SWA2_YEAST
ID SWA2_YEAST Reviewed; 668 AA.
AC Q06677; D6VSV1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Auxilin-like clathrin uncoating factor SWA2;
DE AltName: Full=Bud site selection protein 24;
DE AltName: Full=DnaJ-related protein SWA2;
DE Short=J protein SWA2;
DE AltName: Full=Synthetic lethal with ARF1 protein 2;
GN Name=SWA2; Synonyms=AUX1, BUD24; OrderedLocusNames=YDR320C;
GN ORFNames=D9798.10;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF GLY-388,
RP AND INTERACTION WITH CLC1.
RX PubMed=11084334; DOI=10.1016/s0960-9822(00)00771-5;
RA Gall W.E., Higginbotham M.A., Chen C.-Y., Ingram M.F., Cyr D.M.,
RA Graham T.R.;
RT "The auxilin-like phosphoprotein Swa2p is required for clathrin function in
RT yeast.";
RL Curr. Biol. 10:1349-1358(2000).
RN [4]
RP FUNCTION.
RX PubMed=11146663; DOI=10.1038/35046619;
RA Pishvaee B., Costaguta G., Yeung B.G., Ryazantsev S., Greener T.,
RA Greene L.E., Eisenberg E., McCaffery J.M., Payne G.S.;
RT "A yeast DNA J protein required for uncoating of clathrin-coated vesicles
RT in vivo.";
RL Nat. Cell Biol. 2:958-963(2000).
RN [5]
RP FUNCTION IN ENDOPLASMIC RETICULUM INHERITANCE.
RX PubMed=11553703; DOI=10.1091/mbc.12.9.2614;
RA Du Y., Pypaert M., Novick P., Ferro-Novick S.;
RT "Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 12:2614-2628(2001).
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-64; SER-264; SER-308 AND
RP SER-312, AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-264, AND
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-52; SER-64 AND SER-264, AND
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 [10]
RP STRUCTURE BY NMR OF 137-183, AND INTERACTION WITH UBIQUITIN.
RX PubMed=14997574; DOI=10.1002/prot.10636;
RA Chim N., Gall W.E., Xiao J., Harris M.P., Graham T.R., Krezel A.M.;
RT "Solution structure of the ubiquitin-binding domain in Swa2p from
RT Saccharomyces cerevisiae.";
RL Proteins 54:784-793(2004).
RN [11]
RP DOMAINS, INTERACTION WITH CHC1, AND MUTAGENESIS OF GLY-388 AND
RP 631-HIS--ASP-633.
RX PubMed=16687570; DOI=10.1091/mbc.e06-02-0106;
RA Xiao J., Kim L.S., Graham T.R.;
RT "Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70
RT clathrin-uncoating activity in vivo.";
RL Mol. Biol. Cell 17:3281-3290(2006).
CC -!- FUNCTION: Cofactor for the uncoating of clathrin-coated vesicles (CCVs)
CC by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is
CC important for fusion of vesicles with target membranes and for
CC recycling components of clathrin coats to the cytoplasm for further
CC rounds of vesicle formation. Binds to assembled clathrin and recruits
CC the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of
CC the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts
CC clathrin-clathrin interactions, leading to release of the clathrin
CC coat. In addition, prevents unproductive clathrin assembly in the cell.
CC Also required for cortical endoplasmic reticulum inheritance.
CC {ECO:0000269|PubMed:11084334, ECO:0000269|PubMed:11146663,
CC ECO:0000269|PubMed:11553703}.
CC -!- SUBUNIT: Interacts with the clathrin light and heavy chains CLC1 and
CC CHC1, respectively. Binds to clathrin with its N-terminal domain
CC containing 3 clathrin-binding (CB) motifs. Association with clathrin is
CC transient. Binds to polyubiquitin and ubiquitinated proteins.
CC {ECO:0000269|PubMed:11084334, ECO:0000269|PubMed:14997574,
CC ECO:0000269|PubMed:16687570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11084334}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:11084334};
CC Peripheral membrane protein {ECO:0000269|PubMed:11084334}.
CC -!- DOMAIN: The TPR repeats and the J domain are required for interaction
CC with Hsp70-type chaperones. The J domain is responsible for stimulating
CC the ATPase activity of the chaperone. {ECO:0000269|PubMed:16687570}.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U32517; AAB64756.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12161.1; -; Genomic_DNA.
DR PIR; S59786; S59786.
DR RefSeq; NP_010606.1; NM_001180628.1.
DR PDB; 1PGY; NMR; -; A=137-183.
DR PDBsum; 1PGY; -.
DR AlphaFoldDB; Q06677; -.
DR BMRB; Q06677; -.
DR SMR; Q06677; -.
DR BioGRID; 32376; 384.
DR DIP; DIP-2847N; -.
DR IntAct; Q06677; 7.
DR MINT; Q06677; -.
DR STRING; 4932.YDR320C; -.
DR iPTMnet; Q06677; -.
DR MaxQB; Q06677; -.
DR PaxDb; Q06677; -.
DR PRIDE; Q06677; -.
DR EnsemblFungi; YDR320C_mRNA; YDR320C; YDR320C.
DR GeneID; 851918; -.
DR KEGG; sce:YDR320C; -.
DR SGD; S000002728; SWA2.
DR VEuPathDB; FungiDB:YDR320C; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000167056; -.
DR HOGENOM; CLU_005723_2_0_1; -.
DR InParanoid; Q06677; -.
DR OMA; MEIARLM; -.
DR BioCyc; YEAST:G3O-29878-MON; -.
DR EvolutionaryTrace; Q06677; -.
DR PRO; PR:Q06677; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06677; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0072318; P:clathrin coat disassembly; IDA:SGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:SGD.
DR CDD; cd14329; UBA_SWA2p_like; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR015228; SWA2_UBA.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF09145; Ubiq-assoc; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..668
FT /note="Auxilin-like clathrin uncoating factor SWA2"
FT /id="PRO_0000270621"
FT DOMAIN 140..180
FT /note="UBA"
FT REPEAT 374..407
FT /note="TPR 1"
FT REPEAT 412..445
FT /note="TPR 2"
FT REPEAT 467..500
FT /note="TPR 3"
FT DOMAIN 603..668
FT /note="J"
FT REGION 1..100
FT /note="CB1"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..302
FT /note="CB2"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..362
FT /note="CB3"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 388
FT /note="G->R: In SWA2-1/SWA2-TPR; partial loss of clathrin
FT disassembly function. In SWA2-TPR-J; complete loss of
FT clathrin disassembly function; when associated with 631-
FT AAA-633."
FT /evidence="ECO:0000269|PubMed:11084334,
FT ECO:0000269|PubMed:16687570"
FT MUTAGEN 631..633
FT /note="HPD->AAA: In SWA2-J; abolishes ATPase stimulation
FT activity. In SWA2-TPR-J; complete loss of clathrin
FT disassembly function; when associated with R-388."
FT /evidence="ECO:0000269|PubMed:16687570"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:1PGY"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:1PGY"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:1PGY"
SQ SEQUENCE 668 AA; 75020 MW; CCDF1F78315E3D44 CRC64;
MSDPFAHLLT SLKNKDSASA SKETTPQSSN SPSITGSAVA DVARTDKSPN DSLHSISAPP
LIPSPKVDFS APPLVPTNST TKSNTANNTP PSALANTDDD FNQLFGMGTV TTTDTIQKPD
EDYYGSKEDH LYNGDDALVD EVKDMEIARL MSLGLSIEEA TEFYENDVTY ERYLEILKSK
QKERNDLAIR KKESGIKMEK SGLSNIVGTD SNNLFSMATD FFNKGKKLVD QWTSFPPEAN
DRLNNYSKTH DKVEDYDLPQ VNDSPNRILF EDNEVVENLP PADNPDQDLL TDFETKIDIT
KRTAPDVSHS SSPTSGILIE ENSRRNEPLI EDSLLDFSEG NLTNSKSNED STLFNENSNT
DSTIPISDIE LSGYNEFKAK GTSLFKNGDY INSLQEYEKS LNTLPLNHPL RIIALSNIIA
SQLKIGEYSK SIENSSMALE LFPSSKAKWK NKISNSDPER SFNDIWPKIM IRRAESFEHL
ESFKKALETY QELIKKNFFD DKIMQGKRRC QDFINPPPVK KSMPVKKKTT TTSPATKKQN
LTASSSNSPI SVDSTSEIKK RELENAKLAL YDKVFEKISS WKDGKDDDIR HLLANLSSLL
TWCNWKDVSM QDLVMPKRVK ITYMKAVAKT HPDKIPESLS LENKMIAENI FSTLSIAWDK
FKLQNDIN
