CAPZB_MOUSE
ID CAPZB_MOUSE Reviewed; 277 AA.
AC P47757; A2AMV7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=CapZ beta;
GN Name=Capzb; Synonyms=Cappb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=19341723; DOI=10.1016/j.ydbio.2009.03.020;
RA Geyer C.B., Inselman A.L., Sunman J.A., Bornstein S., Handel M.A.,
RA Eddy E.M.;
RT "A missense mutation in the Capza3 gene and disruption of F-actin
RT organization in spermatids of repro32 infertile male mice.";
RL Dev. Biol. 330:142-152(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PROTEIN SEQUENCE OF 79-92 AND 169-181, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Isoform 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. 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. Isoform 2 also is a component of dynactin complex
CC from brain, which contains the actin-related protein ARP1. Interacts
CC with ACTG1. Directly interacts with CRACD; this interaction decreases
CC binding to actin (By similarity). {ECO:0000250|UniProtKB:P47756}.
CC -!- INTERACTION:
CC P47757; Q9ERD7: Tubb3; NbExp=2; IntAct=EBI-299194, EBI-2255594;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000250}. Cytoplasm, myofibril, sarcomere {ECO:0000250}.
CC Note=In cardiac muscle, isoform 1 is located at Z-disks of sarcomeres
CC while isoform 2 is enriched at intercalated disks. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton, perinuclear
CC theca, calyx {ECO:0000250}. Note=Isoform 3 is located to sperm head
CC cytoskeletal structure tightly associated to the nucleus (By
CC similarity). Isoform 3 colocalizes with the alpha subunit in testicular
CC sperm and to the acrosome in elongating and condensing spermatids.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P47757-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47757-2; Sequence=VSP_000768;
CC Name=3; Synonyms=Capzb3;
CC IsoId=P47757-4; Sequence=VSP_046517, VSP_000768;
CC -!- TISSUE SPECIFICITY: Isoform 3 is testis-specific and is present in
CC round spermatids, but not in pachytene spermatocytes or Sertoli cells.
CC {ECO:0000269|PubMed:19341723}.
CC -!- DEVELOPMENTAL STAGE: Isoform 3 is first detected in testis 22 days
CC after birth, coinciding with the first wave of round spermatid
CC development. It is also detected on 30 and 60 days after birth.
CC {ECO:0000269|PubMed:19341723}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; U10406; AAA52226.1; -; mRNA.
DR EMBL; U10407; AAA52227.1; -; mRNA.
DR EMBL; FJ692320; ACN43612.1; -; mRNA.
DR EMBL; AL807811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18841.1; -. [P47757-2]
DR CCDS; CCDS18842.1; -. [P47757-1]
DR CCDS; CCDS71503.1; -. [P47757-4]
DR PIR; B54819; B54819.
DR RefSeq; NP_001032850.1; NM_001037761.2. [P47757-1]
DR RefSeq; NP_001258334.1; NM_001271405.1. [P47757-4]
DR RefSeq; NP_033928.1; NM_009798.4. [P47757-2]
DR PDB; 7PDZ; EM; 3.80 A; E=1-270.
DR PDBsum; 7PDZ; -.
DR AlphaFoldDB; P47757; -.
DR SMR; P47757; -.
DR BioGRID; 198480; 35.
DR DIP; DIP-31383N; -.
DR IntAct; P47757; 9.
DR MINT; P47757; -.
DR STRING; 10090.ENSMUSP00000099565; -.
DR iPTMnet; P47757; -.
DR PhosphoSitePlus; P47757; -.
DR SwissPalm; P47757; -.
DR REPRODUCTION-2DPAGE; P47757; -.
DR UCD-2DPAGE; P47757; -.
DR EPD; P47757; -.
DR jPOST; P47757; -.
DR MaxQB; P47757; -.
DR PaxDb; P47757; -.
DR PeptideAtlas; P47757; -.
DR PRIDE; P47757; -.
DR ProteomicsDB; 279907; -. [P47757-1]
DR ProteomicsDB; 279908; -. [P47757-2]
DR ProteomicsDB; 279909; -. [P47757-4]
DR Antibodypedia; 7956; 295 antibodies from 37 providers.
DR DNASU; 12345; -.
DR Ensembl; ENSMUST00000030518; ENSMUSP00000030518; ENSMUSG00000028745. [P47757-4]
DR Ensembl; ENSMUST00000102507; ENSMUSP00000099565; ENSMUSG00000028745. [P47757-1]
DR Ensembl; ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745. [P47757-2]
DR GeneID; 12345; -.
DR KEGG; mmu:12345; -.
DR UCSC; uc008vlv.2; mouse. [P47757-1]
DR UCSC; uc012dnq.2; mouse. [P47757-4]
DR CTD; 832; -.
DR MGI; MGI:104652; Capzb.
DR VEuPathDB; HostDB:ENSMUSG00000028745; -.
DR eggNOG; KOG3174; Eukaryota.
DR GeneTree; ENSGT00390000017957; -.
DR HOGENOM; CLU_045864_2_0_1; -.
DR InParanoid; P47757; -.
DR OMA; MIEDMEI; -.
DR OrthoDB; 1076134at2759; -.
DR PhylomeDB; P47757; -.
DR TreeFam; TF105732; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 12345; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Capzb; mouse.
DR PRO; PR:P47757; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P47757; protein.
DR Bgee; ENSMUSG00000028745; Expressed in gastrula and 259 other tissues.
DR ExpressionAtlas; P47757; baseline and differential.
DR Genevisible; P47757; MM.
DR GO; GO:0032279; C:asymmetric synapse; IDA:SynGO.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0033150; C:cytoskeletal calyx; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0097224; C:sperm connecting piece; IDA:MGI.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:MGI.
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:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
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 Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT CHAIN 2..277
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000204635"
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:0007744|PubMed:23806337"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47756"
FT VAR_SEQ 1
FT /note="M -> MHPSRRSLPFPLNCQLVRVGTADYGGASEQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19341723"
FT /id="VSP_046517"
FT VAR_SEQ 246..277
FT /note="LDAIPDNHKFKQLQRELSQVLTQRQVYIQPDN -> VQTFADKSKQEALKND
FT LVEALKRKQQC (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:19341723,
FT ECO:0000303|PubMed:7929588"
FT /id="VSP_000768"
SQ SEQUENCE 277 AA; 31345 MW; C4409B1F9E014033 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
NGLRSLDAIP DNHKFKQLQR ELSQVLTQRQ VYIQPDN
