Descriptions

(Annotation based on sequence homology with Q9Y4D1)
Diaphanous-related formins (DRFs), such as DAAM1 and mDia1, play central roles in actin dynamics through assembling linear actin filaments. The amino-terminal diaphanous inhibitory domain (DID) and the carboxyl-terminal diaphanous autoinhibitory domain (DAD) segment form an intramolecular interaction to restrain the actin assembly activity of FH1-FH2 domains. This autoinhibition is disrupted by Rho GTPase that is able to bind to the GTPase-binding domain (GBD) near DID domain.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8BPM0

Entry ID Method Resolution Chain Position Source
AF-Q8BPM0-F1 Predicted AlphaFoldDB

55 variants for Q8BPM0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389256936 25 E>Q No EVA
rs3389235914 31 R>K No EVA
rs3389175881 38 L>F No EVA
rs260374501 44 A>S No EVA
rs3389241040 60 L>F No EVA
rs3389242376 61 V>G No EVA
rs3389217110 91 K>E No EVA
rs3389238955 111 N>S No EVA
rs3389245053 118 S>T No EVA
rs3389246263 128 E>G No EVA
rs3389250778 150 T>I No EVA
rs3389228613 151 R>I No EVA
rs3389246270 157 G>D No EVA
rs3389250807 183 G>S No EVA
rs3403337313 211 S>T No EVA
rs3389211957 220 K>E No EVA
rs3389246259 252 S>R No EVA
rs3389245085 258 Q>L No EVA
rs3389235965 267 S>G No EVA
rs3389211958 295 V>M No EVA
rs3402715007 306 Y>F No EVA
rs3389216994 329 D>E No EVA
rs3389228639 352 L>P No EVA
rs3389256953 366 L>P No EVA
rs3389241084 367 T>I No EVA
rs3389256970 407 R>I No EVA
rs3389228629 425 T>R No EVA
rs3389256943 426 P>S No EVA
rs3403544003 439 L>* No EVA
rs3403739745 443 N>K No EVA
rs3389246287 475 A>D No EVA
rs3413020086 499 T>S No EVA
rs243128087 499 T>S No EVA
rs233739441 519 N>T No EVA
rs3389253101 525 A>V No EVA
rs1132285838 531 P>H No EVA
rs243116423 586 V>I No EVA
rs3389238982 718 E>V No EVA
rs3389202403 724 K>E No EVA
rs3389250788 727 L>F No EVA
rs3389241077 729 Q>* No EVA
rs3389245029 738 S>G No EVA
rs3389175885 806 S>T No EVA
rs216336487 807 R>C No EVA
rs216336487 807 R>S No EVA
rs3389212038 844 D>G No EVA
rs3389235863 851 K>M No EVA
rs238528567 864 E>D No EVA
rs3389253113 876 E>D No EVA
rs3389246257 909 L>R No EVA
rs3389175856 934 A>D No EVA
rs219571919 958 H>R No EVA
rs46112424 1019 V>M No EVA
rs3389228604 1037 S>P No EVA
rs3389228616 1050 S>* No EVA

No associated diseases with Q8BPM0

5 regional properties for Q8BPM0

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 184 - 192 IPR000629
domain Helicase, C-terminal 249 - 410 IPR001650
domain DEAD/DEAH box helicase domain 62 - 223 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 56 - 253 IPR014001
domain RNA helicase, DEAD-box type, Q motif 37 - 65 IPR014014

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton, cilium basal body
  • Perinuclear
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
ciliary basal body A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
motile cilium A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
stress fiber A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.

3 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.
small GTPase binding Binding to a small monomeric GTPase.

2 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
Wnt signaling pathway The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A0A1D5P556 DAAM2 Disheveled-associated activator of morphogenesis 2 Gallus gallus (Chicken) SS
O95466 FMNL1 Formin-like protein 1 Homo sapiens (Human) SS
Q27J81 INF2 Inverted formin-2 Homo sapiens (Human) EV
Q86T65 DAAM2 Disheveled-associated activator of morphogenesis 2 Homo sapiens (Human) SS
Q9Y4D1 DAAM1 Disheveled-associated activator of morphogenesis 1 Homo sapiens (Human) EV
Q0GNC1 Inf2 Inverted formin-2 Mus musculus (Mouse) SS
Q0QWG9 Grid2ip Delphilin Mus musculus (Mouse) PR
Q80U19 Daam2 Disheveled-associated activator of morphogenesis 2 Mus musculus (Mouse) SS
Q9C7S1 FH12 Formin-like protein 12 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LH02 FH17 Formin-like protein 17 Arabidopsis thaliana (Mouse-ear cress) PR
P0C5K4 FH21A Putative formin-like protein 21a Arabidopsis thaliana (Mouse-ear cress) PR
Q9FF14 FH19 Formin-like protein 19 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAPRKRGGRG ISFIFCCFRN NDHPEITYRL RNDSNFALQT MEPALPMPPV EELDVMFSEL
70 80 90 100 110 120
VDELDLTDKH REAMFALPAE KKWQIYCSKK KDQEENKGAT SWPEFYIDQL NSMAARKSLL
130 140 150 160 170 180
ALEKEEEEER SKTIESLKTA LRTKPMRFVT RFIDLDGLSC ILNFLKTMDY ETSESRIHTS
190 200 210 220 230 240
LIGCIKALMN NSQGRAHVLA HSESINVIAQ SLSTENIKTK VAVLEILGAV CLVPGGHKKV
250 260 270 280 290 300
LQAMLHYQKY ASERTRFQTL INDLDKSTGR YRDEVSLKTA IMSFINAVLS QGAGVESLDF
310 320 330 340 350 360
RLHLRYEFLM LGIQPVIDKL REHENSTLDR HLDFFEMLRN EDELEFAKRF ELVHIDTKSA
370 380 390 400 410 420
TQMFELTRRR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ
430 440 450 460 470 480
DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK
490 500 510 520 530 540
EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELNR RAVCAAVPGG PSPGAPGGPF
550 560 570 580 590 600
PSSGLGSLLP PPPPPLLSGG ALPPPPPPLP PGGPPPPPGP PPLGGVLPPP GAPVSLTLKK
610 620 630 640 650 660
KNIPQPTNAL KSFNWSKLPE NKLDGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQEFFV
670 680 690 700 710 720
NNSKQKEADA IDDTLSSKLK VKELSVIDGR RAQNCNILLS RLKLSNDEIK RAILTMDEQE
730 740 750 760 770 780
DLPKDMLEQL LKFVPEKSDI DLLEEHKHEL DRMAKADRFL FEMSRINHYQ QRLQSLYFKK
790 800 810 820 830 840
KFAERVAEVK PKVEAIRSGS EEVFRSRALK QLLEVVLAFG NYMNKGQRGN AYGFKISSLN
850 860 870 880 890 900
KIADTKSSID KNITLLHYLI TIVENKYPKV LNLSEELRDI PQAAKVNMTE LDKEISTLRS
910 920 930 940 950 960
GLKAVETELE YQKSQPPQPG DKFVSVVSQF ITLASFSFSD VEDLLAEAKE LFTKAVKHFG
970 980 990 1000 1010 1020
EEAGKIQPDE FFGIFDQFLQ AVAEAKQENE NMRKRKEEEE RRARLEAQLK EQRERERKVR
1030 1040 1050 1060 1070
KAKESSEESG EFDDLVSALR SGEVFDKDLS KLKRNRKRIS NQVTDSSRER PITKLNF