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 Q20942

Entry ID Method Resolution Chain Position Source
AF-Q20942-F1 Predicted AlphaFoldDB

No variants for Q20942

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q20942

No associated diseases with Q20942

5 regional properties for Q20942

Type Name Position InterPro Accession
domain CUB domain 371 - 487 IPR000859
repeat Thrombospondin type-1 (TSP1) repeat 628 - 676 IPR000884
domain Peptidase M12A 113 - 312 IPR001506
domain Peptidase, metallopeptidase 120 - 262 IPR006026
domain Astacin-like metallopeptidase domain 128 - 309 IPR034035

Functions

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

1 GO annotations of cellular component

Name Definition
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.

2 GO annotations of molecular function

Name Definition
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).

2 GO annotations of biological process

Name Definition
molting cycle, collagen and cuticulin-based cuticle The periodic shedding of part or all of a collagen and cuticulin-based cuticle, which is then replaced by a new collagen and cuticulin-based cuticle. An example of this is found in the Nematode worm, Caenorhabditis elegans.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

21 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9DER7 TLL1 Tolloid-like protein 1 Gallus gallus (Chicken) PR
P25723 tld Dorsal-ventral patterning protein tolloid Drosophila melanogaster (Fruit fly) PR
O43897 TLL1 Tolloid-like protein 1 Homo sapiens (Human) PR
P98066 TNFAIP6 Tumor necrosis factor-inducible gene 6 protein Homo sapiens (Human) PR
P13497 BMP1 Bone morphogenetic protein 1 Homo sapiens (Human) PR
Q9Y6L7 TLL2 Tolloid-like protein 2 Homo sapiens (Human) PR
P98063 Bmp1 Bone morphogenetic protein 1 Mus musculus (Mouse) PR
Q9WVM6 Tll2 Tolloid-like protein 2 Mus musculus (Mouse) PR
O08859 Tnfaip6 Tumor necrosis factor-inducible gene 6 protein Mus musculus (Mouse) PR
Q62381 Tll1 Tolloid-like protein 1 Mus musculus (Mouse) PR
Q6HA09 Astl Astacin-like metalloendopeptidase Mus musculus (Mouse) PR
P55112 nas-4 Zinc metalloproteinase nas-4 Caenorhabditis elegans PR
P55113 nas-7 Zinc metalloproteinase nas-7 Caenorhabditis elegans PR
P55115 nas-15 Zinc metalloproteinase nas-15 Caenorhabditis elegans PR
Q18439 nas-8 Zinc metalloproteinase nas-8 Caenorhabditis elegans PR
Q20176 nas-39 Zinc metalloproteinase nas-39 Caenorhabditis elegans PR
Q21252 nas-3 Zinc metalloproteinase nas-3 Caenorhabditis elegans PR
Q9U3S9 nas-6 Zinc metalloproteinase nas-6 Caenorhabditis elegans PR
O62243 nas-1 Zinc metalloproteinase nas-1 Caenorhabditis elegans PR
Q22398 nas-22 Zinc metalloproteinase nas-22 Caenorhabditis elegans PR
O57460 tll1 Dorsal-ventral patterning tolloid-like protein 1 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MPSPSYNRHI IIASCFCCLL IFSSAARVPK ASKKHLARVK QLLNDEAERH NTLIQSDSVT
70 80 90 100 110 120
VFDDIQRNPN TGVHHDELAV NNADEYFQGD VDLSEQQVKI IEDQFTQGKR EKRKIGRNPL
130 140 150 160 170 180
YKKWDTRGPI SFDYAESIPF QTRQKIRSAM LLWQQHTCLR FEEGGPNVDR LEFFDGGGCS
190 200 210 220 230 240
SFVGRVGGTQ GISISTPGCD VVGIISHEIG HALGIFHEQA RPDQERHIAI NYNNIPLSRW
250 260 270 280 290 300
NNFQAVGENH AETYNLPYDT GSVMHYGPYG FASDPYTPTI RTLERVQQST IGQRAGPSFL
310 320 330 340 350 360
DYQAINMAYG CTESCADLPC LRNGYTHPNN CSMCACPEGL SGRYCEQVYP SNAQCARGKL
370 380 390 400 410 420
TRERHINERE CYQSAIWTAT KEVKYITSPN YPDKFPIDTE CNWIIAAPIE GRVFMEFEGD
430 440 450 460 470 480
FDFLCEDTCD KAYVEVKYHS DKRLTGARYC CSLLPKNRFI SFKNEMIIIM RGYRSSGAGF
490 500 510 520 530 540
KAKFWSNLGE PEGVSTPLPP TTAPLPEISE TTQKPEPTTV QSTTTYTTAI PRRTAKKQFF
550 560 570 580 590 600
TRKPITIPLT PLTSSSTTTE STTVSSTTQS TTWLPTEPSF ATGETEITTA SPTITLFPSL
610 620 630 640 650 660
STILPPINSL AGVLPSTQAP DIINSVLECG CGAWSEWQGE CSQQCGGCGH RLRKRECKKE
670 680 690 700 710 720
ACRKEEKRPC NFSACPDGTN FLINNAEFHI LWRGCCVGLF RSGDQCSALE TESNPFFKII
730 740
NSLLNIQDAK NNDTLIAKRM MRGEH