ALY1_YEAST
ID ALY1_YEAST Reviewed; 915 AA.
AC P36117; D6VX86;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Arrestin-related trafficking adapter 6;
DE AltName: Full=Arrestin-like protein 1;
GN Name=ALY1; Synonyms=ART6; OrderedLocusNames=YKR021W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [4]
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 [5]
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 [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 INTERACTION WITH RSP5, 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 [8]
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 RSP5. {ECO:0000269|PubMed:17551511,
CC ECO:0000269|PubMed:18976803}.
CC -!- INTERACTION:
CC P36117; P39940: RSP5; NbExp=4; IntAct=EBI-26358, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Ubiquitinated by RSP5. {ECO:0000269|PubMed:17551511}.
CC -!- MISCELLANEOUS: Present with 414 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; Z28246; CAA82093.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09176.1; -; Genomic_DNA.
DR PIR; S38090; S38090.
DR RefSeq; NP_012946.3; NM_001179811.4.
DR AlphaFoldDB; P36117; -.
DR BioGRID; 34153; 52.
DR DIP; DIP-2615N; -.
DR IntAct; P36117; 5.
DR MINT; P36117; -.
DR STRING; 4932.YKR021W; -.
DR iPTMnet; P36117; -.
DR MaxQB; P36117; -.
DR PaxDb; P36117; -.
DR PRIDE; P36117; -.
DR EnsemblFungi; YKR021W_mRNA; YKR021W; YKR021W.
DR GeneID; 853891; -.
DR KEGG; sce:YKR021W; -.
DR SGD; S000001729; ALY1.
DR VEuPathDB; FungiDB:YKR021W; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000176405; -.
DR HOGENOM; CLU_008578_0_1_1; -.
DR InParanoid; P36117; -.
DR OMA; IAISKDW; -.
DR BioCyc; YEAST:G3O-31997-MON; -.
DR PRO; PR:P36117; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36117; 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; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; IGI: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; IBA:GO_Central.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011022; Arrestin_C-like.
DR Pfam; PF02752; Arrestin_C; 1.
DR SMART; SM01017; Arrestin_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..915
FT /note="Arrestin-related trafficking adapter 6"
FT /id="PRO_0000203200"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 915 AA; 102540 MW; 44E43EB7683E4AC4 CRC64;
MLQFNTENDT VAPVFPMEQD INAAPDAVPL VQTTTLQVFV KLAEPIVFLK GFETNGLSEI
APSILRGSLI VRVLKPNKLK SISITFKGIS RTEWPEGIPP KREEFSDVET VVNHTWPFYQ
ADDGMNSFTL EHHSSNNSSN RPSMSDEDYL LEKSGASVYI PPTAEPPKDN SNLSLDAYER
NSLSSDNLSN KPVSSDVSHD DSKLLAIQKT PLPSSSRRGS VPANFHGNSL SPHTFISDLF
TKTFSNSGAT PSPEQEDNYL TPSKDSKEVF IFRPGDYIYT FEQPISQSYP ESIKANFGSV
EYKLSIDIER FGAFKSTIHT QLPIKVVRLP SDGSVEETEA IAISKDWKDL LHYDVVIFSK
EIVLNAFLPI DFHFAPLDKV TLHRIRIYLT ESMEYTCNSN GNHEKARRLE PTKKFLLAEH
NGPKLPHIPA GSNPLKAKNR GNILLDEKSG DLVNKDFQFE VFVPSKFTNS IRLHPDTNYD
KIKAHHWIKI CLRLSKKYGD NRKHFEISID SPIHILNQLC SHANTLLPSY ESHFQYCDED
GNFAPAADQQ NYASHHDSNI FFPKEVLSSP VLSPNVQKMN IRIPSDLPVV RNRAESVKKS
KSDNTSKKND QSSNVFASKQ LVANIYKPNQ IPRELTSPQA LPLSPITSPI LNYQPLSNSP
PPDFDFDLAK RGAADSHAIP VDPPSYFDVL KADGIELPYY DTSSSKIPEL KLNKSRETLA
SIEEDSFNGW SQIDDLSDED DNDGDIASGF NFKLSTSAPS ENVNSHTPIL QSLNMSLDGR
KKNRASLHAT SVLPSTIRQN NQHFNDINQM LGSSDEDAFP KSQSLNFNKK LPILKINDNV
IQSNSNSNNR VDNPEDTVDS SVDITAFYDP RMSSDSKFDW EVSKNHVDPA AYSVNVASEN
RVLDDFKKAF REKRK
