CAZA3_MACFA
ID CAZA3_MACFA Reviewed; 299 AA.
AC Q4R7M8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=F-actin-capping protein subunit alpha-3;
DE AltName: Full=CapZ alpha-3;
GN Name=CAPZA3; ORFNames=QtsA-14785;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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. May play a role in the morphogenesis of spermatid (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC WASH complex, composed of F-actin-capping protein subunit alpha
CC (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta
CC (CAPZB), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AB168787; BAE00894.1; -; mRNA.
DR RefSeq; NP_001270709.1; NM_001283780.1.
DR AlphaFoldDB; Q4R7M8; -.
DR SMR; Q4R7M8; -.
DR STRING; 9541.XP_005570327.1; -.
DR Ensembl; ENSMFAT00000059101; ENSMFAP00000012573; ENSMFAG00000025207.
DR GeneID; 101926750; -.
DR CTD; 93661; -.
DR VEuPathDB; HostDB:ENSMFAG00000025207; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR OMA; VMGDFRF; -.
DR OrthoDB; 1085166at2759; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000025207; Expressed in multicellular organism.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR Gene3D; 3.30.1140.60; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR042489; CapZ_alpha_1.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..299
FT /note="F-actin-capping protein subunit alpha-3"
FT /id="PRO_0000295860"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUV6"
SQ SEQUENCE 299 AA; 35056 MW; 16A3EFF904CC857B CRC64;
MTLSVLSRKD KERVIRRLLL QAPPGEFVNA FDDLCLLIRD EKLMHHQGEC AGHQHCQKYS
VPLCIDGNPV LLSHHNVMGD YRFFDHQSKL SFRYDLLQNQ LKDIQSHGII RNETEYLRVV
VLCALKLYVN DHYPKGNCNV LRKTVKSKEY LIACIEDHNY ETGECWNGLW KSKWIFQVNP
FLTQVTGRIF VQAHFFRCVN LHIEISKDLK ESLEIVNQAQ LALSFARLVE EQENKFQAAV
LEELQELSNE ALRKILRRDL PVTRTLIDWQ RILSDLNLVM YPKLGYVIYS RSVLCNWII