Q0GNC1

SS
Gene name
Inf2
Protein name
Inverted formin-2
Names
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:70435
EC number
Protein Class

Descriptions

INF2 is an unusual formin protein that accelerates both actin polymerization and depolymerization. INF2 binds actin monomers through its diaphanous autoregulatory domain (DAD). In a study with human INF2 (Q27J81), DAD is also participate in an autoinhibitory interaction with the N-terminal diaphanous inhibitory domain (DID). Actin monomer binding to the DAD of INF2 competes with the DID/DAD interaction, thereby activating actin polymerization, and mutation of a key DID residue also results in constitutive INF2 activity.

Autoinhibitory domains (AIDs)

1-431 (DID domain) SS

Target domain

589-1032 (FH2 domain)

Relief mechanism

Partner binding

Assay

1033-1051 (DAD domain) SS

Target domain

589-1032 (FH2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q0GNC1

Entry ID Method Resolution Chain Position Source
AF-Q0GNC1-F1 Predicted AlphaFoldDB

No variants for Q0GNC1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0GNC1

No associated diseases with Q0GNC1

4 regional properties for Q0GNC1

Type Name Position InterPro Accession
domain WH2 domain 1007 - 1022 IPR003124
domain Formin, FH3 domain 156 - 343 IPR010472
domain Formin, GTPase-binding domain 1 - 152 IPR010473
domain Formin, FH2 domain 589 - 1032 IPR015425

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, perinuclear region
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

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.

3 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.
regulation of cellular component size A process that modulates the size of a cellular component.
regulation of mitochondrial fission Any process that modulates the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.

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
Q9Y4D1 DAAM1 Disheveled-associated activator of morphogenesis 1 Homo sapiens (Human) EV
Q86T65 DAAM2 Disheveled-associated activator of morphogenesis 2 Homo sapiens (Human) SS
Q27J81 INF2 Inverted formin-2 Homo sapiens (Human) EV
Q80U19 Daam2 Disheveled-associated activator of morphogenesis 2 Mus musculus (Mouse) SS
Q8BPM0 Daam1 Disheveled-associated activator of morphogenesis 1 Mus musculus (Mouse) PR
Q0QWG9 Grid2ip Delphilin 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
MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY SGLRKRLESS
70 80 90 100 110 120
DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CISCVRAVMN SQQGIEYILS
130 140 150 160 170 180
NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL TLDALDHYKM VCSQQYRFSV
190 200 210 220 230 240
IMSELSDSDN VPYVVTLLSV INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD
250 260 270 280 290 300
LLIQLEAFEE AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH
310 320 330 340 350 360
LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP SPLDKAHKSV
370 380 390 400 410 420
QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ SSSVDIAPQP VALEQCITAL
430 440 450 460 470 480
PLPTPPLSSS TPVLPPTPPP LPGPGATSPL PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP
490 500 510 520 530 540
PPLPGSGTIS PPPPPPPPPL PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP
550 560 570 580 590 600
PPPPLPRAGQ IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK
610 620 630 640 650 660
KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE PSAAPARKEP
670 680 690 700 710 720
KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF DVEVLKQLLK LLPEKHEIEN
730 740 750 760 770 780
LRAFTEERAK LSNADQFYVL LLDIPCYPLR VECMMLCEGT AIVLDMVRPK AQLVLTACES
790 800 810 820 830 840
LLTSQRLPVF CQLILKIGNF LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE
850 860 870 880 890 900
VEKSHPDLLQ LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE
910 920 930 940 950 960
RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR DLFTRALKEN
970 980 990 1000 1010 1020
KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ EEVCVIDALL ADIRKGFQLR
1030 1040 1050 1060 1070 1080
KTARGRGDTE ASGRVAPTDP PKATEPATAS NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA
1090 1100 1110 1120 1130 1140
VTPSPQPSKE EDGPPALERR SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE
1150 1160 1170 1180 1190 1200
FSSNKPPGVK SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG
1210 1220 1230 1240 1250 1260
EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP SRNQEEFVPD
1270
SDDIKAKRLC VIQ