ID   ACTB_DICDI              Reviewed;         295 AA.
AC   P24005; Q54XA5;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Calcium-regulated actin-bundling protein;
DE   AltName: Full=34 kDa actin-binding protein;
GN   Name=abpB; ORFNames=DDB_G0279081;
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 PROTEIN SEQUENCE OF 7-22 AND 225-237.
RX   PubMed=1993662; DOI=10.1016/s0021-9258(18)49930-9;
RA   Fechheimer M., Murdock D., Carney M., Glover C.V.C.;
RT   "Isolation and sequencing of cDNA clones encoding the Dictyostelium
RT   discoideum 30,000-dalton actin-bundling protein.";
RL   J. Biol. Chem. 266:2883-2889(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=8922380; DOI=10.1083/jcb.135.4.965;
RA   Rivero F., Furukawa R., Noegel A.A., Fechheimer M.;
RT   "Dictyostelium discoideum cells lacking the 34,000-dalton actin-binding
RT   protein can grow, locomote, and develop, but exhibit defects in regulation
RT   of cell structure and movement: a case of partial redundancy.";
RL   J. Cell Biol. 135:965-980(1996).
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   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: May contribute to the structure and reorganization of
CC       filopodia and pseudopodia accompanying cell movements.
CC   -!- SUBUNIT: Monomer.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M58022; AAA33144.1; -; mRNA.
DR   EMBL; Z50156; CAA90518.1; -; Genomic_DNA.
DR   EMBL; U32112; AAB48216.1; -; Genomic_DNA.
DR   EMBL; AAFI02000027; EAL67879.1; -; Genomic_DNA.
DR   PIR; A23750; A23750.
DR   RefSeq; XP_641862.1; XM_636770.1.
DR   PDB; 4X3N; X-ray; 1.89 A; A/B/C=1-295.
DR   PDBsum; 4X3N; -.
DR   AlphaFoldDB; P24005; -.
DR   SMR; P24005; -.
DR   PaxDb; P24005; -.
DR   EnsemblProtists; EAL67879; EAL67879; DDB_G0279081.
DR   GeneID; 8621868; -.
DR   KEGG; ddi:DDB_G0279081; -.
DR   dictyBase; DDB_G0279081; abpB.
DR   eggNOG; ENOG502S8KW; Eukaryota.
DR   HOGENOM; CLU_931956_0_0_1; -.
DR   InParanoid; P24005; -.
DR   OMA; KVDVNFD; -.
DR   PRO; PR:P24005; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0031941; C:filamentous actin; IDA:dictyBase.
DR   GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR   GO; GO:0061836; C:intranuclear rod; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR   GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR   GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR   GO; GO:0051764; P:actin crosslink formation; IDA:dictyBase.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR   GO; GO:0030046; P:parallel actin filament bundle assembly; IDA:dictyBase.
DR   DisProt; DP02687; -.
DR   InterPro; IPR040810; F_actin_bund_C.
DR   Pfam; PF18060; F_actin_bund_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Calcium; Direct protein sequencing;
KW   Reference proteome.
FT   CHAIN           1..295
FT                   /note="Calcium-regulated actin-bundling protein"
FT                   /id="PRO_0000073833"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           61..66
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           96..111
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           116..121
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           153..160
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           167..174
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           181..211
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   TURN            214..217
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           220..227
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           232..255
FT                   /evidence="ECO:0007829|PDB:4X3N"
FT   HELIX           273..290
FT                   /evidence="ECO:0007829|PDB:4X3N"
SQ   SEQUENCE   295 AA;  33353 MW;  1BBF85DEA657097D CRC64;
     MAETKVAPNL TGIEQTKAGQ SFTEKLSAEA MEFFCNVAKL PFSQQAVHFL NAYWAEVSKE
     AEFIYSVGWE TIKYADMHCK GIQLVFKYDE GNDLDFDIAL YFYEQLCKFC EDPKNKNYAT
     TYPISQPQML TALKRKQELR EKVDVNFDGR VSFLEYLLYQ YKDFANPADF CTRSMNHDEH
     PEIKKARLAL EEVNKRIRAY EEEKARLTEE SKIPGVKGLG ATNMLAQIDS GPLKEQLNFA
     LISAEAAVRT ASKKYGGAAY SGGAGDAGAG SSAGAIWWMN RDLEEKKKRY GPQKK