ART5_YEAST
ID ART5_YEAST Reviewed; 586 AA.
AC P53244; D6VUK2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Arrestin-related trafficking adapter 5;
GN Name=ART5; OrderedLocusNames=YGR068C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [4]
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 [5]
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 [6]
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 [7]
RP UBIQUITINATION BY RSP5.
RX PubMed=17951556; DOI=10.1074/mcp.m700353-mcp200;
RA Lu J., Lin Y., Qian J., Tao S., Zhu J., Pickart C., Zhu H.;
RT "Functional dissection of a HECT ubiquitin E3 ligase.";
RL Mol. Cell. Proteomics 7:35-45(2008).
RN [8]
RP IDENTIFICATION BY 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).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-364, 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:0000269|PubMed:18976803}.
CC -!- SUBUNIT: Interacts with RSP5. {ECO:0000269|PubMed:17551511,
CC ECO:0000269|PubMed:18976803}.
CC -!- INTERACTION:
CC P53244; P39940: RSP5; NbExp=4; IntAct=EBI-23201, EBI-16219;
CC -!- PTM: Ubiquitinated by RSP5. {ECO:0000269|PubMed:17551511,
CC ECO:0000269|PubMed:17951556}.
CC -!- MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; Z72853; CAA97070.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08163.1; -; Genomic_DNA.
DR PIR; S64363; S64363.
DR RefSeq; NP_011582.1; NM_001181197.1.
DR AlphaFoldDB; P53244; -.
DR BioGRID; 33312; 95.
DR DIP; DIP-1864N; -.
DR IntAct; P53244; 13.
DR MINT; P53244; -.
DR STRING; 4932.YGR068C; -.
DR iPTMnet; P53244; -.
DR MaxQB; P53244; -.
DR PaxDb; P53244; -.
DR PRIDE; P53244; -.
DR EnsemblFungi; YGR068C_mRNA; YGR068C; YGR068C.
DR GeneID; 852960; -.
DR KEGG; sce:YGR068C; -.
DR SGD; S000003300; ART5.
DR VEuPathDB; FungiDB:YGR068C; -.
DR eggNOG; KOG3780; Eukaryota.
DR HOGENOM; CLU_018982_3_0_1; -.
DR InParanoid; P53244; -.
DR OMA; KGNYNLP; -.
DR BioCyc; YEAST:G3O-30782-MON; -.
DR PRO; PR:P53244; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53244; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISA:SGD.
DR Gene3D; 2.60.40.640; -; 1.
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 Endocytosis; Isopeptide bond; Reference proteome; Ubl conjugation.
FT CHAIN 1..586
FT /note="Arrestin-related trafficking adapter 5"
FT /id="PRO_0000202804"
FT REGION 123..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 586 AA; 65477 MW; C85B0D42116C041A CRC64;
MFSLSSLSSS GGHSEQKERE RISYFDIRIN SPYKDIILIQ GSPLELSSIP LSGNLVISVK
NEIVVKKISL RLVGRFKLEF LQVGRYKKNS SSLASLVKEK RKIFECYWDN LLVSSKGDVL
VGGENAENQH NSSSGRSTSN QDMDTSGNAI FLSKRSLSSP VFNKIIRRKT HSSHRKILEL
PENGVTGTPF EGLRENARSR SSSSNTLNNN SHSYSNRDGS GSSYLFLMKR GNYELPFNTM
LPPEVCETIE GLQSGSILYS FEAIIDGRQL WDTDLSVHTS PHGPIGSTST SGNGMRTKNK
IIIKKFKYLR ILRTLSMDNL AMQEEISVGN TWRDKLQYET SIPSRAVPIG STTPVKIKIF
PFEKNIRLDR IEMALIQYYA MKDSSAQIYD DEIAVMKITH LADFGPLTDK LDVDCPFTIP
DNLKQITQDC CLQDNLIRVM HKLQVRILLQ RQVDGEYKNL EIKAQLPMLL FISPHLPMKG
RLVLFDKHDG KIHFRPGELV PLFLTTYPAQ GLTPGVELNS TTTAHLALPQ PPPNYHESTN
DHLMPALQPL GADSVVLTVP SYEQAQAQAS ASSYVTGSVP AYCDDD
