Q76LL6

SS
Gene name
Fhod3 (Fhos2, Kiaa1695)
Protein name
FH1/FH2 domain-containing protein 3
Names
Formin homolog overexpressed in spleen 2, mFHOS2
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:225288
EC number
Protein Class

Descriptions

Formin-family proteins, in the active state, form actinbased structures such as stress fibres. Formin homology domain protein 3 (Fhod3) is a major endothelial formin. In a study with human FHOD1, FHOD1 was normally autoinhibited by intramolecular interaction between the N-terminal domain and C-terminal DAD domain. Since other formin proteins contain a DID domain at N-terminus, Fhod3 may also contain a DID domain and this DID domain may interact with the DAD domain.

Autoinhibitory domains (AIDs)

1515-1547 (DAD domain) SS

Target domain

1039-1492 (FH2 domains)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q76LL6

Entry ID Method Resolution Chain Position Source
AF-Q76LL6-F1 Predicted AlphaFoldDB

24 variants for Q76LL6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs864270611 29 P>S No Ensembl
rs222710271 307 T>A No Ensembl
rs257948418 336 S>R No Ensembl
rs31449439 446 D>N No Ensembl
rs242165232 456 T>S No Ensembl
rs217310322 469 A>T No Ensembl
rs1134191775 474 R>W No Ensembl
rs234264092 503 R>G No Ensembl
rs31449437 506 T>K No Ensembl
rs223896486 523 S>T No Ensembl
rs29670988 575 Y>S No Ensembl
rs250647385 687 A>V No Ensembl
rs13483257 690 S>P No Ensembl
rs220986620 735 A>V No Ensembl
rs250072667 742 I>V No Ensembl
rs31446013 813 W>C No Ensembl
rs30077504 856 G>S No Ensembl
rs238602330 858 P>S No Ensembl
rs249779471 927 Q>H No Ensembl
rs212022043 933 T>I No Ensembl
rs215640666 984 A>T No Ensembl
rs245396529 1009 S>I No Ensembl
rs234334871 1378 S>A No Ensembl
rs218624184 1479 A>V No Ensembl

No associated diseases with Q76LL6

3 regional properties for Q76LL6

Type Name Position InterPro Accession
domain PDZ domain 14 - 94 IPR001478-1
domain PDZ domain 154 - 234 IPR001478-2
domain EBP50, C-terminal 235 - 358 IPR015098

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cytoplasm, myofibril, sarcomere, Z line
  • Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
striated muscle thin filament Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils.
Z disc Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

1 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.

5 GO annotations of biological process

Name Definition
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.
cardiac myofibril assembly The process whose specific outcome is the progression of the cardiac myofibril over time, from its formation to the mature structure. A cardiac myofibril is a myofibril specific to cardiac muscle cells.
cortical 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 actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane.
negative regulation of actin filament polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
sarcomere organization The myofibril assembly process that results in the organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9Y613 FHOD1 FH1/FH2 domain-containing protein 1 Homo sapiens (Human) EV
Q2V2M9 FHOD3 FH1/FH2 domain-containing protein 3 Homo sapiens (Human) SS
Q6P9Q4 Fhod1 FH1/FH2 domain-containing protein 1 Mus musculus (Mouse) SS
10 20 30 40 50 60
MATLACRVQF LDDTDPFNST NFPEPSRPPL FTFREDLALG TQLAGVHRLL RAPHKLDDCT
70 80 90 100 110 120
LQLSHNGAYL DLEATLAEQR DELEGFQDDT GRGKKNSIIL RTQLSVRVHA CIEKLYNSSG
130 140 150 160 170 180
RDLRRALFSL KQIFQDDKDL VHEFVIAEGL TCLIKVGAEA DQNYQNYILR ALGQIMLYVD
190 200 210 220 230 240
GMNGVINHSE TIQWLYTLVG SKFRLVVKTA LKLLLVFVEY SESNAPLLIQ AVSAVDTKRG
250 260 270 280 290 300
VKPWSNIMEI LEEKDGVDTE LLVYAMTLVN KTLAGLPDQD TFYDVVDCLE ELGIAAVSQR
310 320 330 340 350 360
HLNKKGTDLD LLEQFNIYEV ALRHEDGDET AEPPPSGHRD RRRASMCSGG TVGEQQGLDR
370 380 390 400 410 420
RRSRRHSIQN IKSPLSAPTS PCSPSVPAFK PSQVRDLCEK DEEEEEEEEQ PITEPNSEEE
430 440 450 460 470 480
REDDAQCQGK DSKASSASGQ SSPGKDAAPE SSALHTTSSP TSQGRWLSAS TAARSPVLGG
490 500 510 520 530 540
TSGPEASRPA ARLLPPSPGL ATRPSTAPKV SPTIDKLPYV PHSPFHLFSY DFEDSPLLTK
550 560 570 580 590 600
DKGGDSQTEN RYSNFSSNSF QSSRPSPGPS GSPSYASSFS SPQDTRSSPS GLLTSSFRQH
610 620 630 640 650 660
QESLAAERER RRQEREERLQ RIEREERNKF NREYLDKREE QRQARGERYK YLEQLAAETQ
670 680 690 700 710 720
EKEPRSQSVS RGRADLSLDL SLPAAPAPPS PSSQSPSADS QEALPVPSSP PTLQCPQVSG
730 740 750 760 770 780
KDHEPELEAE AGQGADEASQ DIASAHRGAE SQEEPVLELE PEERASLSEK ERQNEEVNER
790 800 810 820 830 840
DNCSASSISS SSSTLEREEK EDKLSEDRAT GLWSTSLQDV GVNGQCGDIL TSKRFMLDML
850 860 870 880 890 900
YAHNRKSTED EEKDDGEPGR SAQEVEAVAS LATRISTLQA NSQAPEESIK RVDIGCLDNR
910 920 930 940 950 960
GSVKAFAEKF NSGEVGRGAI SPDVESQDKV PDTPPAQLKT ESDYIWDQLM ANPRELRIQD
970 980 990 1000 1010 1020
MDFTDLGEED DIDVLDVDLG HREAPGPPPP PPPTFLGLPP PPPPPLLDSV PPPPVPGNLL
1030 1040 1050 1060 1070 1080
ASPVFNTPQG LGWSQVPRGQ PAFTKKKKTI RLFWNEVRPF EWPSKNNRRC REFLWSKLEP
1090 1100 1110 1120 1130 1140
IKVDTSRLEH LFESKSKELS VTKKTAADGK RQEIIVLDSK RSNAINIGLT VLPPPRTIKI
1150 1160 1170 1180 1190 1200
AILNFDEYAL NKEGIEKILT MIPTEEEKQK IQEAQLANPE VPLGSAEQFL LTLSSISELS
1210 1220 1230 1240 1250 1260
ARLHLWAFKM DYETTEKEVA EPLLDLKEGI DQLENNKTLG FILSTLLAIG NFLNGTNAKA
1270 1280 1290 1300 1310 1320
FELSYLEKVP EVKDTVHKQS LLHHVCTMVV ENFPDSSDLY SEIGAITRSA KVDFDQLQDN
1330 1340 1350 1360 1370 1380
LCQMERRCKA SWDHLKAIAK HEMKPVLKQR MSEFLKDCAE RIIILKIVHR RIINRFHSFL
1390 1400 1410 1420 1430 1440
LFMGHPPYAI REVNINKFCR IISEFALEYR TTRERVLQQK QKRANHRERN KTRGKMITDS
1450 1460 1470 1480 1490 1500
GKFSGSSPAA PSQPQGLSYA EDAAEHENMK AVLKTSSPAL EDATPVLGVR TRSRASRGST
1510 1520 1530 1540 1550 1560
SSWTMGTEES PSVTDDAADE IMDRIVKSAT QVPSQRVVPR ERKRSRANRK SLRRTLKSGL
1570
TPEEARALGL VGTSELQL