ID   ALY2_YEAST              Reviewed;        1046 AA.
AC   P47029; D6VW99; Q05742;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Arrestin-related trafficking adapter 3;
DE   AltName: Full=Arrestin-like protein 2;
GN   Name=ALY2; Synonyms=ART3; OrderedLocusNames=YJL084C; ORFNames=J0934;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7483841; DOI=10.1002/yea.320110709;
RA   Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA   Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT   "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT   cerevisiae chromosome X, including putative proteins with leucine zippers,
RT   a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT   alpha 2 binding site.";
RL   Yeast 11:681-689(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   PHOSPHORYLATION, AND INTERACTION WITH PCL6 AND PCL7.
RX   PubMed=12098764;
RA   Shi X.Z., Ao S.Z.;
RT   "Analysis of phosphorylation of YJL084c, a yeast protein.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:433-438(2002).
RN   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-162 AND SER-838, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
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   [10]
RP   INTERACTION WITH RPS5, AND FUNCTION.
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-826; SER-838 AND
RP   SER-900, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-586; SER-838;
RP   SER-900; SER-1022 AND SER-1023, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: May regulate endocytosis by recruiting RSP5 ubiquitin ligase
CC       activity to specific plasma membrane proteins in response to
CC       extracellular stimuli. {ECO:0000269|PubMed:18976803}.
CC   -!- SUBUNIT: Interacts with PCL6, PCL7 and RSP5.
CC       {ECO:0000269|PubMed:12098764, ECO:0000269|PubMed:17551511,
CC       ECO:0000269|PubMed:18976803}.
CC   -!- INTERACTION:
CC       P47029; P39940: RSP5; NbExp=5; IntAct=EBI-25974, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Ubiquitinated by RSP5. {ECO:0000269|PubMed:17551511}.
CC   -!- PTM: Phosphorylated by the cyclin-CDKs PCL6-PHO85 and PCL7-PHO85.
CC       {ECO:0000269|PubMed:12098764}.
CC   -!- MISCELLANEOUS: Present with 49 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ALY1 family. {ECO:0000305}.
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DR   EMBL; X83502; CAA58486.1; -; Genomic_DNA.
DR   EMBL; Z49359; CAA89377.1; -; Genomic_DNA.
DR   EMBL; X88851; CAA61319.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08715.1; -; Genomic_DNA.
DR   PIR; S56026; S56026.
DR   RefSeq; NP_012451.1; NM_001181517.1.
DR   AlphaFoldDB; P47029; -.
DR   BioGRID; 33672; 119.
DR   DIP; DIP-1497N; -.
DR   IntAct; P47029; 9.
DR   MINT; P47029; -.
DR   STRING; 4932.YJL084C; -.
DR   GlyGen; P47029; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P47029; -.
DR   MaxQB; P47029; -.
DR   PaxDb; 4932-YJL084C; -.
DR   PeptideAtlas; P47029; -.
DR   EnsemblFungi; YJL084C_mRNA; YJL084C; YJL084C.
DR   GeneID; 853361; -.
DR   KEGG; sce:YJL084C; -.
DR   AGR; SGD:S000003620; -.
DR   SGD; S000003620; ALY2.
DR   VEuPathDB; FungiDB:YJL084C; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   GeneTree; ENSGT00940000176405; -.
DR   HOGENOM; CLU_008578_0_1_1; -.
DR   InParanoid; P47029; -.
DR   OMA; YVTETME; -.
DR   OrthoDB; 3450674at2759; -.
DR   BioCyc; YEAST:G3O-31541-MONOMER; -.
DR   BioGRID-ORCS; 853361; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P47029; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47029; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005769; C:early endosome; IDA:SGD.
DR   GO; GO:0005770; C:late endosome; IDA:SGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR   GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IMP:SGD.
DR   GO; GO:0032386; P:regulation of intracellular transport; IMP:SGD.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11188:SF17; FI24305P1-RELATED; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..1046
FT                   /note="Arrestin-related trafficking adapter 3"
FT                   /id="PRO_0000203049"
FT   REGION          115..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1008
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         586
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1022
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1023
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        852
FT                   /note="P -> G (in Ref. 1; CAA58486)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1046 AA;  117216 MW;  EAC5711EE1AB1C66 CRC64;
     MPMDQSISSP LFPMEKDIDI PLDATPLAQS SSLQLFIHLA EPVVFLQGFD PQKTEYPSVV
     LRGCLVVRIL KPTKLKSISL SFKGYSRTEW PEGIPPKRQE FVEIKDIVDH TWALYPPTEQ
     KSKKKMDASA PNESNNAANN FLTKESGASL YRTLSDNETI TSRKNSISGL SSLNLSPLGA
     PGNSSVNVKD RESRQRSRSS SVTSSNGPSR NLSPINLLKR ATSPSVSHHN YKPTTTSIFS
     DLLNNTFTHN DAASHHGHHI PTSSNHLAMT SNNFTSGSGG EFFVFQPGDY IYAFEELIPQ
     AYPESIKADF GFVEYFLFAS IERPGAFKSN ISARQVVNIV RTQAHNSVEE SEPIIISRDW
     ENQLYYDIVI ASKDIILDAF LPITFKFAPL DKVTLHRIRI YVTETMEYYC REKKVHRMEP
     TKKFLLTEQK GPKLPNLPND ANLSKAKNMG NLLQDPKNGD LVNKEYEYQI FIPSRFNNHQ
     QLHPDTSYEN IKANHWIKIC LRLSRVVDNK RKHYEISIDS PIHVLHRLCS HANTLLPSYD
     GHPASFPKET DSSISSILES SDDNINLYHN SNIFFPKEVL SSPVLSPNVQ PLDILIPHLP
     STSLTRNSRQ FNRNSKSHPS DNTIFNSAKL KSNIYQPESL QRELASPQAI PLSPITSPMS
     NMEVPPPDFD FSSDFISDAA SGTTTTEVSS SESSILPRDP PSYKDTVLHD NNQKRRPNSK
     HPTPPSLKAS HPNKNSDKNS SETLNKKESM SKIEENKHKR ETTPKKRENR DVKSLSTPQR
     EESKDSTSTG NQSNEKNRKR VLSLSSSLHS SPNNSGFAHS ALGNLSNESL RSLNRRESVQ
     DNLPSTIRHD NPFFTDLNQV LIEDELKNHD KNELNRHSTN TSSTPASARS SFDYSGINIS
     KDKLNMEPLL SKTETLTNKV NEDSFLRPND SYVDLLEPSV DTTIDITAPY ARNSSAWHPL
     QNDNDNNQFS PLLGSNENFL NAANAQNSAE SDHNNDIFTQ GSGLTESSKN SDSEERFISR
     LSSPEKVLIN TLDNESGLQS INESTL
//