CAPZB_DICDI
ID CAPZB_DICDI Reviewed; 272 AA.
AC P13021; Q55FA3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=F-actin-capping protein subunit beta;
DE AltName: Full=Aginactin subunit beta;
DE AltName: Full=CAP32;
GN Name=acpA; Synonyms=abpE; ORFNames=DDB_G0267374;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2663863; DOI=10.1016/s0021-9258(18)63904-3;
RA Hartmann H., Noegel A.A., Eckerskorn C., Rapp S., Schleicher M.;
RT "Ca2+-independent F-actin capping proteins. Cap 32/34, a capping protein
RT from Dictyostelium discoideum, does not share sequence homologies with
RT known actin-binding proteins.";
RL J. Biol. Chem. 264:12639-12647(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1710551; DOI=10.1002/dvg.1020110508;
RA Hartmann H., Schleicher M., Noegel A.A.;
RT "Heterodimeric capping proteins constitute a highly conserved group of
RT actin-binding proteins.";
RL Dev. Genet. 11:369-376(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP FUNCTION.
RX PubMed=8982279; DOI=10.1016/s0167-4889(96)00108-5;
RA Eddy R.J., Han J., Sauterer R.A., Condeelis J.S.;
RT "A major agonist-regulated capping activity in Dictyostelium is due to the
RT capping protein, cap32/34.";
RL Biochim. Biophys. Acta 1314:247-259(1996).
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. {ECO:0000269|PubMed:8982279}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein beta subunit family.
CC {ECO:0000305}.
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DR EMBL; M25131; AAA33175.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73139.1; -; Genomic_DNA.
DR PIR; A61042; A61042.
DR RefSeq; XP_647630.1; XM_642538.1.
DR PDB; 4AKR; X-ray; 2.20 A; B/D=2-272.
DR PDBsum; 4AKR; -.
DR AlphaFoldDB; P13021; -.
DR SMR; P13021; -.
DR STRING; 44689.DDB0191202; -.
DR PaxDb; P13021; -.
DR PRIDE; P13021; -.
DR EnsemblProtists; EAL73139; EAL73139; DDB_G0267374.
DR GeneID; 8616445; -.
DR KEGG; ddi:DDB_G0267374; -.
DR dictyBase; DDB_G0267374; acpA.
DR eggNOG; KOG3174; Eukaryota.
DR HOGENOM; CLU_045864_1_1_1; -.
DR InParanoid; P13021; -.
DR OMA; MIEDMEI; -.
DR PhylomeDB; P13021; -.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P13021; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008290; C:F-actin capping protein complex; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:dictyBase.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR Gene3D; 1.20.58.570; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR001698; CAPZB.
DR InterPro; IPR043175; CAPZB_N.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR PANTHER; PTHR10619; PTHR10619; 1.
DR Pfam; PF01115; F_actin_cap_B; 1.
DR PRINTS; PR00192; FACTINCAPB.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Reference proteome.
FT CHAIN 1..272
FT /note="F-actin-capping protein subunit beta"
FT /id="PRO_0000204638"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 91..112
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 127..138
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 147..162
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 166..183
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 187..204
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 211..235
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:4AKR"
SQ SEQUENCE 272 AA; 30695 MW; EB2977B607512CF5 CRC64;
MTEKQLSCCL DLMRRLPPSQ IEDNLAGLLD LVPDLTEDLL SSIDQPLKVA YDAVSKKDYL
LCDYNRDADS YRSPWSNKYD PPLSGACYPS SKLRDIEVQA NEIFEIYLNL YFEGGVSSVY
CWDLDDNFAA VVLMKKTQDQ SKKGQPMRGT WDSIHVVEVK LGKKDKAVYK LTSTVMLSIE
TDNDNTGKVN LAGSLTRQDE KEYTFNEVDT HCVNIGKMVE DMESKLRQTL ETIYFGKTKE
VVNTLRNATG NSELEKRKNL SNQIGSAIGN RG
