ACBP_DICDI
ID ACBP_DICDI Reviewed; 84 AA.
AC Q5FXM5; Q55D10;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acyl-CoA-binding protein;
DE Short=ACBP;
DE Contains:
DE RecName: Full=SDF-2;
GN Name=acbA; ORFNames=DDB_G0270658;
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], FUNCTION, DEVELOPMENTAL STAGE, SYNTHESIS
RP OF 18-52; 18-31 AND 32-52, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX4;
RX PubMed=15897458; DOI=10.1073/pnas.0501820102;
RA Anjard C., Loomis W.F.;
RT "Peptide signaling during terminal differentiation of Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7607-7611(2005).
RN [2]
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 [3]
RP FUNCTION OF SDF-2.
RX PubMed=9473320; DOI=10.1006/dbio.1997.8804;
RA Anjard C., Zeng C., Loomis W.F., Nellen W.;
RT "Signal transduction pathways leading to spore differentiation in
RT Dictyostelium discoideum.";
RL Dev. Biol. 193:146-155(1998).
RN [4]
RP FUNCTION OF SDF-2, AND INTERACTION WITH DHKA.
RX PubMed=10373524; DOI=10.1128/mcb.19.7.4750;
RA Wang N., Soderbom F., Anjard C., Shaulsky G., Loomis W.F.;
RT "SDF-2 induction of terminal differentiation in Dictyostelium discoideum is
RT mediated by the membrane-spanning sensor kinase DhkA.";
RL Mol. Cell. Biol. 19:4750-4756(1999).
RN [5]
RP INDUCTION.
RX PubMed=16672332; DOI=10.1242/dev.02399;
RA Anjard C., Loomis W.F.;
RT "GABA induces terminal differentiation of Dictyostelium through a GABAB
RT receptor.";
RL Development 133:2253-2261(2006).
CC -!- FUNCTION: Binds to acyl-CoA. Processed into the SDF-2 (spore
CC differentiation factor 2) a peptide which triggers sporulation. SDF-2
CC appears to stimulate prestalk cells to release additional SDF-2 by
CC acting through a signal transduction pathway that also involves dhkA,
CC regA and PKA. Induces encapsulation of prespore cells in a dhkA-
CC dependent manner. GABA induces the release of acbA from prespore cells
CC and induces the exposure of tagC on the surface of prestalk cells where
CC it can convert acbA to SDF-2. Glutamate acts as a competitive inhibitor
CC and is also able to inhibit induction of sporulation by SDF-2.
CC {ECO:0000269|PubMed:10373524, ECO:0000269|PubMed:15897458,
CC ECO:0000269|PubMed:9473320}.
CC -!- SUBUNIT: Interacts with dhkA. {ECO:0000269|PubMed:10373524}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells but is rapidly
CC turned over during early development before reaccumulating during late
CC development in prespore cells but not in prestalk cells. Expression
CC decreases in early development and reappears in late development.
CC Highly expressed in prespore cells at the slug stage (at protein
CC level). {ECO:0000269|PubMed:15897458}.
CC -!- DISRUPTION PHENOTYPE: Cells form fruiting bodies with a reduction of
CC 90% of viable spores and without SDF-2 activity. Diazepam (Valium) can
CC mimic SDF-2 in Dictyostelium bioassay. {ECO:0000269|PubMed:15897458}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AY878075; AAW70088.1; -; Genomic_DNA.
DR EMBL; AAFI02000005; EAL72679.1; -; Genomic_DNA.
DR RefSeq; XP_646321.1; XM_641229.1.
DR AlphaFoldDB; Q5FXM5; -.
DR SMR; Q5FXM5; -.
DR STRING; 44689.DDB0231469; -.
DR PaxDb; Q5FXM5; -.
DR EnsemblProtists; EAL72679; EAL72679; DDB_G0270658.
DR GeneID; 8617276; -.
DR KEGG; ddi:DDB_G0270658; -.
DR dictyBase; DDB_G0270658; acbA.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; Q5FXM5; -.
DR OMA; RYKFEAW; -.
DR PhylomeDB; Q5FXM5; -.
DR Reactome; R-DDI-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-DDI-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:Q5FXM5; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IMP:dictyBase.
DR GO; GO:0005576; C:extracellular region; IMP:dictyBase.
DR GO; GO:0031982; C:vesicle; IMP:dictyBase.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:dictyBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IGI:dictyBase.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IGI:dictyBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IEP:dictyBase.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IGI:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW Cytokinin signaling pathway; Developmental protein; Differentiation;
KW Lipid-binding; Reference proteome; Sporulation; Transport.
FT CHAIN 1..84
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000328371"
FT PEPTIDE 18..52
FT /note="SDF-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000328372"
FT DOMAIN 1..84
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 12
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 27..31
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 9431 MW; D86989ADD83F4EFC CRC64;
MTTFEEAAQK VKEFTKKPSN DELLSLYGLY KQGTDGDCNI SEPWAVQVEA KAKYNAWNAL
KGTSKEDAKA KYVALYEQLA TKYA
