CAZA1_CHICK
ID CAZA1_CHICK Reviewed; 286 AA.
AC P13127;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=F-actin-capping protein subunit alpha-1;
DE AltName: Full=Beta-actinin subunit I;
DE AltName: Full=CapZ 36/32;
GN Name=CAPZA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Embryo;
RX PubMed=2762296; DOI=10.1073/pnas.86.15.5800;
RA Casella J.F., Casella S.J., Hollands J.A., Caldwell J.E., Cooper J.;
RT "Isolation and characterization of cDNA encoding the alpha subunit of Cap
RT Z(36/32), an actin-capping protein from the Z line of skeletal muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5800-5804(1989).
RN [2]
RP PROTEIN SEQUENCE OF 211-221 AND 231-250.
RC TISSUE=Muscle;
RX PubMed=2341404; DOI=10.1016/s0021-9258(19)38947-1;
RA Maruyama K., Kurokawa H., Oosawa M., Shimaoka S., Yamamoto H., Ito M.,
RA Maruyama K.;
RT "Beta-actinin is equivalent to Cap Z protein.";
RL J. Biol. Chem. 265:8712-8715(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=12660160; DOI=10.1093/emboj/cdg167;
RA Yamashita A., Maeda K., Maeda Y.;
RT "Crystal structure of CapZ: structural basis for actin filament barbed end
RT capping.";
RL EMBO J. 22:1529-1538(2003).
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. {ECO:0000250|UniProtKB:P52907}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC WASH complex (By similarity). {ECO:0000250|UniProtKB:P52907}.
CC -!- INTERACTION:
CC P13127; P14315-1: CAPZB; NbExp=14; IntAct=EBI-1036025, EBI-15845670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line.
CC Note=CapZ is located at the Z line in chicken muscle.
CC -!- TISSUE SPECIFICITY: Present in all tissues examined.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have an internal disulfide bond.
CC {ECO:0000305|PubMed:2762296}.
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DR EMBL; M25534; AAA48657.1; -; mRNA.
DR PIR; A33546; A33546.
DR RefSeq; NP_990846.1; NM_205515.1.
DR PDB; 1IZN; X-ray; 2.10 A; A/C=1-286.
DR PDB; 2KXP; NMR; -; A=7-281.
DR PDB; 2KZ7; NMR; -; A=1-286.
DR PDB; 3AA0; X-ray; 1.70 A; A=1-286.
DR PDB; 3AA1; X-ray; 1.90 A; A=1-286.
DR PDB; 3AA6; X-ray; 1.90 A; A=1-286.
DR PDB; 3AA7; X-ray; 1.90 A; A=1-286.
DR PDB; 3AAA; X-ray; 2.20 A; A=1-286.
DR PDB; 3AAE; X-ray; 3.30 A; A/C/E/G/I=1-286.
DR PDB; 3LK2; X-ray; 2.20 A; A=1-286.
DR PDB; 3LK3; X-ray; 2.68 A; A=1-286.
DR PDB; 3LK4; X-ray; 1.99 A; 1/4/7/A/D/G/J/M/P/S/V/Y=1-286.
DR PDB; 7DS2; X-ray; 1.95 A; A=1-286.
DR PDB; 7DS3; X-ray; 2.09 A; A=1-286.
DR PDB; 7DS4; X-ray; 1.85 A; A=1-286.
DR PDB; 7DS6; X-ray; 1.69 A; A=1-286.
DR PDB; 7DS8; X-ray; 1.95 A; A=1-286.
DR PDB; 7DSA; X-ray; 2.80 A; A=1-286.
DR PDB; 7DSB; X-ray; 2.44 A; A=1-286.
DR PDBsum; 1IZN; -.
DR PDBsum; 2KXP; -.
DR PDBsum; 2KZ7; -.
DR PDBsum; 3AA0; -.
DR PDBsum; 3AA1; -.
DR PDBsum; 3AA6; -.
DR PDBsum; 3AA7; -.
DR PDBsum; 3AAA; -.
DR PDBsum; 3AAE; -.
DR PDBsum; 3LK2; -.
DR PDBsum; 3LK3; -.
DR PDBsum; 3LK4; -.
DR PDBsum; 7DS2; -.
DR PDBsum; 7DS3; -.
DR PDBsum; 7DS4; -.
DR PDBsum; 7DS6; -.
DR PDBsum; 7DS8; -.
DR PDBsum; 7DSA; -.
DR PDBsum; 7DSB; -.
DR AlphaFoldDB; P13127; -.
DR SMR; P13127; -.
DR DIP; DIP-35364N; -.
DR IntAct; P13127; 8.
DR MINT; P13127; -.
DR STRING; 9031.ENSGALP00000002349; -.
DR PaxDb; P13127; -.
DR Ensembl; ENSGALT00000056559; ENSGALP00000056898; ENSGALG00000001547.
DR GeneID; 396521; -.
DR KEGG; gga:396521; -.
DR CTD; 829; -.
DR VEuPathDB; HostDB:geneid_396521; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; P13127; -.
DR OMA; LKVDVHY; -.
DR OrthoDB; 1200844at2759; -.
DR PhylomeDB; P13127; -.
DR Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
DR EvolutionaryTrace; P13127; -.
DR PRO; PR:P13127; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000001547; Expressed in spleen and 14 other tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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:0034329; P:cell junction assembly; ISS:UniProtKB.
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; Actin capping; Actin-binding; Cytoplasm;
KW Direct protein sequencing; Reference proteome.
FT CHAIN 1..286
FT /note="F-actin-capping protein subunit alpha-1"
FT /id="PRO_0000208634"
FT VARIANT 163
FT /note="F -> I"
FT CONFLICT 221
FT /note="D -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="N -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1IZN"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3AA0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1IZN"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3AA6"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3AA0"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 169..180
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 185..198
FT /evidence="ECO:0007829|PDB:7DS6"
FT STRAND 202..217
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 221..252
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:7DS6"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:7DS6"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2KXP"
SQ SEQUENCE 286 AA; 32960 MW; 187E7C51541665DE CRC64;
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
QFTPVKIEGY DDQVLITEHG DLGNGRFLDP RNKISFKFDH LRKEASDPQP EDTESALKQW
RDACDSALRA YVKDHYPNGF CTVYGKSIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
ITPPTAQVAA VLKIQVHYYE DGNVQLVSHK DIQDSVQVSS DVQTAKEFIK IIENAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
