CAPZB_BOVIN
ID CAPZB_BOVIN Reviewed; 301 AA.
AC P79136; Q3T012;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=CapZ beta;
GN Name=CAPZB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2 AND BETA-3), AND
RP CHARACTERIZATION.
RC TISSUE=Sperm;
RX PubMed=9184090; DOI=10.1006/excr.1997.3564;
RA von Buelow M., Rackwitz H.-R., Zimbelmann R., Franke W.W.;
RT "CP beta3, a novel isoform of an actin-binding protein, is a component of
RT the cytoskeletal calyx of the mammalian sperm head.";
RL Exp. Cell Res. 233:216-224(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-3).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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. The isoform beta-3 may play a role in spermatogenesis.
CC Alternatively, may play a role in later maturation steps such as
CC capacitation and fertilization which involve changes of membrane
CC domains. May play a role in the regulation of cell morphology and
CC cytoskeletal organization.
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 -!- INTERACTION:
CC P79136; Q3T0F7: MTPN; NbExp=2; IntAct=EBI-2128126, EBI-2128107;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca,
CC calyx. Note=Sperm head cytoskeletal structure tightly associated to the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Beta-3;
CC IsoId=P79136-1; Sequence=Displayed;
CC Name=Beta-1;
CC IsoId=P79136-3; Sequence=Not described;
CC Name=Beta-2;
CC IsoId=P79136-2; Sequence=VSP_000766;
CC -!- TISSUE SPECIFICITY: The isoform beta-3 is predominantly expressed in
CC the testis. It is only detected in total sperm, sperm heads and the
CC calyx fraction, but not in sperm tails or any supernatant fraction.
CC Weaker expression also found in brain.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; Z85980; CAB06626.1; -; mRNA.
DR EMBL; Y10372; CAA71401.1; -; mRNA.
DR EMBL; BC102613; AAI02614.1; -; mRNA.
DR RefSeq; NP_788821.1; NM_176648.4. [P79136-1]
DR AlphaFoldDB; P79136; -.
DR BMRB; P79136; -.
DR SMR; P79136; -.
DR CORUM; P79136; -.
DR IntAct; P79136; 3.
DR MINT; P79136; -.
DR STRING; 9913.ENSBTAP00000005983; -.
DR PaxDb; P79136; -.
DR PeptideAtlas; P79136; -.
DR PRIDE; P79136; -.
DR GeneID; 338052; -.
DR KEGG; bta:338052; -.
DR CTD; 832; -.
DR eggNOG; KOG3174; Eukaryota.
DR HOGENOM; CLU_045864_1_1_1; -.
DR InParanoid; P79136; -.
DR OrthoDB; 1076134at2759; -.
DR TreeFam; TF105732; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0033150; C:cytoskeletal calyx; IEA:UniProtKB-SubCell.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..301
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000204633"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT VAR_SEQ 1..30
FT /note="MHPCRRSLPFPLNCQLVKVGTADYGGASDQ -> M (in isoform
FT Beta-2)"
FT /evidence="ECO:0000303|PubMed:9184090"
FT /id="VSP_000766"
SQ SEQUENCE 301 AA; 33741 MW; E4029F1A53614719 CRC64;
MHPCRRSLPF PLNCQLVKVG TADYGGASDQ SDQQLDCALD LMRRLPPQQI EKNLSDLIDL
VPSLCEDLLS SVDQPLKIAR DKVVGKDYLL CDYNRDGDSY RSPWSNKYDP PLEDGAMPSA
RLRKLEVEAN NAFDQYRDLY FEGGVSSVYL WDLDHGFAGV ILIKKAGDGS KKIKGCWDSI
HVVEVQEKSS GRTAHYKLTS TVMLWLQTNK SGSGTMNLGG SLTRQMEKDE TVSDCSPHIA
NIGRLVEDME NKIRSTLNEI YFGKTKDIVN GLRSVQTFAD KSKQEALKND LVEALKRKQQ
C
