Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

1-244 (TPR repeats and activation domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A7E3N7

Entry ID Method Resolution Chain Position Source
AF-A7E3N7-F1 Predicted AlphaFoldDB

No variants for A7E3N7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7E3N7

No associated diseases with A7E3N7

5 regional properties for A7E3N7

Type Name Position InterPro Accession
domain Pleckstrin homology domain 350 - 455 IPR001849
domain FERM central domain 263 - 555 IPR019748
domain Band 4.1 domain 94 - 556 IPR019749
domain Kindlin/fermitin, PH domain 350 - 474 IPR037837
domain Kindlin-2, N-terminal 11 - 98 IPR040790

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell membrane
  • Translocation to membranes depends on NOXO1 or NCF1 and maybe RAC1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
NADPH oxidase complex A enzyme complex of which the core is a heterodimer composed of a light (alpha) and heavy (beta) chain, and requires several other water-soluble proteins of cytosolic origin for activity. Functions in superoxide generation by the NADPH-dependent reduction of O2.

4 GO annotations of molecular function

Name Definition
enzyme binding Binding to an enzyme, a protein with catalytic activity.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
small GTPase binding Binding to a small monomeric GTPase.
superoxide-generating NADPH oxidase activator activity Binds to and increases the activity of the enzyme superoxide-generating NADPH oxidase.

4 GO annotations of biological process

Name Definition
regulation of hydrogen peroxide metabolic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving hydrogen peroxide.
regulation of respiratory burst Any process that modulates the rate frequency or extent of a phase of elevated metabolic activity, during which oxygen consumption increases; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals.
superoxide anion generation The enzymatic generation of superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species, by a cell in response to environmental stress, thereby mediating the activation of various stress-inducible signaling pathways.
superoxide metabolic process The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O77775 NCF2 Neutrophil cytosol factor 2 Bos taurus (Bovine) PR
Q5HYK7 SH3D19 SH3 domain-containing protein 19 Homo sapiens (Human) PR
Q6XZF7 DNMBP Dynamin-binding protein Homo sapiens (Human) PR
P19878 NCF2 Neutrophil cytosol factor 2 Homo sapiens (Human) PR
Q86UR1 NOXA1 NADPH oxidase activator 1 Homo sapiens (Human) EV
O70145 Ncf2 Neutrophil cytosol factor 2 Mus musculus (Mouse) PR
Q8CJ00 Noxa1 NADPH oxidase activator 1 Mus musculus (Mouse) SS
A7E3N2 Ncf2 Neutrophil cytosol factor 2 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSSLGDQIRD WHRGVLAVAR EDWDSALCFF SDVREPLAKM YFNMGCVHLM AGDPEAALRA
70 80 90 100 110 120
FDQAVTKDTC MAVGFLQRGV ANFQLQRLQE AVSDFQLALA QLRGNAAIDY TQLGLDFKLQ
130 140 150 160 170 180
AWEVLYNMAS VQCQAGLWTK AANTLVEAIS KRPEGAQDTL EAAMDKVQKQ VPLQLRQVPK
190 200 210 220 230 240
GEVFQPPRRY LKHLEPMDFL GKAKVVASVI PDDHNSDIQP QQSSQVEQAG LQSSSPVCKR
250 260 270 280 290 300
VLSTRGGHMS PGLWDSLLAT GGPVPGPSED SSSAEGTATK DPESLVTVTV QCHFTVPLKV
310 320 330 340 350 360
PRGTDLSSFR TLLSQALLQQ TQKGQFSYKA RGEDRAWVPI STEDSLQSVW RNVPVSPRGL
370 380 390 400 410 420
QLQCRGAWGR PVLYQVVAQY DYRAQRPEDL DFRQGDTVDV LCEVDEAWLE GHRDGRVGIF
430 440
PKCFVVPAAT CVEALPVPEP QPGEQH