ARF1_PLAF7
ID ARF1_PLAF7 Reviewed; 181 AA.
AC Q7KQL3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ADP-ribosylation factor 1 {ECO:0000303|PubMed:21045287, ECO:0000312|EMBL:AAN35400.1};
DE Short=pfARF1 {ECO:0000303|PubMed:21045287};
GN Name=ARF1 {ECO:0000250|UniProtKB:Q94650};
GN Synonyms=ARF {ECO:0000250|UniProtKB:Q94650}; ORFNames=PF10_0203;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1] {ECO:0000312|EMBL:AAN35400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000305}
RP FUNCTION, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP.
RC STRAIN=3D7;
RX PubMed=21045287; DOI=10.1107/s1744309110036997;
RA Cook W.J., Smith C.D., Senkovich O., Holder A.A., Chattopadhyay D.;
RT "Structure of Plasmodium falciparum ADP-ribosylation factor 1.";
RL Acta Crystallogr. F 66:1426-1431(2010).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC {ECO:0000269|PubMed:21045287}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P19146}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000255}.
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DR EMBL; AE014185; AAN35400.1; -; Genomic_DNA.
DR RefSeq; XP_001347487.1; XM_001347451.1.
DR PDB; 3LRP; X-ray; 2.50 A; A=1-181.
DR PDBsum; 3LRP; -.
DR AlphaFoldDB; Q7KQL3; -.
DR SMR; Q7KQL3; -.
DR STRING; 5833.PF10_0203; -.
DR SwissPalm; Q7KQL3; -.
DR PRIDE; Q7KQL3; -.
DR EnsemblProtists; CZT98464; CZT98464; PF3D7_1020900.
DR GeneID; 810360; -.
DR KEGG; pfa:PF3D7_1020900; -.
DR VEuPathDB; PlasmoDB:PF3D7_1020900; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; Q7KQL3; -.
DR OMA; VEYRNIQ; -.
DR PhylomeDB; Q7KQL3; -.
DR Reactome; R-PFA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-PFA-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-PFA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-PFA-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-PFA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-PFA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-PFA-6811438; Intra-Golgi traffic.
DR EvolutionaryTrace; Q7KQL3; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:GeneDB.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; TAS:GeneDB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 3D-structure; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Lipoprotein; Myristate; Nucleotide-binding; Protein transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19146"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1"
FT /evidence="ECO:0000250|UniProtKB:P19146"
FT /id="PRO_0000412994"
FT BINDING 27..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21045287"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P18085"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21045287"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21045287"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P19146"
FT HELIX 2..8
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3LRP"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3LRP"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3LRP"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3LRP"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3LRP"
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
