ID   ARF_NEUCR               Reviewed;         185 AA.
AC   Q7RVM2; V5IQ49;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ADP-ribosylation factor;
GN   ORFNames=NCU08340;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; CM002236; ESA44151.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44152.1; -; Genomic_DNA.
DR   RefSeq; XP_011393189.1; XM_011394887.1.
DR   RefSeq; XP_011393190.1; XM_011394888.1.
DR   AlphaFoldDB; Q7RVM2; -.
DR   SMR; Q7RVM2; -.
DR   BioGRID; 1982572; 1.
DR   STRING; 5141.EFNCRP00000006444; -.
DR   PRIDE; Q7RVM2; -.
DR   EnsemblFungi; ESA44151; ESA44151; NCU08340.
DR   EnsemblFungi; ESA44152; ESA44152; NCU08340.
DR   GeneID; 3881408; -.
DR   KEGG; ncr:NCU08340; -.
DR   VEuPathDB; FungiDB:NCU08340; -.
DR   HOGENOM; CLU_040729_9_3_1; -.
DR   InParanoid; Q7RVM2; -.
DR   OMA; VEYRNIQ; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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   3: Inferred from homology;
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                   /evidence="ECO:0000250"
FT   CHAIN           2..185
FT                   /note="ADP-ribosylation factor"
FT                   /id="PRO_0000207415"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..74
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..132
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   185 AA;  20979 MW;  46E4476E6B365C1A CRC64;
     MGNTLSIFGK LFDGLFGKKE MRILMVGLDA AGKTTILYKL KLGEVVTTIP TIGFNVETVE
     YKNIQFTVWD VGGQDKIRPL WRHYFQNTQG IIFVVDSNDR DRVVEAREEL QRMLNEDELR
     DALLLVFANK QDLPNAMNAA EITDKLGLSS LRQRSWYIQA TCATTGDGLF EGLDWLSTEL
     KKKSP