ID   CAZA2_RAT               Reviewed;         286 AA.
AC   Q3T1K5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=F-actin-capping protein subunit alpha-2;
DE   AltName: Full=CapZ alpha-2;
GN   Name=Capza2;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-15; 38-47 AND 122-129, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fibroblast;
RA   Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL   Submitted (JUN-2009) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 20-37 AND 194-210, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   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 (By 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. Interacts with
CC       RCSD1/CAPZIP (By similarity). Directly interacts with CRACD; this
CC       interaction decreases binding to actin (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P47755}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; DP000027; AAR16310.1; -; Genomic_DNA.
DR   EMBL; BC101867; AAI01868.1; -; mRNA.
DR   RefSeq; NP_001009180.1; NM_001009180.2.
DR   PDB; 2KBM; NMR; -; X/Y=265-276.
DR   PDBsum; 2KBM; -.
DR   AlphaFoldDB; Q3T1K5; -.
DR   BMRB; Q3T1K5; -.
DR   SMR; Q3T1K5; -.
DR   BioGRID; 268810; 4.
DR   IntAct; Q3T1K5; 3.
DR   MINT; Q3T1K5; -.
DR   STRING; 10116.ENSRNOP00000037217; -.
DR   iPTMnet; Q3T1K5; -.
DR   PhosphoSitePlus; Q3T1K5; -.
DR   jPOST; Q3T1K5; -.
DR   PaxDb; Q3T1K5; -.
DR   PRIDE; Q3T1K5; -.
DR   GeneID; 493810; -.
DR   KEGG; rno:493810; -.
DR   UCSC; RGD:1549770; rat.
DR   CTD; 830; -.
DR   RGD; 1549770; Capza2.
DR   VEuPathDB; HostDB:ENSRNOG00000056207; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   HOGENOM; CLU_045161_0_0_1; -.
DR   InParanoid; Q3T1K5; -.
DR   OMA; HVHYYED; -.
DR   OrthoDB; 1085166at2759; -.
DR   PhylomeDB; Q3T1K5; -.
DR   TreeFam; TF314822; -.
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   Reactome; R-RNO-879415; Advanced glycosylation endproduct receptor signaling.
DR   Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR   EvolutionaryTrace; Q3T1K5; -.
DR   PRO; PR:Q3T1K5; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000056207; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; Q3T1K5; RN.
DR   GO; GO:0005903; C:brush border; ISO:RGD.
DR   GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR   GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
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   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   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..286
FT                   /note="F-actin-capping protein subunit alpha-2"
FT                   /id="PRO_0000288478"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   HELIX           271..275
FT                   /evidence="ECO:0007829|PDB:2KBM"
SQ   SEQUENCE   286 AA;  32967 MW;  E706A9BC1830E70B CRC64;
     MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
     QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAIESW
     RTSVETALRA YVKEHYPNGV CTVYGKKVDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
     VTPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA