Descriptions

(Annotation from UniProt)
The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.

Autoinhibitory domains (AIDs)

Target domain

94-490 (GBD/FH3 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P40450

Entry ID Method Resolution Chain Position Source
AF-P40450-F1 Predicted AlphaFoldDB

43 variants for P40450

Variant ID(s) Position Change Description Diseaes Association Provenance
s09-41898 25 V>A No SGRP
s09-42076 84 N>K No SGRP
s09-42275 151 T>A No SGRP
s09-42365 181 T>A No SGRP
s09-42785 321 H>Y No SGRP
s09-42866 348 Q>E No SGRP
s09-43004 394 F>V No SGRP
s09-43644 607 S>N No SGRP
s09-43664 614 G>C No SGRP
s09-43715 631 A>T No SGRP
s09-44120 766 P>S No SGRP
s09-44274 817 A>V No SGRP
s09-44331 836 G>D No SGRP
s09-44333 837 P>S No SGRP
s09-44342 840 H>N No SGRP
s09-44390 856 S>P No SGRP
s09-44414 864 P>S No SGRP
s09-44423 867 T>A No SGRP
s09-44424 867 T>I No SGRP
s09-44426 868 D>N No SGRP
s09-44433 870 K>R No SGRP
s09-44435 871 P>A No SGRP
s09-44438 872 P>T No SGRP
s09-44441 873 P>S No SGRP
s09-44444 874 T>S No SGRP
s09-44580 919 I>T No SGRP
s09-44586 921 K>R No SGRP
s09-44619 932 R>K No SGRP
s09-44634 937 S>L No SGRP
s09-44636 938 I>V No SGRP
s09-44643 940 L>S No SGRP
s09-44770 982 M>I No SGRP
s09-44944 1040 L>F No SGRP
s09-44979 1052 A>V No SGRP
s09-45053 1077 I>V No SGRP
s09-45096 1091 K>R No SGRP
s09-45203 1127 I>V No SGRP
s09-45243 1140 V>G No SGRP
s09-45363 1180 I>T No SGRP
s09-45559 1245 K>N No SGRP
s09-45691 1289 D>E No SGRP
s09-45705 1294 S>N No SGRP
s09-45746 1308 K>E No SGRP

No associated diseases with P40450

6 regional properties for P40450

Type Name Position InterPro Accession
domain Pancreatic trypsin inhibitor Kunitz domain 50 - 104 IPR002223-1
domain Pancreatic trypsin inhibitor Kunitz domain 122 - 175 IPR002223-2
domain Pancreatic trypsin inhibitor Kunitz domain 220 - 273 IPR002223-3
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 81 - 99 IPR020901-1
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 152 - 170 IPR020901-2
conserved_site Proteinase inhibitor I2, Kunitz, conserved site 250 - 268 IPR020901-3

Functions

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

3 GO annotations of cellular component

Name Definition
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
cellular bud neck The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
mating projection tip The apex of the mating projection in unicellular fungi exposed to mating pheromone; site of polarized growth.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
profilin binding Binding to profilin, an actin-binding protein that forms a complex with G-actin and prevents it from polymerizing to form F-actin.
small GTPase binding Binding to a small monomeric GTPase.

6 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 nucleation The initial step in the formation of an actin filament, in which actin monomers combine to form a new filament. Nucleation is slow relative to the subsequent addition of more monomers to extend the filament.
barbed-end actin filament capping The binding of a protein or protein complex to the barbed (or plus) end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
formin-nucleated actin cable assembly The aggregation, arrangement and bonding together of a set of components to form a formin-nucleated actin cable. A formin-nucleated actin cable is an actin filament bundle that consists of short filaments organized into bundles of uniform polarity, and is nucleated by formins.
mitotic actomyosin contractile ring assembly Any actomyosin contractile ring assembly that is involved in mitotic cytokinesis.
positive regulation of actin cytoskeleton reorganization Any process that activates or increases the frequency, rate or extent of actin cytoskeleton reorganization.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P41832 BNI1 Protein BNI1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
10 20 30 40 50 60
MDSSPNKKTY RYPRRSLSLH ARDRVSEARK LEELNLNDGL VAAGLQLVGV ALEKQGTGSH
70 80 90 100 110 120
IYMKQKNFSA NDVSSSPMVS EEVNGSEMDF NPKCMPQDAS LVERMFDELL KDGTFFWGAA
130 140 150 160 170 180
YKNLQNISLR RKWLLICKIR SSNHWGKKKV TSSTTYSTHL ATNELAENAH FLDGLVRNLS
190 200 210 220 230 240
TGGMKLSKAL YKLEKFLRKQ SFLQLFLKDE IYLTTLIEKT LPLISKELQF VYLRCFKILM
250 260 270 280 290 300
NNPLARIRAL HSEPLIRWFT ELLTDQNSNL KCQLLSMELL LLLTYVEGST GCELIWDQLS
310 320 330 340 350 360
ILFTDWLEWF DKILADDIAI HSSLYLNWNQ LKIDYSTTFL LLINSILQGF NNKTALEILN
370 380 390 400 410 420
FLKKNNIHNT ITFLELAYKD DPNSVVIMEQ IKQFKSKESA IFDSMIKTTN DTNSLHPTKD
430 440 450 460 470 480
IARIESEPLC LENCLLLKAK DSPVEAPINE IIQSLWKILD SQKPYSESIK LLKLINSLLF
490 500 510 520 530 540
YLIDSFQVST NPSFDETLES AENVDYVFQD SVNKLLDSLQ SDEIARRAVT EIDDLNAKIS
550 560 570 580 590 600
HLNEKLNLVE NHDKDHLIAK LDESESLISL KTKEIENLKL QLKATKKRLD QITTHQRLYD
610 620 630 640 650 660
QPPSLASSNL SIAGSIIKNN SHGNIIFQNL AKKQQQQQKI SLPKRSTSLL KSKRVTSLSS
670 680 690 700 710 720
YLTDANNENE SQNESEDKSK DSLFQRSTST INFNIPSMKN ITNMQNVSLN SILSELEFSN
730 740 750 760 770 780
SLGTQPNYQS SPVLSSVSSS PKLFPRLSSD SLDNGIQLVP EVVKLPQLPP PPPPPPPPPL
790 800 810 820 830 840
PQSLLTEAEA KPDGVSCIAA PAPPPLPDLF KTKTCGAVPP PPPPPPLPES LSMNKGPSNH
850 860 870 880 890 900
DLVTPPAPPL PNGLLSSSSV SINPTTTDLK PPPTEKRLKQ IHWDKVEDIK DTLWEDTFQR
910 920 930 940 950 960
QETIKELQTD GIFSQIEDIF KMKSPTKIAN KRNAESSIAL SSNNGKSSNE LKKISFLSRD
970 980 990 1000 1010 1020
LAQQFGINLH MFSQLSDMEF VMKVLNCDND IVQNVNILKF FCKEELVNIP KSMLNKYEPY
1030 1040 1050 1060 1070 1080
SQGKDGKAVS DLQRADRIFL ELCINLRFYW NARSKSLLTL STYERDYYDL IFKLQKIDDA
1090 1100 1110 1120 1130 1140
ISHLNRSPKF KSLMFIITEI GNHMNKRIVK GIKLKSLTKL AFVRSSIDQN VSFLHFIEKV
1150 1160 1170 1180 1190 1200
IRIKYPDIYG FVDDLKNIED LGKISLEHVE SECHEFHKKI EDLVTQFQVG KLSKEENLDP
1210 1220 1230 1240 1250 1260
RDQIIKKVKF KINRAKTKSE LLIGQCKLTL IDLNKLMKYY GEDPKDKESK NEFFQPFIEF
1270 1280 1290 1300 1310 1320
LAMFKKCAKE NIEKEEMERV YEQRKSLLDM RTSSNKKSNG SDENDGEKVN RDAVDLLISK
1330 1340 1350 1360 1370
LREVKKDPEP LRRRKSTKLN EIAINVHEGD VKTRKDEDHV LLERTHAMLN DIQNI