4K17

Crystal Structure of mouse CARMIL residues 1-668

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF07560	e4k17A1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: EUF07560	ECOD (1.6)
A	LRR_8_4	e4k17A2	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Leucine-rich repeats (From Topology)	T: Leucine-rich repeats	F: LRR_8_4	ECOD (1.6)
B	EUF07560	e4k17B4	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: EUF07560	ECOD (1.6)
B	LRR_8_4	e4k17B3	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Leucine-rich repeats (From Topology)	T: Leucine-rich repeats	F: LRR_8_4	ECOD (1.6)
C	EUF07560	e4k17C6	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: EUF07560	ECOD (1.6)
C	LRR_8_4	e4k17C5	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Leucine-rich repeats (From Topology)	T: Leucine-rich repeats	F: LRR_8_4	ECOD (1.6)
D	EUF07560	e4k17D1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: EUF07560	ECOD (1.6)
D	LRR_8_4	e4k17D2	A: beta duplicates or obligate multimers	X: Single-stranded right-handed beta-helix	H: Leucine-rich repeats (From Topology)	T: Leucine-rich repeats	F: LRR_8_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
A	6.10.140.1850	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
A	3.80.10.10	Alpha Beta	Alpha-Beta Horseshoe	Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)	Ribonuclease Inhibitor	CATH (4.3.0)
B	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
B	6.10.140.1850	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
B	3.80.10.10	Alpha Beta	Alpha-Beta Horseshoe	Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)	Ribonuclease Inhibitor	CATH (4.3.0)
C	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
C	6.10.140.1850	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
C	3.80.10.10	Alpha Beta	Alpha-Beta Horseshoe	Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)	Ribonuclease Inhibitor	CATH (4.3.0)
D	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)
D	6.10.140.1850	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)
D	3.80.10.10	Alpha Beta	Alpha-Beta Horseshoe	Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)	Ribonuclease Inhibitor	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13516	Leucine Rich repeat (LRR_6)	Leucine Rich repeat	-	Repeat
A, B, C, D	PF17888	Carmil pleckstrin homology domain (Carm_PH)	Carmil pleckstrin homology domain	This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and ...	This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6 . Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Leucine-rich repeat-containing protein 16A	protein-containing complex binding binding	lamellipodium assembly plasma membrane bounded cell projection organization cell projection organization plasma membrane bounded cell projection assembly cellular component organization cellular component biogenesis cellular component assembly lamellipodium organization cellular process cellular component organization or biogenesis cell projection assembly positive regulation of substrate adhesion-dependent cell spreading regulation of biological process regulation of cellular process lamellipodium assembly plasma membrane bounded cell projection organization cell projection organization plasma membrane bounded cell projection assembly cellular component organization cellular component biogenesis cellular component assembly lamellipodium organization cellular process cellular component organization or biogenesis cell projection assembly positive regulation of substrate adhesion-dependent cell spreading regulation of biological process regulation of cellular process regulation of cell-substrate adhesion positive regulation of cell adhesion regulation of substrate adhesion-dependent cell spreading regulation of cell adhesion biological regulation positive regulation of biological process cell-substrate adhesion cell adhesion positive regulation of cell-substrate adhesion substrate adhesion-dependent cell spreading positive regulation of cellular process cell migration cell motility positive regulation of organelle organization regulation of cytoskeleton organization regulation of cellular component organization positive regulation of cellular component organization regulation of actin filament-based process regulation of cellular component size protein-containing complex disassembly positive regulation of actin filament depolymerization regulation of protein-containing complex disassembly actin filament depolymerization regulation of actin filament depolymerization actin filament-based process regulation of biological quality positive regulation of protein-containing complex disassembly cellular component disassembly actin polymerization or depolymerization regulation of actin filament organization actin cytoskeleton organization protein-containing complex organization regulation of protein depolymerization positive regulation of protein depolymerization positive regulation of cytoskeleton organization actin filament organization regulation of actin polymerization or depolymerization positive regulation of supramolecular fiber organization actin filament uncapping regulation of organelle organization barbed-end actin filament uncapping organelle organization regulation of actin filament length regulation of actin cytoskeleton organization regulation of supramolecular fiber organization supramolecular fiber organization protein depolymerization cytoskeleton organization regulation of anatomical structure size negative regulation of biological process actin filament capping positive regulation of protein polymerization negative regulation of supramolecular fiber organization negative regulation of actin filament polymerization barbed-end actin filament capping negative regulation of cellular component organization negative regulation of barbed-end actin filament capping negative regulation of protein depolymerization negative regulation of protein-containing complex assembly regulation of protein polymerization regulation of barbed-end actin filament capping regulation of protein-containing complex assembly positive regulation of protein-containing complex assembly negative regulation of protein-containing complex disassembly negative regulation of cellular process protein-containing complex assembly negative regulation of protein polymerization regulation of actin filament polymerization protein polymerization actin filament polymerization negative regulation of cytoskeleton organization positive regulation of cellular component biogenesis regulation of cellular component biogenesis negative regulation of organelle organization negative regulation of actin filament depolymerization positive regulation of actin filament polymerization establishment or maintenance of cell polarity positive regulation of locomotion regulation of cell motility positive regulation of cell migration regulation of locomotion positive regulation of cell motility regulation of cell migration locomotion ruffle organization localization import into cell macropinocytosis transport pinocytosis endocytosis establishment of localization vesicle-mediated transport actin filament network formation organonitrogen compound metabolic process small molecule metabolic process metabolic process urate metabolic process purine-containing compound metabolic process regulation of Arp2/3 complex-mediated actin nucleation regulation of actin nucleation Arp2/3 complex-mediated actin nucleation actin nucleation regulation of cell projection organization positive regulation of lamellipodium organization regulation of lamellipodium organization positive regulation of cell projection organization regulation of plasma membrane bounded cell projection organization regulation of actin filament bundle assembly positive regulation of actin filament bundle assembly actin filament bundle organization positive regulation of stress fiber assembly stress fiber assembly actomyosin structure organization regulation of stress fiber assembly contractile actin filament bundle assembly regulation of actomyosin structure organization actin filament bundle assembly	cell projection cell leading edge cellular anatomical entity plasma membrane bounded cell projection lamellipodium membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck nuclear body intracellular organelle cell projection cell leading edge cellular anatomical entity plasma membrane bounded cell projection lamellipodium membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear speck nuclear body intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen cytoplasm cytosol cell periphery plasma membrane membrane endosome intracellular vesicle macropinosome endomembrane system cytoplasmic vesicle vesicle pinosome polymeric cytoskeletal fiber protein-containing complex actin filament actin cytoskeleton filamentous actin cytoskeleton intracellular non-membrane-bounded organelle supramolecular fiber supramolecular polymer supramolecular complex non-membrane-bounded organelle intermediate filament cytoskeleton

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR031943	CARMIL, C-terminal domain	Domain
A, B, C, D	IPR041245	CARMIL, pleckstrin homology domain	Domain
A, B, C, D	IPR011993	PH-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR001611	Leucine-rich repeat	Repeat
A, B, C, D	IPR032675	Leucine-rich repeat domain superfamily	Homologous Superfamily
A, B, C, D	IPR051279	Protein Phosphatase 1 Regulatory and Actin Interaction Protein	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.