ALY2_YEAST
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 03-AUG-2022, entry version 155.
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; 102.
DR DIP; DIP-1497N; -.
DR IntAct; P47029; 9.
DR MINT; P47029; -.
DR STRING; 4932.YJL084C; -.
DR iPTMnet; P47029; -.
DR MaxQB; P47029; -.
DR PaxDb; P47029; -.
DR PRIDE; P47029; -.
DR EnsemblFungi; YJL084C_mRNA; YJL084C; YJL084C.
DR GeneID; 853361; -.
DR KEGG; sce:YJL084C; -.
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; DWEDQLH; -.
DR BioCyc; YEAST:G3O-31541-MON; -.
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:0015031; P:protein transport; IBA:GO_Central.
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 Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 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