ARF_CANAL
ID ARF_CANAL Reviewed; 179 AA.
AC P22274; A0A1D8PTU0; Q5A316;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 5.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ADP-ribosylation factor;
GN Name=ARF1; OrderedLocusNames=CAALFM_CR08700CA;
GN ORFNames=CaO19.13805, CaO19.6447;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1544569; DOI=10.1016/0378-1119(92)90455-x;
RA Denich K., Malloy P.J., Feldman D.;
RT "Cloning and characterization of the gene encoding the ADP-ribosylation
RT factor in Candida albicans.";
RL Gene 110:123-128(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1512254; DOI=10.1016/s0021-9258(18)41908-4;
RA Langner C.A., Lodge J.K., Travis S.J., Caldwell J.E., Lu T., Li Q.,
RA Bryant M.L., Devadas B., Gokel G.W., Kobayashi G.S.;
RT "4-oxatetradecanoic acid is fungicidal for Cryptococcus neoformans and
RT inhibits replication of human immunodeficiency virus I.";
RL J. Biol. Chem. 267:17159-17169(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking; may
CC modulate vesicle budding and uncoating within the Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; M54910; AAA64266.1; -; Genomic_DNA.
DR EMBL; S43354; AAB23053.2; -; Genomic_DNA.
DR EMBL; CP017630; AOW31549.1; -; Genomic_DNA.
DR PIR; JH0260; JH0260.
DR RefSeq; XP_716284.1; XM_711191.1.
DR PDB; 6PTA; X-ray; 2.50 A; A/B/C/D=1-179.
DR PDBsum; 6PTA; -.
DR AlphaFoldDB; P22274; -.
DR SMR; P22274; -.
DR STRING; 237561.P22274; -.
DR PRIDE; P22274; -.
DR GeneID; 3642130; -.
DR KEGG; cal:CAALFM_CR08700CA; -.
DR CGD; CAL0000186453; ARF1.
DR VEuPathDB; FungiDB:CR_08700C_A; -.
DR eggNOG; KOG0070; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P22274; -.
DR OMA; LWRILNI; -.
DR OrthoDB; 1362554at2759; -.
DR PRO; PR:P22274; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..179
FT /note="ADP-ribosylation factor"
FT /id="PRO_0000207412"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CONFLICT 149
FT /note="R -> M (in Ref. 1; AAA64266)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6PTA"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6PTA"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6PTA"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6PTA"
SQ SEQUENCE 179 AA; 20258 MW; BBB1949760975202 CRC64;
MGLTISKLFA SLLGRREMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRY YFQNTQGIIF VVDSNDRDRI NEAREELQSM LNEDELKDAV
LLVLANKQDL PNAMNAAEIT EKMGLHSIRN RPWFIQATCA TTGDGLYEGL EWLSNQVGK
