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FLASH GENE

Symbol

INF2

contributors: mct/npt/pgu - updated : 01-02-2017

HGNC name	inverted formin, FH2 and WH2 domain containing
HGNC id	23791

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

DNA

TYPE	functioning gene
STRUCTURE	30.01 kb     23 Exon(s)

MAPPING

cloned

Y

linked

N

status

provisional

mode	radiation hybrid

RNA

TRANSCRIPTS	type	messenger

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_001031714 22 - 4668 NP_001026884 - 1240 - 2009 19366733 NM_022489 23 - 4725 NP_071934 - 1249 - 2009 19366733 NM_032714 5 - 1704 NP_116103 - 234 - 2009 19366733

EXPRESSION

Type

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Nervous brain         Homo sapiens Urinary kidney nephron renal capsule     Homo sapiens

cells

System Cell Pubmed Species Stage Rna symbol Nervous Schawnn cell Homo sapiens Urinary podocyte Homo sapiens

cell lineage

cell lines

fluid/secretion

at STAGE

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	an N-terminal diaphanous inhibitory domain (DID), and this DID-containing N terminus of INF2 does not directly bind the Rho GTPase CDC42
	an FH1 domain and a dimeric formin homology 2 (FH2) domain that binds filament barbed ends and is critical for polymerization and depolymerization activities , and the (FH2) domain accelerates actin filament assembly and remains at the barbed end, modulating elongation
	a C-terminal diaphanous autoregulatory domain (DAD)/ WASP homology-2 (WH2) domain, actin monomer-binding, required for depolymerization activity, and also serves as a diaphanous autoregulatory domain (DAD), which binds to the N-terminal diaphanous inhibitory domain (DID) , but do not display barbed end binding abilities , and WH2 domain of INF2 might aid in actin nucleation, in a manner perhaps similar to FMNL3 and other formins

HOMOLOGY

Homologene

FAMILY

diaphanous formin family

CATEGORY

unknown/unspecified

SUBCELLULAR LOCALIZATION	intracellular
	intracellular,cytoplasm,organelle,endoplasmic reticulum

basic FUNCTION	formin protein with the unique biochemical ability to accelerate actin filament depolymerization
	physiologically, INF2 acts in the secretory pathway
	INF2 and stable, detyrosinated microtubules are central players in centrosome reorientation in T cells
	upon TCR triggering the INF2 formin, together with the formins DIAPH1 and FMNL1, promotes the formation of a specialized array of stable detyrosinated MT that breaks the symmetrical organization of the T-cell microtubule (MT) cytoskeleton
	unusual formin protein in that it accelerates both actin polymerization and depolymerization, the latter through an actin filament-severing activity
	important role for the formin INF2 in specifying the function of fibrillar focal adhesions (FAs) through its ability to generate dorsal stress fibers (SFs)
	in addition to the common formin ability to accelerate actin nucleation and elongation, INF2 can also sever filaments and accelerate their depolymerization
	FHOD1 and INF2 are novel components and additional actin-based regulators of podosomes in primary human macrophages
	FHOD1 and INF2 are novel regulators of inter- and intra-structural contractility of podosomes
	encoding a diaphanous formin family protein that regulates actin cytoskeleton dynamics, and cause human focal segmental glomerulosclerosis (FSGS)

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

PATHWAY

metabolism

signaling

a component

INTERACTION

DNA

RNA

small molecule

protein	interacts with the Rho-GTPase CDC42 and myelin and lymphocyte protein (MAL) that are implicated in essential steps of myelination and myelin maintenance
	INF2-induced actin filaments may drive initial mitochondrial constriction, which allows DNM1L-driven secondary constriction
	formin protein with unique biochemical effects on actin
	SPIRE1 cooperates with INF2 to regulate actin assembly at ER-mitochondrial contacts
	SPOP recognizes a Ser/Thr (S/T)-rich motif in the C-terminal region of INF2 and triggers atypical polyubiquitination of INF2
	INF2 is important for SPOP inactivation-induced prostate cancer cell migration and invasion
	interacts with INF2

cell & other

REGULATION

Other

post-translationally modified by a C-terminal farnesyl group, and this modification is required for ER interaction

ASSOCIATED DISORDERS

corresponding disease(s)

FSGS5 , CMTDIE

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS

in mice, normal Inf2 function is not required for glomerular development but normal Inf2 is required for regulation of the actin-based behaviors necessary for response to and/or recovery from injury