ID   CAZA3_RAT               Reviewed;         299 AA.
AC   Q9WUV6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=F-actin-capping protein subunit alpha-3;
DE   AltName: Full=CapZ alpha-3;
GN   Name=Capza3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9406198;
RX   DOI=10.1002/(sici)1098-2795(199801)49:1<81::aid-mrd9>3.0.co;2-k;
RA   Hurst S., Howes E.A., Coadwell J., Jones R.;
RT   "Expression of a testis-specific putative actin-capping protein associated
RT   with the developing acrosome during rat spermiogenesis.";
RL   Mol. Reprod. Dev. 49:81-91(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-290, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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.
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   -!- TISSUE SPECIFICITY: Exclusively expressed in the testis.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; Y12538; CAA73137.1; -; mRNA.
DR   AlphaFoldDB; Q9WUV6; -.
DR   SMR; Q9WUV6; -.
DR   STRING; 10116.ENSRNOP00000011555; -.
DR   iPTMnet; Q9WUV6; -.
DR   PaxDb; Q9WUV6; -.
DR   PRIDE; Q9WUV6; -.
DR   UCSC; RGD:2271; rat.
DR   RGD; 2271; Capza3.
DR   eggNOG; KOG0836; Eukaryota.
DR   InParanoid; Q9WUV6; -.
DR   PhylomeDB; Q9WUV6; -.
DR   Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR   Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q9WUV6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR   GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; IEP:RGD.
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   1: Evidence at protein 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_0000208633"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   299 AA;  35007 MW;  3D753088BCF79BE5 CRC64;
     MSLSVLSRQD KEKVIHRLLI QAPPGEFVNA FDDLCLLIRD EKLMHHQGEC AGHQHCQKYC
     VPLCIDGNPV LLSHHNVMGD FRFFDYQSKL SFRFDLLQNQ LRDIQSHGII RNENEYLRSV
     VMCALKLYVN DHYPNGNCNV LRKTVKNKEF LIACIEKHSY DNGECWNGLW KSKWIFQVNP
     FLTQVTGRIF VQAHYFRCVN LHVEVSKDLK ESLEVVNQAQ LALSFARLVE EQENKFQAAV
     IEELQELSNE ALRKILRRDL PVTRTLIDWQ RILSDLNLVM YPKLGYVIYS RSVLCNWII