B7YZY9

EV
Gene name
Su(dx) (AIP4, anon-WO0073329.1, anon-WO0073329.2, anon-WO0073329.4, Dmel\CG4244, ITCH, Itch, Su, (Dx), Su(deltex), Su(DX), Su(Dx), su(dx), CG4244, Dmel_CG4244)
Protein name
E3 ubiquitin-protein ligase
Names
EC 2.3.2.26
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG4244
EC number
2.3.2.-: Aminoacyltransferases
Protein Class
HECT DOMAIN UBIQUITIN-PROTEIN LIGASE (PTHR11254)

Descriptions

The E3 ubiquitin-protein ligase Itch (Su(dx), also known as Itch) is a protein that accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates The Su(dx) exhibited enhanced ligase activity when either the WW2 or L domain was removed. The domains in WW domains, except for the L domain, robustly inhibit the ligase activity of the Su(dx) HECT domain in a dose-dependent manner. This indicates that the L domain is essential but not sufficient for its autoinhibition. Furthermore, the WW domains are involved in its ligase regulation. The recruitment of the adaptor protein dNdfip, which contains multiple-PY motifs, via WW domains results in the release of the inhibitory state of Su(dx), leading to substrate ubiquitination.

Autoinhibitory domains (AIDs)

395-454 (WW2L domains) EV

Target domain

585-949 (HECT domain)

Relief mechanism

Partner binding

Assay

Structural analysis, Deletion assay, Mutagenesis experiment

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B7YZY9

Entry ID Method Resolution Chain Position Source
AF-B7YZY9-F1 Predicted AlphaFoldDB

No variants for B7YZY9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7YZY9

No associated diseases with B7YZY9

2 regional properties for B7YZY9

Type Name Position InterPro Accession
domain Gasdermin, pore forming domain 3 - 233 IPR040460
domain Gasdermin, PUB domain 252 - 416 IPR041263

Functions

Description
EC Number 2.3.2.- Aminoacyltransferases
Subcellular Localization
PANTHER Family PTHR11254 HECT DOMAIN UBIQUITIN-PROTEIN LIGASE
PANTHER Subfamily PTHR11254:SF429 E3 UBIQUITIN-PROTEIN LIGASE SU(DX)
PANTHER Protein Class ubiquitin-protein ligase
PANTHER Pathway Category Ubiquitin proteasome pathway
E3

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond

3 GO annotations of biological process

Name Definition
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
regulation of signal transduction Any process that modulates the frequency, rate or extent of signal transduction.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADGNGLPAG AASGGMEAGQ TVNGAGSASP TPTSSSGAGA SGSANQGYHQ LSVTIEEASL
70 80 90 100 110 120
RNNGFLKPNP YVELLIDSKS KRKTDLVKNS YLPKWNEEFT VLITPNSTLH FKVLDHSSFR
130 140 150 160 170 180
KDAMLGERII NLAHILQHYN GRCEFLELTI DLFVTSKSDN RQTKSGELVA ILNGLKLDMS
190 200 210 220 230 240
KLQIQPVAGQ QNGNPPVQAV NPSVVSDAAA GRSCMIYGGV RARMRLRSSS GNSNGGETRS
250 260 270 280 290 300
PLPNGGGDHR RSTQAPPVWE QQQQQSQNQQ QPLRMVNGSG AAVPQTAPYP QQPPAPALAR
310 320 330 340 350 360
PLTQVYGALP ENTQPAAVYL PAGGGAAVGP PGVAGPPIEQ PGVGLPVSQS TDPQLQTQPA
370 380 390 400 410 420
DDEPLPAGWE IRLDQYGRRY YVDHNTRSTY WEKPTPLPPG WEIRKDGRGR VYYVDHNTRK
430 440 450 460 470 480
TTWQRPNSER LMHFQHWQGQ RAHVVSQGNQ RYLYSQQQQQ PTAVTAQVTQ DDEDALGPLP
490 500 510 520 530 540
DGWEKKIQSD NRVYFVNHKN RTTQWEDPRT QGQEVSLINE GPLPPGWEIR YTAAGERFFV
550 560 570 580 590 600
DHNTRRTTFE DPRPGAPKGA KGVYGVPRAY ERSFRWKLSQ FRYLCQSNAL PSHIKITVTR
610 620 630 640 650 660
QTLFEDSYHQ IMRLPAYELR RRLYIIFRGE EGLDYGGVSR EWFFLLSHEV LNPMYCLFEY
670 680 690 700 710 720
ANKNNYSLQI NPASYVNPDH LQYFKFIGRF IAMALYHGRF IYSGFTMPFY KRMLNKKLTI
730 740 750 760 770 780
KDIETIDPEF YNSLIWVKDN NIDECGLELW FSVDFEVLGQ IIHHELKENG EKERVTEENK
790 800 810 820 830 840
EEYITLMTEW RMTRGIEQQT KTFLEGFNEV VPLEWLKYFD ERELELILCG MQDVDVEDWQ
850 860 870 880 890 900
RNTIYRHYNR NSKQVVWFWQ FVRETDNEKR ARLLQFVTGT CRVPVGGFAE LMGSNGPQRF
910 920 930 940
CIEKVGKETW LPRSHTCFNR LDLPPYKSYD QLVEKLTFAI EETEGFCQE