CAPZA_DICDI
ID CAPZA_DICDI Reviewed; 281 AA.
AC P13022; Q559U1; Q75JU7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=F-actin-capping protein subunit alpha;
DE AltName: Full=Aginactin subunit alpha;
DE AltName: Full=CAP34;
GN Name=acpB; Synonyms=abpD; ORFNames=DDB_G0272104;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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 [GENOMIC DNA].
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 32-49; 102-115 AND 209-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
RN [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
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 -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; M25132; AAA33176.1; -; Genomic_DNA.
DR EMBL; AAFI02000008; EAL71204.1; -; Genomic_DNA.
DR PIR; B61042; B61042.
DR RefSeq; XP_645243.1; XM_640151.1.
DR PDB; 4AKR; X-ray; 2.20 A; A/C=1-281.
DR PDBsum; 4AKR; -.
DR AlphaFoldDB; P13022; -.
DR SMR; P13022; -.
DR STRING; 44689.DDB0191243; -.
DR PaxDb; P13022; -.
DR EnsemblProtists; EAL71204; EAL71204; DDB_G0272104.
DR GeneID; 8618410; -.
DR KEGG; ddi:DDB_G0272104; -.
DR dictyBase; DDB_G0272104; acpB.
DR eggNOG; KOG0836; Eukaryota.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; P13022; -.
DR OMA; HVHYYED; -.
DR PhylomeDB; P13022; -.
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:P13022; -.
DR Proteomes; UP000002195; Chromosome 2.
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; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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; Direct protein sequencing;
KW Reference proteome.
FT CHAIN 1..281
FT /note="F-actin-capping protein subunit alpha"
FT /id="PRO_0000208638"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 37..43
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 145..158
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 163..175
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 179..194
FT /evidence="ECO:0007829|PDB:4AKR"
FT STRAND 196..213
FT /evidence="ECO:0007829|PDB:4AKR"
FT HELIX 217..248
FT /evidence="ECO:0007829|PDB:4AKR"
FT TURN 249..254
FT /evidence="ECO:0007829|PDB:4AKR"
SQ SEQUENCE 281 AA; 31163 MW; 488C23AF378FC2F7 CRC64;
MASNQELVQI ATNFLLNAPP CEFMEVVSDV RALLPSESLL NASAGSTFRE YNTSQMVSVQ
TSKGSALITK EGEISNNEYL DPKNKQVITY DHIKQEVTGE RSASGEIEQD IEQYRAAFDE
EATKYCNEYY PNGVSAVYGT KVSEGIKITV CISTCIYKPN AFYSGRWRSV WTCTFKPGSG
NVTSNGKVQV NVHYFEDGNV QLNTVTQKQT TSPSADAQST AVNAFKAIGK AELNLHTALD
NNYSTMGDTT FKALRRALPI NRTKINWQKV KNFKIANELN K
