
Q20942 nas-38 Zinc metalloproteinase nas-38 Caenorhabditis elegans PR
Q21252 nas-3 Zinc metalloproteinase nas-3 Caenorhabditis elegans PR
P55115 nas-15 Zinc metalloproteinase nas-15 Caenorhabditis elegans PR
Q20176 nas-39 Zinc metalloproteinase nas-39 Caenorhabditis elegans PR
O57460 tll1 Dorsal-ventral patterning tolloid-like protein 1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MKGMRLMPMK MKAKLVVLSV GALWMMMFFL VDYAEGRRLS QLPESECDFD FKEQPEDFFG
70 80 90 100 110 120
ILDSSLVPPK EPKDDIYQLK TTRQHSGRRR KQSHKSQNKA ALRLPPPFLW TDDAVDVLQH
130 140 150 160 170 180
SHSPTLNGQP IQRRRRAVTV RKERTWDYGV IPYEIDTIFS GAHKALFKQA MRHWENFTCI
190 200 210 220 230 240
KFVERDPNLH ANYIYFTVKN CGCCSFLGKN GNGRQPISIG RNCEKFGIII HELGHTIGFH
250 260 270 280 290 300
HEHARGDRDK HIVINKGNIM RGQEYNFDVL SPEEVDLPLL PYDLNSIMHY AKNSFSKSPY
310 320 330 340 350 360
LDTITPIGIP PGTHLELGQR KRLSRGDIVQ ANLLYKCASC GRTYQQNSGH IVSPHFIYSG
370 380 390 400 410 420
NGVLSEFEGS GDAGEDPSAE SEFDASLTNC EWRITATNGE KVILHLQQLH LMSSDDCTQD
430 440 450 460 470 480
YLEIRDGYWH KSPLVRRICG NVSGEVITTQ TSRMLLNYVN RNAAKGYRGF KARFEVVCGG
490 500 510 520 530 540
DLKLTKDQSI DSPNYPMDYM PDKECVWRIT APDNHQVALK FQSFELEKHD GCAYDFVEIR
550 560 570 580 590 600
DGNHSDSRLI GRFCGDKLPP NIKTRSNQMY IRFVSDSSVQ KLGFSAALML DVDECKFTDH
610 620 630 640 650 660
GCQHLCINTL GSYQCGCRAG YELQANGKTC EDACGGVVDA TKSNGSLYSP SYPDVYPNSK
670 680 690 700 710 720
QCVWEVVAPP NHAVFLNFSH FDLEGTRFHY TKCNYDYLII YSKMRDNRLK KIGIYCGHEL
730 740 750 760 770 780
PPVVNSEQSI LRLEFYSDRT VQRSGFVAKF VIDVDECSMN NGGCQHRCRN TFGSYQCSCR
790 800 810 820 830 840
NGYTLAENGH NCTETRCKFE ITTSYGVLQS PNYPEDYPRN IYCYWHFQTV LGHRIQLTFH
850 860 870 880 890 900
DFEVESHQEC IYDYVAIYDG RSENSSTLGI YCGGREPYAV IASTNEMFMV LATDAGLQRK
910 920 930 940 950 960
GFKATFVSEC GGYLRATNHS QTFYSHPRYG SRPYKRNMYC DWRIQADPES SVKIRFLHFE
970 980 990 1000 1010 1020
IEYSERCDYD YLEITEEGYS MNTIHGRFCG KHKPPIIISN SDTLLLRFQT DESNSLRGFA
1030 1040 1050 1060
ISFMAVDPPE DSVGEDFDAV TPFPGYLKSM YSSETGSDHL LPPSRLI