Annotations: 1CUN

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1cuna1	All alpha proteins	Spectrin repeat-like	Spectrin repeat	Spectrin repeat	Spectrin alpha chain	chicken (Gallus gallus ) [TaxId: 9031 ],	SCOPe (2.08)
B	d1cunb1	All alpha proteins	Spectrin repeat-like	Spectrin repeat	Spectrin repeat	Spectrin alpha chain	chicken (Gallus gallus ) [TaxId: 9031 ],	SCOPe (2.08)
C	d1cunc1	All alpha proteins	Spectrin repeat-like	Spectrin repeat	Spectrin repeat	Spectrin alpha chain	chicken (Gallus gallus ) [TaxId: 9031 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Spectrin repeat	8042773	3000156	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Spectrin repeat	8042773	3000156	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Spectrin repeat	8042773	3000156	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Spectrin	e1cunA1	A: alpha bundles	X: Spectrin repeat-like	H: Spectrin repeat (From Topology)	T: Spectrin repeat	F: Spectrin	ECOD (1.6)
B	Spectrin	e1cunB1	A: alpha bundles	X: Spectrin repeat-like	H: Spectrin repeat (From Topology)	T: Spectrin repeat	F: Spectrin	ECOD (1.6)
C	Spectrin	e1cunC1	A: alpha bundles	X: Spectrin repeat-like	H: Spectrin repeat (From Topology)	T: Spectrin repeat	F: Spectrin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.58.60	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
B	1.20.58.60	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)
C	1.20.58.60	Mainly Alpha	Up-down Bundle	Methane Monooxygenase Hydroxylase	Chain G, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00435	Spectrin repeat (Spectrin)	Spectrin repeat	Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference [2]. The spectr ...	Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference [2]. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteristic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	PROTEIN (ALPHA SPECTRIN)	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding cytoskeletal protein binding actin binding protein-containing complex binding protein binding actin filament binding calmodulin binding	regulation of cellular process regulation of cellular component size negative regulation of biological process protein-containing complex disassembly regulation of protein-containing complex disassembly actin filament depolymerization regulation of actin filament depolymerization cellular component biogenesis actin filament capping cellular component assembly actin filament-based process negative regulation of supramolecular fiber organization regulation of biological quality negative regulation of actin filament polymerization regulation of cellular process regulation of cellular component size negative regulation of biological process protein-containing complex disassembly regulation of protein-containing complex disassembly actin filament depolymerization regulation of actin filament depolymerization cellular component biogenesis actin filament capping cellular component assembly actin filament-based process negative regulation of supramolecular fiber organization regulation of biological quality negative regulation of actin filament polymerization cellular component disassembly regulation of biological process negative regulation of cellular component organization actin filament organization regulation of organelle organization negative regulation of protein depolymerization negative regulation of protein-containing complex assembly regulation of protein polymerization regulation of supramolecular fiber organization supramolecular fiber organization regulation of cytoskeleton organization regulation of cellular component organization regulation of actin filament-based process cellular component organization 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 cellular component organization or biogenesis regulation of actin filament polymerization actin polymerization or depolymerization protein polymerization regulation of actin filament organization actin cytoskeleton organization actin filament polymerization protein-containing complex organization regulation of protein depolymerization negative regulation of cytoskeleton organization biological regulation regulation of actin polymerization or depolymerization regulation of cellular component biogenesis organelle organization negative regulation of organelle organization regulation of actin filament length regulation of actin cytoskeleton organization cellular process negative regulation of actin filament depolymerization protein depolymerization cytoskeleton organization regulation of anatomical structure size	cell junction cellular anatomical entity intracellular anatomical structure cell cortex cortical cytoskeleton actin cytoskeleton intracellular organelle cell periphery cytoskeleton organelle intracellular non-membrane-bounded organelle cortical actin cytoskeleton cytoplasm non-membrane-bounded organelle cell junction cellular anatomical entity intracellular anatomical structure cell cortex cortical cytoskeleton actin cytoskeleton intracellular organelle cell periphery cytoskeleton organelle intracellular non-membrane-bounded organelle cortical actin cytoskeleton cytoplasm non-membrane-bounded organelle costamere contractile muscle fiber supramolecular fiber myofibril supramolecular polymer supramolecular complex plasma membrane membrane cell projection

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
A, B, C	IPR035825	Alpha Spectrin, SH3 domain	Domain
A, B, C	IPR001452	SH3 domain	Domain
A, B, C	IPR014837	EF-hand, Ca insensitive	Domain
A, B, C	IPR036028	SH3-like domain superfamily	Homologous Superfamily
A, B, C	IPR018159	Spectrin/alpha-actinin	Repeat
A, B, C	IPR002048	EF-hand domain	Domain
A, B, C	IPR011992	EF-hand domain pair	Homologous Superfamily
A, B, C	IPR002017	Spectrin repeat	Repeat

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.