ID   CAZA1_MOUSE             Reviewed;         286 AA.
AC   P47753; Q91YN7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=F-actin-capping protein subunit alpha-1;
DE   AltName: Full=CapZ alpha-1;
GN   Name=Capza1; Synonyms=Cappa1;
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 [LARGE SCALE MRNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
RC   TISSUE=Muscle;
RX   PubMed=9331217;
RX   DOI=10.1002/(sici)1097-0169(1997)38:2<120::aid-cm2>3.0.co;2-b;
RA   Hart M.C., Korshunova Y.O., Cooper J.A.;
RT   "Vertebrates have conserved capping protein alpha isoforms with specific
RT   expression patterns.";
RL   Cell Motil. Cytoskeleton 38:120-132(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 194-210.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, 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. May play a role in the formation of epithelial cell
CC       junctions (By similarity). Forms, with CAPZB, the barbed end of the
CC       fast growing ends of actin filaments in the dynactin complex and
CC       stabilizes dynactin structure. The dynactin multiprotein complex
CC       activates the molecular motor dynein for ultra-processive transport
CC       along microtubules (By similarity). {ECO:0000250|UniProtKB:A0PFK5,
CC       ECO:0000250|UniProtKB:P52907}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Subunit of
CC       dynactin, a multiprotein complex part of a tripartite complex with
CC       dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin
CC       complex is built around ACTR1A/ACTB filament and consists of an actin-
CC       related filament composed of a shoulder domain, a pointed end and a
CC       barbed end. Its length is defined by its flexible shoulder domain. The
CC       soulder is composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. The 4
CC       DCNT2 (via N-terminus) bind the ACTR1A filament and act as molecular
CC       rulers to determine the length. The pointed end is important for
CC       binding dynein-dynactin cargo adapters. Consists of 4 subunits: ACTR10,
CC       DCNT4, DCTN5 and DCTN6. The barbed end is composed of a CAPZA1:CAPZB
CC       heterodimers, which binds ACTR1A/ACTB filament and dynactin and
CC       stabilizes dynactin (By similarity). Component of the WASH complex,
CC       composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or
CC       CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASHC1,
CC       WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), WASHC2 (WASHC2A or WASHC2C),
CC       WASHC3, WASHC4 and WASHC5. Interacts with S100A (By similarity).
CC       Interacts with S100B. Interacts with SH3BP1; recruits CAPZA1 to forming
CC       cell junctions. Interacts with CD2AP. Directly interacts with CRACD;
CC       this interaction decreases binding to actin (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:A0PFK5,
CC       ECO:0000250|UniProtKB:P52907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:A0PFK5}.
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; BC016232; AAH16232.1; -; mRNA.
DR   EMBL; U16740; AAC00566.1; -; mRNA.
DR   CCDS; CCDS38580.1; -.
DR   PDB; 7CCC; X-ray; 3.20 A; C=1-286.
DR   PDB; 7PDZ; EM; 3.80 A; F=1-286.
DR   PDBsum; 7CCC; -.
DR   PDBsum; 7PDZ; -.
DR   AlphaFoldDB; P47753; -.
DR   BMRB; P47753; -.
DR   EMDB; EMD-13343; -.
DR   SMR; P47753; -.
DR   BioGRID; 198477; 56.
DR   IntAct; P47753; 26.
DR   MINT; P47753; -.
DR   STRING; 10090.ENSMUSP00000102381; -.
DR   iPTMnet; P47753; -.
DR   PhosphoSitePlus; P47753; -.
DR   SwissPalm; P47753; -.
DR   REPRODUCTION-2DPAGE; P47753; -.
DR   EPD; P47753; -.
DR   jPOST; P47753; -.
DR   MaxQB; P47753; -.
DR   PaxDb; 10090-ENSMUSP00000102381; -.
DR   PeptideAtlas; P47753; -.
DR   ProteomicsDB; 265675; -.
DR   Pumba; P47753; -.
DR   AGR; MGI:106227; -.
DR   MGI; MGI:106227; Capza1.
DR   eggNOG; KOG0836; Eukaryota.
DR   InParanoid; P47753; -.
DR   PhylomeDB; P47753; -.
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-879415; Advanced glycosylation endproduct receptor signaling.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 12340; 5 hits in 76 CRISPR screens.
DR   ChiTaRS; Capza1; mouse.
DR   PRO; PR:P47753; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P47753; Protein.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0008290; C:F-actin capping protein complex; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IDA:MGI.
DR   GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB.
DR   Gene3D; 3.30.1140.60; F-actin capping protein, alpha subunit; 1.
DR   Gene3D; 3.90.1150.210; F-actin capping protein, beta subunit; 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; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10653:SF5; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-1; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 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; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   CHAIN           2..286
FT                   /note="F-actin-capping protein subunit alpha-1"
FT                   /id="PRO_0000208625"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52907"
FT   CONFLICT        222
FT                   /note="V -> I (in Ref. 2; AAC00566)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..22
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           29..40
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           43..49
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           118..135
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          139..148
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          151..164
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   TURN            165..168
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          169..180
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          186..198
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   STRAND          200..216
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           221..252
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           254..258
FT                   /evidence="ECO:0007829|PDB:7CCC"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:7CCC"
SQ   SEQUENCE   286 AA;  32940 MW;  6FE97BCE5D9B9D3A CRC64;
     MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
     QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNQISFKFDH LRKEASDPQP EDVDGGLKSW
     RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
     ITPPSAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EVQTTKEFIK IIESAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//