ARF1_PLAFA
ID ARF1_PLAFA Reviewed; 181 AA.
AC Q94650; O02502; O02593;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ADP-ribosylation factor 1;
DE Short=plARF;
GN Name=ARF1; Synonyms=ARF;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GTP-BINDING, AND DEVELOPMENTAL STAGE.
RC STRAIN=T9/96; TISSUE=Blood;
RX PubMed=8954160; DOI=10.1111/j.1432-1033.1996.0104r.x;
RA Stafford W.H., Stockley R.W., Ludbrook S.B., Holder A.A.;
RT "Isolation, expression and characterization of the gene for an ADP-
RT ribosylation factor from the human malaria parasite, Plasmodium
RT falciparum.";
RL Eur. J. Biochem. 242:104-113(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9084044; DOI=10.1016/s0166-6851(96)02803-4;
RA Truong R.M., Francis S.E., Chakrabarti D., Goldberg D.E.;
RT "Cloning and characterization of Plasmodium falciparum ADP-ribosylation
RT factor and factor-like genes.";
RL Mol. Biochem. Parasitol. 84:247-253(1997).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated and reaches a maximum at
CC or just after nuclear division (at 30 - 36h) when the daughter
CC parasites produced by asexual reproduction are segregating to become
CC individual merozoites. The levels drop dramatically at 36 - 42h and
CC remain low through the rest of the life cycle. Detected in the schizont
CC stage. Increased expression may correlate with post-mitotic nuclear
CC vesicle fusion. {ECO:0000269|PubMed:8954160,
CC ECO:0000269|PubMed:9084044}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; Z80359; CAB02498.1; -; Genomic_DNA.
DR EMBL; U57370; AAB63304.1; -; mRNA.
DR AlphaFoldDB; Q94650; -.
DR SMR; Q94650; -.
DR EnsemblProtists; CZT98464; CZT98464; PF3D7_1020900.
DR VEuPathDB; PlasmoDB:PF3D7_1020900; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000306500; -.
DR VEuPathDB; PlasmoDB:Pf7G8_100025400; -.
DR VEuPathDB; PlasmoDB:PfCD01_100026200; -.
DR VEuPathDB; PlasmoDB:PfDd2_100026300; -.
DR VEuPathDB; PlasmoDB:PfGA01_100026300; -.
DR VEuPathDB; PlasmoDB:PfGB4_100026000; -.
DR VEuPathDB; PlasmoDB:PfGN01_100026500; -.
DR VEuPathDB; PlasmoDB:PfHB3_100025400; -.
DR VEuPathDB; PlasmoDB:PfIT_100025000; -.
DR VEuPathDB; PlasmoDB:PfKE01_100026300; -.
DR VEuPathDB; PlasmoDB:PfKH01_100025500; -.
DR VEuPathDB; PlasmoDB:PfKH02_100026400; -.
DR VEuPathDB; PlasmoDB:PfML01_100025200; -.
DR VEuPathDB; PlasmoDB:PfNF135_100026200; -.
DR VEuPathDB; PlasmoDB:PfNF166_100025800; -.
DR VEuPathDB; PlasmoDB:PfNF54_100026000; -.
DR VEuPathDB; PlasmoDB:PfSD01_100025600; -.
DR VEuPathDB; PlasmoDB:PfSN01_100026400; -.
DR VEuPathDB; PlasmoDB:PfTG01_100026300; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1"
FT /id="PRO_0000207447"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 20912 MW; 18013B069BEA2413 CRC64;
MGLYVSRLFN RLFQKKDVRI LMVGLDAAGK TTILYKVKLG EVVTTIPTIG FNVETVEFRN
ISFTVWDVGG QDKIRPLWRH YYSNTDGLIF VVDSNDRERI DDAREELHRM INEEELKDAI
ILVFANKQDL PNAMSAAEVT EKLHLNTIRE RNWFIQSTCA TRGDGLYEGF DWLTTHLNNA
K
