ARL3_YEAST
ID ARL3_YEAST Reviewed; 198 AA.
AC Q02804; D6W3W3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ADP-ribosylation factor-like protein 3;
DE AltName: Full=Arf-like GTPase 3;
GN Name=ARL3; Synonyms=ARP1; OrderedLocusNames=YPL051W;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9920936; DOI=10.1074/jbc.274.6.3819;
RA Huang C.F., Buu L.M., Yu W.L., Lee F.-J.S.;
RT "Characterization of a novel ADP-ribosylation factor-like protein (yARL3)
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:3819-3827(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
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, AND INTERACTION WITH SLO1.
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 ACETYLATION AT MET-1, AND INTERACTION WITH SYS1.
RX PubMed=15077113; DOI=10.1038/ncb1120;
RA Behnia R., Panic B., Whyte J.R.C., Munro S.;
RT "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal
RT acetylation and the membrane protein Sys1p.";
RL Nat. Cell Biol. 6:405-413(2004).
RN [9]
RP ACETYLATION AT MET-1, AND INTERACTION WITH SYS1.
RX PubMed=15077114; DOI=10.1038/ncb1121;
RA Setty S.R., Strochlic T.I., Tong A.H., Boone C., Burd C.G.;
RT "Golgi targeting of ARF-like GTPase Arl3p requires its Nalpha-acetylation
RT and the integral membrane protein Sys1p.";
RL Nat. Cell Biol. 6:414-419(2004).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in the targeting of ARL1 to the Golgi. Can bind and
CC hydrolyze GTP. {ECO:0000269|PubMed:12620188,
CC ECO:0000269|PubMed:12620189}.
CC -!- SUBUNIT: Interacts with SYS1 and SLO1. {ECO:0000269|PubMed:12620189,
CC ECO:0000269|PubMed:15077113, ECO:0000269|PubMed:15077114}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- MISCELLANEOUS: Present with 1920 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; AF017142; AAD13357.1; -; Genomic_DNA.
DR EMBL; U39205; AAB68314.1; -; Genomic_DNA.
DR EMBL; AY558323; AAS56649.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11379.1; -; Genomic_DNA.
DR PIR; S61091; S61091.
DR RefSeq; NP_015274.1; NM_001183865.1.
DR PDB; 6YGC; X-ray; 2.99 A; D=1-5.
DR PDBsum; 6YGC; -.
DR AlphaFoldDB; Q02804; -.
DR SMR; Q02804; -.
DR BioGRID; 36129; 429.
DR DIP; DIP-2122N; -.
DR IntAct; Q02804; 6.
DR MINT; Q02804; -.
DR STRING; 4932.YPL051W; -.
DR iPTMnet; Q02804; -.
DR MaxQB; Q02804; -.
DR PaxDb; Q02804; -.
DR PRIDE; Q02804; -.
DR EnsemblFungi; YPL051W_mRNA; YPL051W; YPL051W.
DR GeneID; 856056; -.
DR KEGG; sce:YPL051W; -.
DR SGD; S000005972; ARL3.
DR VEuPathDB; FungiDB:YPL051W; -.
DR eggNOG; KOG0076; Eukaryota.
DR GeneTree; ENSGT00940000156407; -.
DR HOGENOM; CLU_040729_7_2_1; -.
DR InParanoid; Q02804; -.
DR OMA; QCHGIIF; -.
DR BioCyc; YEAST:G3O-33964-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q02804; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02804; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane 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:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
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; Acetylation; Golgi apparatus; GTP-binding; Isopeptide bond;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..198
FT /note="ADP-ribosylation factor-like protein 3"
FT /id="PRO_0000207422"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:15077113,
FT ECO:0000269|PubMed:15077114"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 198 AA; 22782 MW; 46E8CFEB1931A220 CRC64;
MFHLVKGLYN NWNKKEQYSI LILGLDNAGK TTFLETLKKE YSLAFKALEK IQPTVGQNVA
TIPVDSKQIL KFWDVGGQES LRSMWSEYYS LCHGIIFIVD SSDRERLDEC STTLQSVVMD
EEIEGVPILM LANKQDRQDR MEVQDIKEVF NKIAEHISAR DSRVLPISAL TGEGVKDAIE
WMIVRLERNK KSRPPIYK
