CAPZB_MESAU
ID CAPZB_MESAU Reviewed; 97 AA.
AC P86209;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=F-actin-capping protein subunit beta {ECO:0000250|UniProtKB:P47756};
DE AltName: Full=CapZ beta {ECO:0000250|UniProtKB:P47756};
DE Flags: Fragments;
GN Name=CAPZB {ECO:0000250|UniProtKB:P47756};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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), WASH (WASHC1, WASH2P,
CC WASH3P, WASH4P, WASH5P or WASH6P), WASHC2 (WASHC2A or WASHC2C), 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
CC {ECO:0000250|UniProtKB:Q5XI32}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P86209; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
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; 3.90.1150.210; -; 1.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR001698; CAPZB.
DR PANTHER; PTHR10619; PTHR10619; 2.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR SUPFAM; SSF90096; SSF90096; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN <1..>97
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000394301"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT NON_CONS 9..10
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 43..44
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 97
SQ SEQUENCE 97 AA; 10833 MW; 581C6DE6604E7B1D CRC64;
RLPPQQIEKS PWSNKYDPPL EDGAMPSARG CWDSIHVVEV QEKSGSGTMN LGGSLTRQME
KDETVSDCSP HIANIGRLVE DMENKIRSTL NEIYFGK
