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

174-696 (GBD/FH3 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

4 structures for P41832

Entry ID Method Resolution Chain Position Source
1UX4 X-ray 330 A A/B 1352-1765 PDB
1UX5 X-ray 250 A A 1350-1760 PDB
1Y64 X-ray 305 A B 1327-1769 PDB
AF-P41832-F1 Predicted AlphaFoldDB

40 variants for P41832

Variant ID(s) Position Change Description Diseaes Association Provenance
s14-135053 111 S>F No SGRP
s14-134936 150 S>L No SGRP
s14-134871 172 Y>H No SGRP
s14-134682 235 T>A No SGRP
s14-134514 291 V>I No SGRP
s14-134508 293 T>A No SGRP
s14-134238 383 A>T No SGRP
s14-134188 399 L>F No SGRP
s14-133723 554 M>I No SGRP
s14-133596 597 V>I No SGRP
s14-133049 779 A>V No SGRP
s14-132930 819 G>S No SGRP
s14-132926 820 T>S No SGRP
s14-132647 913 N>S No SGRP
s14-132375 1004 E>K No SGRP
s14-132298 1029 D>E No SGRP
s14-132264 1041 E>K No SGRP
s14-132251 1045 E>G No SGRP
s14-132252 1045 E>K No SGRP
s14-131976 1137 S>P No SGRP
s14-131913 1158 Y>H No SGRP
s14-131841 1182 A>T No SGRP
s14-131820 1189 D>Y No SGRP
s14-131795 1197 G>E No SGRP
s14-131783 1201 R>P No SGRP
s14-131763 1208 D>N No SGRP
s14-131736 1217 S>G No SGRP
s14-131676 1237 S>T No SGRP
s14-131669 1239 P>L No SGRP
s14-131596 1263 K>N No SGRP
s14-131588 1266 D>G No SGRP
s14-131553 1278 P>T No SGRP
s14-131439 1316 T>A No SGRP
s14-131439 1316 T>S No SGRP
s14-131237 1383 A>V No SGRP
s14-131043 1448 I>V No SGRP
s14-130983 1468 S>P No SGRP
s14-130902 1495 E>K No SGRP
s14-130096 1763 I>M No SGRP
s14-129801 1862 T>A No SGRP

No associated diseases with P41832

4 regional properties for P41832

Type Name Position InterPro Accession
domain Formin, GTPase-binding domain 173 - 459 IPR010473
domain Diaphanous autoregulatory (DAD) domain 1792 - 1826 IPR014767
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 174 - 696 IPR014768
domain Formin, FH2 domain 1348 - 1824 IPR015425

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane
  • Cell projection, ruffle membrane
  • Cytoplasm, cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

9 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.
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.
cellular bud tip The end of a cellular bud distal to the site of attachment to the mother cell.
incipient cellular bud site The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence.
mating projection tip The apex of the mating projection in unicellular fungi exposed to mating pheromone; site of polarized growth.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
polarisome Protein complex that plays a role in determining cell polarity by directing the localized assembly of actin filaments at polarization sites; in Saccharomyces the polarisome includes Bni1p, Spa2p, Pea2p, and Bud6p.
prospore membrane The prospore membrane is a double-membraned structure that extends from the cytoplasmic face of the spindle pole bodies to encompass the spindle pole bodies and the four nuclear lobes that are formed during meiosis. It helps isolate the meiotic nuclei from the cytoplasm during spore formation and serves as a foundation for the formation of the spore walls. An example of this component is found in Schizosaccharomyces pombe.

4 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
identical protein binding Binding to an identical protein or proteins.
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.

9 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.
budding cell apical bud growth Growth at the tip of a bud, in a cell that reproduces by budding.
establishment of mitotic spindle orientation A cell cycle process that sets the alignment of mitotic spindle relative to other cellular structures.
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.
regulation of protein localization Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P40450 BNR1 BNI1-related protein 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
10 20 30 40 50 60
MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ HSPVGNEVST
70 80 90 100 110 120
SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM NGKLSGDVPV SSQHARSHSM
130 140 150 160 170 180
QSKYSYSKRN SSQASNKLTR QHTGQSHSAS SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY
190 200 210 220 230 240
EVEVLFEDIM YKRNIFQSLS EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA
250 260 270 280 290 300
SRTSMASDHH PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK
310 320 330 340 350 360
LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL TSDEMKDLWV
370 380 390 400 410 420
TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT KELLEKENSF FKCFRVLSML
430 440 450 460 470 480
SQGLYEFSTH RLMTDTVAEG LFSTKLATRK MATEIFVCML EKKNKSRFEA VLTSLDKKFR
490 500 510 520 530 540
IGQNLHMIQN FKKMPQYFSH LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG
550 560 570 580 590 600
GGENAILEYC QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ
610 620 630 640 650 660
IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL VSLVQHLFLS
670 680 690 700 710 720
SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM NMAIQRLYDA MQTDEVARRA
730 740 750 760 770 780
ILESRALTKK LEEIQAERDS LSEKLSKAEH GLVGQLEDEL HERDRILAKN QRVMQQLEAE
790 800 810 820 830 840
LEELKKKHLL EKHQQEVELR KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ
850 860 870 880 890 900
DGLSRAKKDY KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP
910 920 930 940 950 960
IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF NVEERVNELF
970 980 990 1000 1010 1020
NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD VETEEDANYA SLDPKTYQKK
1030 1040 1050 1060 1070 1080
LDEINRITDQ LLDIQTQTEH EIQVEEDGES DLSSSSSDDE SEEIYQDASP TQELRSEHSE
1090 1100 1110 1120 1130 1140
LSSGSGPGSF LDALSQKYGT GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS
1150 1160 1170 1180 1190 1200
SAPYLEELTQ KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG
1210 1220 1230 1240 1250 1260
RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP AKLFGESLEK
1270 1280 1290 1300 1310 1320
EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG ETPPPPPLPS VLSSSTDGVI
1330 1340 1350 1360 1370 1380
PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE
1390 1400 1410 1420 1430 1440
KFADDLYEKG VLADLEKAFA AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS
1450 1460 1470 1480 1490 1500
VADLVKKILN CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP
1510 1520 1530 1540 1550 1560
EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR KVDKAVSALQ
1570 1580 1590 1600 1610 1620
ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI KDTTNSMTFL NYVEKIVRLN
1630 1640 1650 1660 1670 1680
YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV
1690 1700 1710 1720 1730 1740
LIKTLPVLPE ARKKGDLLED EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY
1750 1760 1770 1780 1790 1800
KKAQAQNLAA EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV
1810 1820 1830 1840 1850 1860
MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG SILYSPEAMD
1870 1880 1890 1900 1910 1920
PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE EISDRARMLL KELRGSDTPV
1930 1940 1950
KQNSILDEHL EKLRARKERS IGEASTGNRL SFK