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Auxilin-like clathrin uncoating factor SWA2 (Bud site selection protein 24) (DnaJ-related protein SWA2) (J protein SWA2) (Synthetic lethal with ARF1 protein 2)

 SWA2_YEAST              Reviewed;         668 AA.
Q06677; D6VSV1;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Auxilin-like clathrin uncoating factor SWA2;
AltName: Full=Bud site selection protein 24;
AltName: Full=DnaJ-related protein SWA2;
Short=J protein SWA2;
AltName: Full=Synthetic lethal with ARF1 protein 2;
Name=SWA2; Synonyms=AUX1, BUD24; OrderedLocusNames=YDR320C;
ORFNames=D9798.10;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF
GLY-388, AND INTERACTION WITH CLC1.
PubMed=11084334; DOI=10.1016/S0960-9822(00)00771-5;
Gall W.E., Higginbotham M.A., Chen C.-Y., Ingram M.F., Cyr D.M.,
Graham T.R.;
"The auxilin-like phosphoprotein Swa2p is required for clathrin
function in yeast.";
Curr. Biol. 10:1349-1358(2000).
[4]
FUNCTION.
PubMed=11146663; DOI=10.1038/35046619;
Pishvaee B., Costaguta G., Yeung B.G., Ryazantsev S., Greener T.,
Greene L.E., Eisenberg E., McCaffery J.M., Payne G.S.;
"A yeast DNA J protein required for uncoating of clathrin-coated
vesicles in vivo.";
Nat. Cell Biol. 2:958-963(2000).
[5]
FUNCTION IN ENDOPLASMIC RETICULUM INHERITANCE.
PubMed=11553703; DOI=10.1091/mbc.12.9.2614;
Du Y., Pypaert M., Novick P., Ferro-Novick S.;
"Aux1p/Swa2p is required for cortical endoplasmic reticulum
inheritance in Saccharomyces cerevisiae.";
Mol. Biol. Cell 12:2614-2628(2001).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-264; SER-308 AND
SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-264, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-64 AND SER-264,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[10]
STRUCTURE BY NMR OF 137-183, AND INTERACTION WITH UBIQUITIN.
PubMed=14997574; DOI=10.1002/prot.10636;
Chim N., Gall W.E., Xiao J., Harris M.P., Graham T.R., Krezel A.M.;
"Solution structure of the ubiquitin-binding domain in Swa2p from
Saccharomyces cerevisiae.";
Proteins 54:784-793(2004).
[11]
DOMAINS, INTERACTION WITH CHC1, AND MUTAGENESIS OF GLY-388 AND
631-HIS--ASP-633.
PubMed=16687570; DOI=10.1091/mbc.E06-02-0106;
Xiao J., Kim L.S., Graham T.R.;
"Dissection of Swa2p/auxilin domain requirements for cochaperoning
Hsp70 clathrin-uncoating activity in vivo.";
Mol. Biol. Cell 17:3281-3290(2006).
-!- FUNCTION: Cofactor for the uncoating of clathrin-coated vesicles
(CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat
disassembly is important for fusion of vesicles with target
membranes and for recycling components of clathrin coats to the
cytoplasm for further rounds of vesicle formation. Binds to
assembled clathrin and recruits the ATP-activated chaperone to
CCVs. Stimulates the ATPase activity of the clathrin-associated
Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin
interactions, leading to release of the clathrin coat. In
addition, prevents unproductive clathrin assembly in the cell.
Also required for cortical endoplasmic reticulum inheritance.
{ECO:0000269|PubMed:11084334, ECO:0000269|PubMed:11146663,
ECO:0000269|PubMed:11553703}.
-!- SUBUNIT: Interacts with the clathrin light and heavy chains CLC1
and CHC1, respectively. Binds to clathrin with its N-terminal
domain containing 3 clathrin-binding (CB) motifs. Association with
clathrin is transient. Binds to polyubiquitin and ubiquitinated
proteins. {ECO:0000269|PubMed:11084334,
ECO:0000269|PubMed:14997574, ECO:0000269|PubMed:16687570}.
-!- INTERACTION:
Q12250:RPN5; NbExp=4; IntAct=EBI-30084, EBI-15935;
P11484:SSB1; NbExp=3; IntAct=EBI-30084, EBI-8627;
Q12049:THP3; NbExp=4; IntAct=EBI-30084, EBI-34263;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11084334}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:11084334};
Peripheral membrane protein {ECO:0000269|PubMed:11084334}.
-!- DOMAIN: The TPR repeats and the J domain are required for
interaction with Hsp70-type chaperones. The J domain is
responsible for stimulating the ATPase activity of the chaperone.
{ECO:0000269|PubMed:16687570}.
-!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U32517; AAB64756.1; -; Genomic_DNA.
EMBL; BK006938; DAA12161.1; -; Genomic_DNA.
PIR; S59786; S59786.
RefSeq; NP_010606.1; NM_001180628.1.
PDB; 1PGY; NMR; -; A=137-183.
PDBsum; 1PGY; -.
ProteinModelPortal; Q06677; -.
SMR; Q06677; -.
BioGrid; 32376; 379.
DIP; DIP-2847N; -.
IntAct; Q06677; 321.
MINT; Q06677; -.
STRING; 4932.YDR320C; -.
iPTMnet; Q06677; -.
MaxQB; Q06677; -.
PaxDb; Q06677; -.
PRIDE; Q06677; -.
EnsemblFungi; YDR320C; YDR320C; YDR320C.
GeneID; 851918; -.
KEGG; sce:YDR320C; -.
EuPathDB; FungiDB:YDR320C; -.
SGD; S000002728; SWA2.
HOGENOM; HOG000001055; -.
InParanoid; Q06677; -.
OMA; SGYNEFK; -.
OrthoDB; EOG092C1MUD; -.
BioCyc; YEAST:G3O-29878-MONOMER; -.
EvolutionaryTrace; Q06677; -.
PRO; PR:Q06677; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0031982; C:vesicle; IBA:GO_Central.
GO; GO:0030276; F:clathrin binding; IDA:SGD.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0072318; P:clathrin coat disassembly; IDA:SGD.
GO; GO:0048309; P:endoplasmic reticulum inheritance; IMP:SGD.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:SGD.
GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
CDD; cd14329; UBA_SWA2p_like; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR015228; SWA2_UBA.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
InterPro; IPR009060; UBA-like_sf.
Pfam; PF09145; Ubiq-assoc; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Membrane; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
CHAIN 1 668 Auxilin-like clathrin uncoating factor
SWA2.
/FTId=PRO_0000270621.
DOMAIN 140 180 UBA.
REPEAT 374 407 TPR 1.
REPEAT 412 445 TPR 2.
REPEAT 467 500 TPR 3.
DOMAIN 603 668 J.
REGION 1 100 CB1.
REGION 238 302 CB2.
REGION 303 362 CB3.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MUTAGEN 388 388 G->R: In SWA2-1/SWA2-TPR; partial loss of
clathrin disassembly function. In SWA2-
TPR-J; complete loss of clathrin
disassembly function; when associated
with 631-AAA-633.
{ECO:0000269|PubMed:11084334,
ECO:0000269|PubMed:16687570}.
MUTAGEN 631 633 HPD->AAA: In SWA2-J; abolishes ATPase
stimulation activity. In SWA2-TPR-J;
complete loss of clathrin disassembly
function; when associated with R-388.
{ECO:0000269|PubMed:16687570}.
HELIX 140 153 {ECO:0000244|PDB:1PGY}.
HELIX 158 167 {ECO:0000244|PDB:1PGY}.
HELIX 171 179 {ECO:0000244|PDB:1PGY}.
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


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