ARF_CRYNJ
ID ARF_CRYNJ Reviewed; 182 AA.
AC P0CM16; P34728; Q55PQ9; Q5KDP9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=ADP-ribosylation factor;
GN Name=ARF; OrderedLocusNames=CNG03220;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MYRISTOYLATION AT GLY-2.
RC STRAIN=L210425;
RX PubMed=8300631; DOI=10.1016/s0021-9258(17)42038-2;
RA Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I.;
RT "Comparison of myristoyl-CoA:protein N-myristoyltransferases from three
RT pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and
RT Candida albicans.";
RL J. Biol. Chem. 269:2996-3009(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; L25115; AAA17546.1; -; Genomic_DNA.
DR EMBL; AE017347; AAW44725.1; -; Genomic_DNA.
DR PIR; C49993; C49993.
DR RefSeq; XP_572032.1; XM_572032.1.
DR AlphaFoldDB; P0CM16; -.
DR SMR; P0CM16; -.
DR STRING; 5207.AAW44725; -.
DR iPTMnet; P0CM16; -.
DR PaxDb; P0CM16; -.
DR EnsemblFungi; AAW44725; AAW44725; CNG03220.
DR GeneID; 3258864; -.
DR KEGG; cne:CNG03220; -.
DR VEuPathDB; FungiDB:CNG03220; -.
DR eggNOG; KOG0070; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P0CM16; -.
DR OMA; VEYRNIQ; -.
DR OrthoDB; 1362554at2759; -.
DR Proteomes; UP000002149; Chromosome 7.
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 ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Myristate;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..182
FT /note="ADP-ribosylation factor"
FT /id="PRO_0000207413"
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:0000269|PubMed:8300631"
SQ SEQUENCE 182 AA; 20593 MW; 31729C7BA185D706 CRC64;
MGLSVSKLLN GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGIIF VVDSNDRERI TEAREELQRM LSEDELRDAL
LLVFANKQDL PNAMNAAEIT DKLGLHSLRQ RSWYIQAACA TSGDGLYEGL EWLSANLKRK
SP
