Descriptions

(Annotation from UniProt)
The DAD domain may regulate activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition may be released upon competitive binding of an activated GTPase. The release of DAD may allow the FH2 domain to nucleate and elongate nonbranched actin filaments.

Autoinhibitory domains (AIDs)

Target domain

23-469 (GBD/FH3 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A2APV2

Entry ID Method Resolution Chain Position Source
AF-A2APV2-F1 Predicted AlphaFoldDB

4 variants for A2APV2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs13476502 158 M>V No Ensembl
rs241895132 547 T>I No Ensembl
rs1133603072 805 I>V No Ensembl
rs227442452 1080 V>M No Ensembl

No associated diseases with A2APV2

4 regional properties for A2APV2

Type Name Position InterPro Accession
domain Formin, FH3 domain 278 - 482 IPR010472
domain Formin, GTPase-binding domain 23 - 275 IPR010473
domain Rho GTPase-binding/formin homology 3 (GBD/FH3) domain 23 - 469 IPR014768
domain Formin, FH2 domain 615 - 1052 IPR015425

Functions

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

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

2 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.
small GTPase binding Binding to a small monomeric GTPase.

5 GO annotations of biological process

Name Definition
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
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.
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.
regulation of cell morphogenesis Any process that modulates the frequency, rate or extent of cell morphogenesis. Cell morphogenesis is the developmental process in which the shape of a cell is generated and organized.
regulation of cell shape Any process that modulates the surface configuration of a cell.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VUC6 Frl Formin-like protein Drosophila melanogaster (Fruit fly) EV
O95466 FMNL1 Formin-like protein 1 Homo sapiens (Human) SS
Q8IVF7 FMNL3 Formin-like protein 3 Homo sapiens (Human) SS
Q96PY5 FMNL2 Formin-like protein 2 Homo sapiens (Human) SS
Q6ZPF4 Fmnl3 Formin-like protein 3 Mus musculus (Mouse) SS
Q9JL26 Fmnl1 Formin-like protein 1 Mus musculus (Mouse) SS
10 20 30 40 50 60
MGNAGSMDSQ QTDFKAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK
70 80 90 100 110 120
WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG
130 140 150 160 170 180
WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTMES TVDKSKPWSR SIEDLHRGSN
190 200 210 220 230 240
LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM
250 260 270 280 290 300
VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF
310 320 330 340 350 360
EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE
370 380 390 400 410 420
SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI
430 440 450 460 470 480
VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT
490 500 510 520 530 540
IKIQKKGDGD IAILPVMASG TLSTGSELAV GNYVGSVPGA TTSGPSVPPP PPLPPSSDTS
550 560 570 580 590 600
EAAQNGTASP PMSPPPPPPP PPPPPPPPPP PLPGPAAETS PAPPLPPPPP PSAPPLPGTS
610 620 630 640 650 660
SPTVVFNSGL AAVKIKKPIK TKFRMPVFNW VALKPNQING TVFNEIDDER ILEDLNVDEF
670 680 690 700 710 720
EEIFKTKAQG PAIDLSSSKQ KITQKASSKV TLLEANRAKN LAITLRKAGK SADEICKAIH
730 740 750 760 770 780
VFDLKTLPVD FVECLMRFLP TENEVKVLRL YERERKPLEN LSDEDRFMMQ FSKIERLLQK
790 800 810 820 830 840
MTIMAFIGNF TESIQMLTPQ LHAIIAASVS IKSSQKLKKI LEIILALGNY MNSSKRGAVY
850 860 870 880 890 900
GFKLQSLDLL LDTKSTDRKQ TLLHYISNVV KEKYQQVTLF YNELHYVEKA AAVSLENVLL
910 920 930 940 950 960
DVKELQRGMD LTKREYTMHD HNTLLKEFLL HNEGKLKKLQ EDAKIAQDAF DDVVKYFGEN
970 980 990 1000 1010 1020
PKTTPPSVFF PVFVRFVKAY KQAEEENELR KKQEQALMEK LLEQEALMEQ QDAKSPSHKS
1030 1040 1050 1060 1070 1080
KRQQQELIAE LRRRQVKDNR HVYEGKDGAI EDIITALKKN NITKFPNVHS RVRISSSTPV
VEDTQS