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 P54680

Entry ID Method Resolution Chain Position Source
AF-P54680-F1 Predicted AlphaFoldDB

No variants for P54680

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P54680

No associated diseases with P54680

10 regional properties for P54680

Type Name Position InterPro Accession
conserved_site Actinin-type actin-binding domain, conserved site 204 - 228 IPR001589-1
conserved_site Actinin-type actin-binding domain, conserved site 381 - 390 IPR001589-2
conserved_site Actinin-type actin-binding domain, conserved site 460 - 484 IPR001589-3
domain Calponin homology domain 116 - 232 IPR001715-1
domain Calponin homology domain 260 - 365 IPR001715-2
domain Calponin homology domain 379 - 488 IPR001715-3
domain Calponin homology domain 501 - 608 IPR001715-4
domain EF-hand domain 7 - 78 IPR002048
binding_site EF-Hand 1, calcium-binding site 20 - 32 IPR018247-1
binding_site EF-Hand 1, calcium-binding site 56 - 68 IPR018247-2

Functions

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

7 GO annotations of cellular component

Name Definition
actin filament A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
actin filament bundle An assembly of actin filaments that are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
cell leading edge The area of a motile cell closest to the direction of movement.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
phagocytic cup An invagination of the cell membrane formed by an actin dependent process during phagocytosis. Following internalization it is converted into a phagosome.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.

2 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
calcium ion binding Binding to a calcium ion (Ca2+).

3 GO annotations of biological process

Name Definition
actin filament bundle assembly The assembly of actin filament bundles; actin filaments are on the same axis but may be oriented with the same or opposite polarities and may be packed with different levels of tightness.
actin filament network formation The assembly of a network of actin filaments; actin filaments on different axes and with differing orientations are crosslinked together to form a mesh of filaments.
sexual reproduction A type of reproduction that combines the genetic material of two gametes (such as a sperm or egg cell or fungal spores). The gametes have an haploid genome (with a single set of chromosomes, the product of a meiotic division) and combines with one another to produce a zygote (diploid).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTNFSESEIS EFKASFNQFD ENGDGQISAL ELQKILTKCG EKVTGVEVRD MIKEVDTDGN
70 80 90 100 110 120
GSIDFKEFLQ VMQKARQHSA NASPAFASAV KKVGAVNTIG GYSGSTASGV QHSYSDEEKV
130 140 150 160 170 180
AYIDWINNCL AKDVDLKSRL PIPEDGDKFF AACNDGLLLC KLINDAVPDT IDERVLNKKN
190 200 210 220 230 240
LNAFRINENQ VLCINSAKAI GCNVVNIGAG DLVEGRAHLI MGLTWQIIKI GLFARINLTN
250 260 270 280 290 300
HPELYRLLHD GETIEDLLKL PVEEILLRWF NYHLAAAGSQ RRVKNFSGDI KDSECYTILL
310 320 330 340 350 360
KQIAPKDAGV ETSALNISNL DQRAVKVLEN ADKLGCKKFL KPKDIVTGFQ KLNLAFVANL
370 380 390 400 410 420
FNTHPALEPV EDVVIIEETR EEKTFRNWMN SLGVDPFVNN LYEGTYDGLI LIQLFDKIYP
430 440 450 460 470 480
GLVDHKKVNY PPYKAMGAEM KKIENCNYAI QLGKDCKYSL VGIDGKNVYD KNKTLTLSIL
490 500 510 520 530 540
WQLMRGHVIS ILTALSGSGK PIADADIVNW TNSKLSAAGK KQISGFKDST ISTGIPILDV
550 560 570 580 590 600
IEAVRPGSVD PALVATSGSA EDNLLNAKLA VSTARKVGAV VFALPEDIVE VKPKMVLTLF
ASLWQVEMTK