ARL1_YEAST
ID ARL1_YEAST Reviewed; 183 AA.
AC P38116; D6VQG0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=ADP-ribosylation factor-like protein 1;
DE AltName: Full=Arf-like GTPase 1;
GN Name=ARL1; Synonyms=ARF3; OrderedLocusNames=YBR164C; ORFNames=YBR1216;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=9388248; DOI=10.1074/jbc.272.49.30998;
RA Lee F.-J.S., Huang C.F., Yu W.L., Buu L.M., Lin C.Y., Huang M.C., Moss J.,
RA Vaughan M.;
RT "Characterization of an ADP-ribosylation factor-like 1 protein in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:30998-31005(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND INTERACTION WITH MON2.
RX PubMed=12052896; DOI=10.1128/mcb.22.13.4914-4928.2002;
RA Jochum A., Jackson D., Schwarz H., Pipkorn R., Singer-Krueger B.;
RT "Yeast Ysl2p, homologous to Sec7 domain guanine nucleotide exchange
RT factors, functions in endocytosis and maintenance of vacuole integrity and
RT interacts with the Arf-Like small GTPase Arl1p.";
RL Mol. Cell. Biol. 22:4914-4928(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IMH1.
RX PubMed=12620188; DOI=10.1016/s0960-9822(03)00089-7;
RA Setty S.R.G., Shin M.E., Yoshino A., Marks M.S., Burd C.G.;
RT "Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is
RT regulated by Arf-like GTPase 3.";
RL Curr. Biol. 13:401-404(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IMH1.
RX PubMed=12620189; DOI=10.1016/s0960-9822(03)00091-5;
RA Panic B., Whyte J.R.C., Munro S.;
RT "The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with
RT vesicle-tethering factors at the Golgi apparatus.";
RL Curr. Biol. 13:405-410(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.17 ANGSTROMS).
RX PubMed=11535602; DOI=10.1074/jbc.m106660200;
RA Amor J.C., Horton J.R., Zhu X., Wang Y., Sullards C., Ringe D., Cheng X.,
RA Kahn R.A.;
RT "Structures of yeast ARF2 and ARL1: distinct roles for the N-terminus in
RT the structure and function of ARF family GTPases.";
RL J. Biol. Chem. 276:42477-42484(2001).
CC -!- FUNCTION: Recruits golgins such as IMH1 to the Golgi. Can bind and
CC hydrolyze GTP. May be involved in trafficking events within the
CC endosomal system. {ECO:0000269|PubMed:12052896,
CC ECO:0000269|PubMed:12620188, ECO:0000269|PubMed:12620189}.
CC -!- SUBUNIT: Homodimer. Binds in a GTP-dependent manner to the GRIP domain
CC of IMH1. Interacts with MON2. {ECO:0000269|PubMed:12052896,
CC ECO:0000269|PubMed:12620188, ECO:0000269|PubMed:12620189}.
CC -!- INTERACTION:
CC P38116; Q06704: IMH1; NbExp=3; IntAct=EBI-2869, EBI-33343;
CC P38116; P47061: VPS53; NbExp=3; IntAct=EBI-2869, EBI-25828;
CC P38116; Q12071: VPS54; NbExp=3; IntAct=EBI-2869, EBI-36751;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:12620188,
CC ECO:0000269|PubMed:12620189}.
CC -!- MISCELLANEOUS: Present with 5190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; U89332; AAC49875.1; -; mRNA.
DR EMBL; Z36033; CAA85125.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07280.1; -; Genomic_DNA.
DR PIR; S46035; S46035.
DR RefSeq; NP_009723.3; NM_001178512.3.
DR PDB; 1MOZ; X-ray; 3.17 A; A/B=1-183.
DR PDBsum; 1MOZ; -.
DR AlphaFoldDB; P38116; -.
DR SMR; P38116; -.
DR BioGRID; 32864; 421.
DR ComplexPortal; CPX-1028; NEO1-MON2-ARL1-DOP1 membrane remodeling complex.
DR IntAct; P38116; 8.
DR MINT; P38116; -.
DR STRING; 4932.YBR164C; -.
DR TCDB; 3.A.30.1.1; the endoplasmic reticulum surface retrieval pathway (er-surf).
DR iPTMnet; P38116; -.
DR MaxQB; P38116; -.
DR PaxDb; P38116; -.
DR PRIDE; P38116; -.
DR EnsemblFungi; YBR164C_mRNA; YBR164C; YBR164C.
DR GeneID; 852462; -.
DR KEGG; sce:YBR164C; -.
DR SGD; S000000368; ARL1.
DR VEuPathDB; FungiDB:YBR164C; -.
DR eggNOG; KOG0072; Eukaryota.
DR GeneTree; ENSGT00940000155118; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P38116; -.
DR OMA; VRWSKDQ; -.
DR BioCyc; YEAST:G3O-29114-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR EvolutionaryTrace; P38116; -.
DR PRO; PR:P38116; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38116; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
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 CHAIN 2..183
FT /note="ADP-ribosylation factor-like protein 1"
FT /id="PRO_0000207421"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
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:9388248"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1MOZ"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1MOZ"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:1MOZ"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:1MOZ"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1MOZ"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:1MOZ"
SQ SEQUENCE 183 AA; 20434 MW; 84D0E1F79EC21E38 CRC64;
MGNIFSSMFD KLWGSNKELR ILILGLDGAG KTTILYRLQI GEVVTTKPTI GFNVETLSYK
NLKLNVWDLG GQTSIRPYWR CYYADTAAVI FVVDSTDKDR MSTASKELHL MLQEEELQDA
ALLVFANKQD QPGALSASEV SKELNLVELK DRSWSIVASS AIKGEGITEG LDWLIDVIKE
EQL
