ID   ART10_YEAST             Reviewed;         518 AA.
AC   P18634; D6VZ27;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Arrestin-related trafficking adapter 10;
GN   Name=ART10; OrderedLocusNames=YLR392C; ORFNames=L8084.13;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210.
RX   PubMed=2141026; DOI=10.1016/s0021-9258(19)38763-0;
RA   Ackerman S.H., Tzagoloff A.;
RT   "ATP 10, a yeast nuclear gene required for the assembly of the
RT   mitochondrial F1-F0 complex.";
RL   J. Biol. Chem. 265:9952-9959(1990).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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   [6]
RP   INTERACTION WITH RSP5, AND UBIQUITINATION BY RSP5.
RX   PubMed=17551511; DOI=10.1038/msb4100159;
RA   Gupta R., Kus B., Fladd C., Wasmuth J., Tonikian R., Sidhu S., Krogan N.J.,
RA   Parkinson J., Rotin D.;
RT   "Ubiquitination screen using protein microarrays for comprehensive
RT   identification of Rsp5 substrates in yeast.";
RL   Mol. Syst. Biol. 3:116-116(2007).
RN   [7]
RP   GENE NAME.
RX   PubMed=18976803; DOI=10.1016/j.cell.2008.09.025;
RA   Lin C.H., MacGurn J.A., Chu T., Stefan C.J., Emr S.D.;
RT   "Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and
RT   protein turnover at the cell surface.";
RL   Cell 135:714-725(2008).
RN   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY
RP   MASS 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: May regulate endocytosis by recruiting RSP5 ubiquitin ligase
CC       activity to specific plasma membrane proteins in response to
CC       extracellular stimuli. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RSP5. {ECO:0000269|PubMed:17551511}.
CC   -!- INTERACTION:
CC       P18634; P39940: RSP5; NbExp=5; IntAct=EBI-27197, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Ubiquitinated by RSP5. {ECO:0000269|PubMed:17551511}.
CC   -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ART10 family. {ECO:0000305}.
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DR   EMBL; U19729; AAB82352.1; -; Genomic_DNA.
DR   EMBL; J05463; AAB05631.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09693.1; -; Genomic_DNA.
DR   PIR; S55948; S55948.
DR   RefSeq; NP_013496.3; NM_001182280.3.
DR   AlphaFoldDB; P18634; -.
DR   BioGRID; 31651; 43.
DR   DIP; DIP-1946N; -.
DR   IntAct; P18634; 2.
DR   MINT; P18634; -.
DR   STRING; 4932.YLR392C; -.
DR   iPTMnet; P18634; -.
DR   MaxQB; P18634; -.
DR   PaxDb; 4932-YLR392C; -.
DR   PeptideAtlas; P18634; -.
DR   EnsemblFungi; YLR392C_mRNA; YLR392C; YLR392C.
DR   GeneID; 851108; -.
DR   KEGG; sce:YLR392C; -.
DR   AGR; SGD:S000004384; -.
DR   SGD; S000004384; ART10.
DR   VEuPathDB; FungiDB:YLR392C; -.
DR   eggNOG; ENOG502QWIY; Eukaryota.
DR   HOGENOM; CLU_540776_0_0_1; -.
DR   InParanoid; P18634; -.
DR   OMA; FKTCTIK; -.
DR   OrthoDB; 2010588at2759; -.
DR   BioCyc; YEAST:G3O-32457-MONOMER; -.
DR   BioGRID-ORCS; 851108; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P18634; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P18634; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IBA:GO_Central.
DR   CDD; cd22952; ART10-like; 1.
DR   Gene3D; 2.60.40.640; -; 1.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11188:SF172; ARRESTIN DOMAIN-CONTAINING PROTEIN 5; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endocytosis; Isopeptide bond; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..518
FT                   /note="Arrestin-related trafficking adapter 10"
FT                   /id="PRO_0000203235"
FT   CROSSLNK        118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   518 AA;  59758 MW;  65399EA2FFFC2C23 CRC64;
     MAPKISISLN PPYNGEFYSS NDQMSGIVSL QLTKALSIRK ISVILKGFSE TLTKIDQEYM
     FQQNGMMMPG QDNKSFHTLM KFEQRVFPPD NVWNALDGSS KPFKVKPGSY NYSFQFDKFP
     RKPECLKNHT AKTVAFVTRS NARLPPTFNS HWQEFNKIDN LDLYFYSFGK VIYMVQVQLE
     LGKSSSWFKP FHKLIREIET FEFIPEPKDL IIEPDEDDNE ELNAFSNNSR GNSMVTNNEF
     FNSSNLKVPS KDVKVVNGVG YIKSDRNFSQ ANSILIENGD IRSRPVSSVT STRQSTRLVN
     GMKVFPSTYK MGLPDGESNM RIEVRSRDLK QIYRKDYLFR SGSQNFDKVY VVMEGNIASL
     SKMQITPLKL QLNLLETTTY LSQGIANGNY SSLKLIEIDL NQLKSNKPLL DLNEIRENFD
     GSMFECELRL KDHPILRKLV FNEEDYRHRG NRLYSFKTCT IKRTFSLQLL IEWGINGIRK
     QSEVNIDPVQ IFCQVREHVE AEALPRYVPP PTYTEMAS
//