CAPZB_PIG
ID CAPZB_PIG Reviewed; 277 AA.
AC A0PFK7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=CapZ beta;
GN Name=CAPZB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Glenz M.H., Hinssen H.;
RT "Actin binding activities of individual CapZ-subunit isoforms and their
RT interaction with smooth muscle a-actinin.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. Plays a role in the regulation of cell morphology and
CC cytoskeletal organization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC ARHGAP17 and RCSD1/CAPZIP. Component of the WASH complex, composed of
CC F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-
CC actin-capping protein subunit beta (CAPZB), WASHC1, WASHC2, WASHC3,
CC WASHC4 and WASHC5. Interacts with ACTG1. Directly interacts with CRACD;
CC this interaction decreases binding to actin (By similarity).
CC {ECO:0000250|UniProtKB:P47756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AM410996; CAL69437.1; -; mRNA.
DR RefSeq; NP_001090925.1; NM_001097456.1.
DR AlphaFoldDB; A0PFK7; -.
DR SMR; A0PFK7; -.
DR STRING; 9823.ENSSSCP00000003793; -.
DR PaxDb; A0PFK7; -.
DR PeptideAtlas; A0PFK7; -.
DR PRIDE; A0PFK7; -.
DR eggNOG; KOG3174; Eukaryota.
DR InParanoid; A0PFK7; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
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: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 2: Evidence at transcript level;
KW Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..277
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000280482"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
SQ SEQUENCE 277 AA; 31315 MW; 08D55B195900803C CRC64;
MGDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
NGLRSLDAIP DNHKFKQLQR ELSQVLTQRQ VYIQPDN