ARF6_SCHPO
ID ARF6_SCHPO Reviewed; 184 AA.
AC Q9Y7Z2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ADP-ribosylation factor 6;
GN Name=arf6; ORFNames=SPBC1539.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18060866; DOI=10.1016/j.bbrc.2007.11.117;
RA Fujita A.;
RT "ADP-ribosylation factor arf6p may function as a molecular switch of new
RT end take off in fission yeast.";
RL Biochem. Biophys. Res. Commun. 366:193-198(2008).
CC -!- FUNCTION: GTP-binding protein that functions as a molecular switch for
CC the activation of 'new end take off' (NETO), a process in which the
CC directions of cell growth change from a monopolar manner to a bipolar
CC manner in fission yeast. Involved in supplying membrane to the growing
CC new end. {ECO:0000269|PubMed:18060866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18060866};
CC Peripheral membrane protein {ECO:0000269|PubMed:18060866}. Cell septum
CC {ECO:0000269|PubMed:18060866}. Note=Localizes at both cell ends and
CC presumptive septa in a cell-cycle dependent manner.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB51340.1; -; Genomic_DNA.
DR PIR; T39467; T39467.
DR RefSeq; NP_596822.1; NM_001023842.2.
DR AlphaFoldDB; Q9Y7Z2; -.
DR SMR; Q9Y7Z2; -.
DR BioGRID; 276481; 66.
DR STRING; 4896.SPBC1539.08.1; -.
DR MaxQB; Q9Y7Z2; -.
DR PaxDb; Q9Y7Z2; -.
DR EnsemblFungi; SPBC1539.08.1; SPBC1539.08.1:pep; SPBC1539.08.
DR GeneID; 2539937; -.
DR KEGG; spo:SPBC1539.08; -.
DR PomBase; SPBC1539.08; arf6.
DR VEuPathDB; FungiDB:SPBC1539.08; -.
DR eggNOG; KOG0071; Eukaryota.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; Q9Y7Z2; -.
DR OMA; WSVIPTI; -.
DR PhylomeDB; Q9Y7Z2; -.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR PRO; PR:Q9Y7Z2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISS:PomBase.
DR GO; GO:0051523; P:cell growth mode switching, monopolar to bipolar; IMP:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041838; Arf6.
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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..184
FT /note="ADP-ribosylation factor 6"
FT /id="PRO_0000207417"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 184 AA; 20723 MW; CF174910F5EBB971 CRC64;
MGNSLFKGFS KPFSRLFSNK EMRILMLGLD AAGKTTILYK LKLNQSVVTI PTVGFNVETV
TYKNIKFNVW DVGGQDKIRP LWRHYFTGTK GLIFVVDSAD SNRISEARQE LHRIISDREM
RDCLLLVLAN KQDLPGALSP AQITDVLQLD KLKDRLWNVQ PTCALTGDGL LEGLAWLSQN
AKLK
