ID   CAPZB_PONAB             Reviewed;         272 AA.
AC   Q5R507;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=F-actin-capping protein subunit beta;
DE   AltName: Full=CapZ beta;
GN   Name=CAPZB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861078; CAH93159.1; ALT_TERM; mRNA.
DR   RefSeq; NP_001127638.1; NM_001134166.1.
DR   AlphaFoldDB; Q5R507; -.
DR   BMRB; Q5R507; -.
DR   SMR; Q5R507; -.
DR   STRING; 9601.ENSPPYP00000002072; -.
DR   Ensembl; ENSPPYT00000044471; ENSPPYP00000040573; ENSPPYG00000001789.
DR   GeneID; 100174717; -.
DR   KEGG; pon:100174717; -.
DR   CTD; 832; -.
DR   eggNOG; KOG3174; Eukaryota.
DR   GeneTree; ENSGT00390000017957; -.
DR   InParanoid; Q5R507; -.
DR   OrthoDB; 1076134at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
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:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
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; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P47756"
FT   CHAIN           2..272
FT                   /note="F-actin-capping protein subunit beta"
FT                   /id="PRO_0000289719"
FT   COILED          210..272
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47756"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47756"
FT   MOD_RES         235
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P47756"
SQ   SEQUENCE   272 AA;  30629 MW;  E6466A68B1254FD0 CRC64;
     MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
     LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
     LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
     KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
     NGLRSVQTFA DKSKQEALKN DLVEALKRKQ QC