Descriptions

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

36-473 (DID domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q80U19

Entry ID Method Resolution Chain Position Source
AF-Q80U19-F1 Predicted AlphaFoldDB

54 variants for Q80U19

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389382507 2 A>T No EVA
rs3389469092 14 L>I No EVA
rs3389470131 31 H>Q No EVA
rs3389460569 42 I>N No EVA
rs3389463917 68 A>T No EVA
rs3389469069 105 R>C No EVA
rs3389382585 113 Q>P No EVA
rs235945261 150 D>E No EVA
rs3389419251 187 N>K No EVA
rs3389382561 210 T>I No EVA
rs3389465008 215 T>S No EVA
rs3389465035 220 L>M No EVA
rs3389428527 220 L>RDG* No EVA
rs3389382580 222 I>S No EVA
rs3389470174 222 I>V No EVA
rs3389419257 225 A>P No EVA
rs246034793 245 A>V No EVA
rs3389428555 265 G>D No EVA
rs3405945528 306 M>V No EVA
rs3389460563 326 K>Q No EVA
rs3389469094 339 D>N No EVA
rs3389476460 343 A>S No EVA
rs3389463852 391 N>Y No EVA
rs3389382590 407 Q>H No EVA
rs3389470171 450 K>R No EVA
rs3389471163 477 E>V No EVA
rs3389471093 502 G>E No EVA
rs3389485803 505 A>T No EVA
rs3389463861 518 P>S No EVA
rs3389476426 522 P>Q No EVA
rs3389428533 525 P>L No EVA
rs3389485768 531 L>M No EVA
rs3389463887 541 P>A No EVA
rs3389471944 556 P>L No EVA
rs3389428561 616 E>* No EVA
rs3389469085 630 Q>H No EVA
rs3389471965 770 E>D No EVA
rs3389437252 779 E>D No EVA
rs3389460545 814 K>* No EVA
rs3389465002 852 A>V No EVA
rs3389437296 855 N>K No EVA
rs3389448612 892 Y>* No EVA
rs3389470114 894 I>N No EVA
rs3389437278 895 M>K No EVA
rs3389460557 945 Y>F No EVA
rs3389463859 980 N>K No EVA
rs3389428518 1004 E>K No EVA
rs3389448528 1036 R>S No EVA
rs3389481013 1038 R>H No EVA
rs47143619 1054 R>T No EVA
rs46545517 1056 R>K No EVA
rs46025208 1062 G>S No EVA
rs3389471991 1064 L>R No EVA
rs3389485746 1115 Y>C No EVA

No associated diseases with Q80U19

6 regional properties for Q80U19

Type Name Position InterPro Accession
domain Forkhead-associated (FHA) domain 470 - 534 IPR000253
domain Kinesin motor domain 3 - 360 IPR001752
conserved_site Kinesin motor domain, conserved site 246 - 257 IPR019821
domain Kinesin-like KIF1-type 748 - 792 IPR022140
domain Kinesin-like 1222 - 1281 IPR022164
domain Kinesin-associated 391 - 468 IPR032405

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
small GTPase binding Binding to a small monomeric GTPase.

12 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.
determination of left/right symmetry The establishment of an organism's body plan or part of an organism with respect to the left and right halves. The pattern can either be symmetric, such that the halves are mirror images, or asymmetric where the pattern deviates from this symmetry.
dorsal spinal cord development The process whose specific outcome is the progression of the dorsal region of the spinal cord over time, from its formation to the mature structure. The dorsal region of the mature spinal cord contains neurons that process and relay sensory input.
negative regulation of oligodendrocyte differentiation Any process that stops, prevents, or reduces the frequency, rate or extent of oligodendrocyte differentiation.
podocyte cell migration The orderly movement of a podocyte from one site to another, often during the development of a multicellular organism or multicellular structure. A podocyte is a specialized kidney epithelial cell.
positive regulation of canonical Wnt signaling pathway Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
regulation of actin filament polymerization Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament.
regulation of canonical Wnt signaling pathway Any process that modulates the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
regulation of filopodium assembly Any process that modulates the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
regulation of non-canonical Wnt signaling pathway Any process that modulates the frequency, rate or extent of non-canonical Wnt signaling pathway.
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
Q9Y4D1 DAAM1 Disheveled-associated activator of morphogenesis 1 Homo sapiens (Human) EV
Q86T65 DAAM2 Disheveled-associated activator of morphogenesis 2 Homo sapiens (Human) SS
Q0GNC1 Inf2 Inverted formin-2 Mus musculus (Mouse) SS
Q0QWG9 Grid2ip Delphilin Mus musculus (Mouse) PR
Q8BPM0 Daam1 Disheveled-associated activator of morphogenesis 1 Mus musculus (Mouse) PR
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
MALRKRSPHG LGFLCCFGGS DLPEIDLRDS HPLQYLEFSG PIPNPEELNV RFAELVDELD
70 80 90 100 110 120
LTDKNREAVF ALPPEKKWQI YCSKRKEQED PNKLATSWPE YYIDRINAMA AMQNLYETED
130 140 150 160 170 180
EETDKRNQVV EDLKTALRTQ PMRFVTRFID LEGLTCLLNF LRGMDHTTCE SRIHTSLIGC
190 200 210 220 230 240
IKALMNNSQG RAHVLAQPEA ISIIAQSLRT ENSKTKVAVL EILGAVCLVP GGHKKVLQAM
250 260 270 280 290 300
LHYQAYAAER TRFQTLLNEL DRSLGRYRDE VNLKTAIMSF INAVLNAGAG EDNLEFRLHL
310 320 330 340 350 360
RYEFLMLGIQ PVIDKLRQHE NAILDKHLDF FEMVRNEDDL ELARRFDMVH IDTKSASQMF
370 380 390 400 410 420
ELIHKKLKHT EAYPCLLSVL HHCLQMPYKR NGGYFQQWQL LDRILQQIVL QDERGVDPDL
430 440 450 460 470 480
APLENFNVKN IVNMLINENE VKQWRDQAEK FRKEHMELMS RLERKERECE TKTLEKEEMM
490 500 510 520 530 540
RTLNKMKDKL ARESQELRQA RGQVAELVAR HNESSTGPVS SPPPPGGPLT LSSSRTTNDL
550 560 570 580 590 600
PPPPPPLPFD SCPPPPAPPL PPGGPPIPPG APPCFSSGPP PSHDPFSSNE APLRKKRIPQ
610 620 630 640 650 660
PSHPLKSFNW VKLNEERVSG TVWNEIDDSQ VFRILDLEDF EKMFSAYQRH QACMQEGPQR
670 680 690 700 710 720
ERGNVRDGGA ASRPLPAVEA SAHRTEKASR SMVSATGAKK ELGSTEDIYI TSRKVKELSV
730 740 750 760 770 780
IDGRRAQNCI ILLSKLKLSN DEIRQAILRM DEQEDLAKDM LEQLLKFIPE KSDIDLLEEH
790 800 810 820 830 840
KHEIERMARA DRFLYEMSRI DHYQQRLQAL FFKKKFQERL AEAKPKVEAI LLASRELTLS
850 860 870 880 890 900
QRLKQMLEVV LAIGNFMNKG QRGGAYGFRV ASLNKIADTK SSIDRNISLL HYLIMILEKH
910 920 930 940 950 960
FPDILNMPSE LKHLSEAAKV NLAELEKEVS ILRRGLRAVE VELEYQRHQA RDPNDKFVPV
970 980 990 1000 1010 1020
MSDFITVSSF SFSELEDQLN EARDKFAKAL THFGEQESKM QPDEFFGIFD TFLQAFLEAR
1030 1040 1050 1060 1070 1080
QDLEAMRRRK EEDERRARME FMLKEQREKE RWQRQRKVLA GGALEESGEF DDLVSALRSG
1090 1100 1110
EVFDKDLSKF KRNRKRPGSQ VPEVTRERAI NRLNY