CAPZB_CHICK
ID CAPZB_CHICK Reviewed; 277 AA.
AC P14315;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=F-actin-capping protein subunit beta isoforms 1 and 2;
DE AltName: Full=Beta-actinin subunit II;
DE AltName: Full=CapZ 36/32;
DE AltName: Full=CapZ B1 and B2;
GN Name=CAPZB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2745461; DOI=10.1016/s0021-9258(18)63905-5;
RA Caldwell J.E., Waddle J.A., Cooper J.A., Hollands J.A., Casella S.J.,
RA Casella J.F.;
RT "cDNAs encoding the beta subunit of cap Z, the actin-capping protein of the
RT Z line of muscle.";
RL J. Biol. Chem. 264:12648-12652(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=7929588; DOI=10.1083/jcb.127.2.453;
RA Schafer D.A., Korshunova Y.O., Schroer T.A., Cooper J.A.;
RT "Differential localization and sequence analysis of capping protein beta-
RT subunit isoforms of vertebrates.";
RL J. Cell Biol. 127:453-465(1994).
RN [3]
RP PROTEIN SEQUENCE OF 160-168 AND 182-198.
RC TISSUE=Muscle;
RX PubMed=2341404; DOI=10.1016/s0021-9258(19)38947-1;
RA Maruyama K., Kurokawa H., Oosawa M., Shimaoka S., Yamamoto H., Ito M.,
RA Maruyama K.;
RT "Beta-actinin is equivalent to Cap Z protein.";
RL J. Biol. Chem. 265:8712-8715(1990).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. May play a role in the regulation of cell morphology
CC and cytoskeletal organization.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC WASH complex (By similarity). Isoform 2 also is a component of dynactin
CC complex from brain, which contains the actin-related protein ARP1.
CC {ECO:0000250, ECO:0000269|PubMed:7929588}.
CC -!- INTERACTION:
CC P14315-1; P13127: CAPZA1; NbExp=14; IntAct=EBI-15845670, EBI-1036025;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000269|PubMed:7929588}. Note=In cardiac muscle, isoform 1 is
CC located at Z-disks of sarcomeres. {ECO:0000269|PubMed:7929588}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, myofibril, sarcomere, I
CC band {ECO:0000269|PubMed:7929588}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5XI32}. Note=In cardiac muscle, isoform 2 is
CC located at sarcomere intercalated disks. {ECO:0000269|PubMed:7929588}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Beta-1;
CC IsoId=P14315-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-2;
CC IsoId=P14315-2; Sequence=VSP_000769;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in pectoral muscle, cardiac
CC muscle and gizzard. Isoform 2 is detected in brain and liver (at
CC protein level). Isoform 2 is the predominant isoform of nonmuscle
CC tissues and isoform 1 is the predominant isoform of muscle tissues.
CC {ECO:0000269|PubMed:7929588}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; J04959; AAA49144.1; -; mRNA.
DR EMBL; U07826; AAA52222.1; -; mRNA.
DR PIR; A34335; A34335.
DR PIR; A54819; A54819.
DR RefSeq; NP_001167000.1; NM_001173529.1. [P14315-2]
DR RefSeq; NP_990768.1; NM_205437.2. [P14315-1]
DR RefSeq; XP_015152321.1; XM_015296835.1. [P14315-1]
DR PDB; 1IZN; X-ray; 2.10 A; B/D=1-277.
DR PDB; 2KXP; NMR; -; B=2-271.
DR PDB; 2KZ7; NMR; -; B=1-277.
DR PDB; 3AA0; X-ray; 1.70 A; B=1-244.
DR PDB; 3AA1; X-ray; 1.90 A; B=1-244.
DR PDB; 3AA6; X-ray; 1.90 A; B=1-244.
DR PDB; 3AA7; X-ray; 1.90 A; B=1-244.
DR PDB; 3AAA; X-ray; 2.20 A; B=1-277.
DR PDB; 3AAE; X-ray; 3.30 A; B/D/F/H/J=1-277.
DR PDB; 3LK2; X-ray; 2.20 A; B=1-243.
DR PDB; 3LK3; X-ray; 2.68 A; B=1-277.
DR PDB; 3LK4; X-ray; 1.99 A; 2/5/8/B/E/H/K/N/Q/T/W/Z=1-277.
DR PDB; 7DS2; X-ray; 1.95 A; B=1-244.
DR PDB; 7DS3; X-ray; 2.09 A; B=1-244.
DR PDB; 7DS4; X-ray; 1.85 A; B=1-244.
DR PDB; 7DS6; X-ray; 1.69 A; B=1-244.
DR PDB; 7DS8; X-ray; 1.95 A; B=1-244.
DR PDB; 7DSA; X-ray; 2.80 A; B=1-244.
DR PDB; 7DSB; X-ray; 2.44 A; B=1-244.
DR PDBsum; 1IZN; -.
DR PDBsum; 2KXP; -.
DR PDBsum; 2KZ7; -.
DR PDBsum; 3AA0; -.
DR PDBsum; 3AA1; -.
DR PDBsum; 3AA6; -.
DR PDBsum; 3AA7; -.
DR PDBsum; 3AAA; -.
DR PDBsum; 3AAE; -.
DR PDBsum; 3LK2; -.
DR PDBsum; 3LK3; -.
DR PDBsum; 3LK4; -.
DR PDBsum; 7DS2; -.
DR PDBsum; 7DS3; -.
DR PDBsum; 7DS4; -.
DR PDBsum; 7DS6; -.
DR PDBsum; 7DS8; -.
DR PDBsum; 7DSA; -.
DR PDBsum; 7DSB; -.
DR AlphaFoldDB; P14315; -.
DR SMR; P14315; -.
DR BioGRID; 676667; 1.
DR DIP; DIP-35365N; -.
DR IntAct; P14315; 3.
DR MINT; P14315; -.
DR STRING; 9031.ENSGALP00000006415; -.
DR PaxDb; P14315; -.
DR Ensembl; ENSGALT00000006424; ENSGALP00000006414; ENSGALG00000004034. [P14315-2]
DR Ensembl; ENSGALT00000006425; ENSGALP00000006415; ENSGALG00000004034. [P14315-1]
DR Ensembl; ENSGALT00000061238; ENSGALP00000049427; ENSGALG00000004034. [P14315-1]
DR GeneID; 396418; -.
DR KEGG; gga:396418; -.
DR CTD; 832; -.
DR VEuPathDB; HostDB:geneid_396418; -.
DR eggNOG; KOG3174; Eukaryota.
DR GeneTree; ENSGT00390000017957; -.
DR HOGENOM; CLU_045864_2_0_1; -.
DR InParanoid; P14315; -.
DR OMA; MIEDMEI; -.
DR OrthoDB; 1076134at2759; -.
DR PhylomeDB; P14315; -.
DR Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-9013405; RHOD GTPase cycle.
DR Reactome; R-GGA-9035034; RHOF GTPase cycle.
DR Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR EvolutionaryTrace; P14315; -.
DR PRO; PR:P14315; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000004034; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; P14315; baseline and differential.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0097224; C:sperm connecting piece; IEA:Ensembl.
DR GO; GO:0071203; C:WASH complex; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:Ensembl.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR Gene3D; 1.20.58.570; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR001698; CAPZB.
DR InterPro; IPR043175; CAPZB_N.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..277
FT /note="F-actin-capping protein subunit beta isoforms 1 and
FT 2"
FT /id="PRO_0000204636"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 246..277
FT /note="IDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN -> VQTFADKSKQEALKND
FT LVEALKRKQQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7929588"
FT /id="VSP_000769"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 91..112
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 145..158
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 162..178
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3AA0"
FT STRAND 186..202
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 209..233
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:1IZN"
SQ SEQUENCE 277 AA; 31364 MW; 55E5271EDA5454D6 CRC64;
MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
KTGSGTMNLG GSLTRQMEKD ETVSDSSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
NGLRSIDAIP DNQKYKQLQR ELSQVLTQRQ IYIQPDN
