BZZ1_YEAST
ID BZZ1_YEAST Reviewed; 633 AA.
AC P38822; D3DL64; E9P8V2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein BZZ1;
DE AltName: Full=LAS17-binding protein 7;
GN Name=BZZ1; Synonyms=LSB7; OrderedLocusNames=YHR114W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LAS17 AND MYO5.
RX PubMed=12391157; DOI=10.1128/mcb.22.22.7889-7906.2002;
RA Soulard A., Lechler T., Spiridonov V., Shevchenko A., Shevchenko A., Li R.,
RA Winsor B.;
RT "Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin
RT patch polarization and is able to recruit actin-polymerizing machinery in
RT vitro.";
RL Mol. Cell. Biol. 22:7889-7906(2002).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=16231105; DOI=10.1007/s00709-005-0108-4;
RA Soulard A., Friant S., Fitterer C., Orange C., Kaneva G., Mirey G.,
RA Winsor B.;
RT "The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early
RT stage of endocytosis.";
RL Protoplasma 226:89-101(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-463; SER-472 AND
RP SER-476, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463; SER-472 AND SER-476, 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 [9]
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 498-633.
RA Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M.;
RT "Structural genomics of yeast SH3 domains.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in endocytosis and trafficking to the vacuole.
CC Functions with type I myosins to restore polarity of the actin
CC cytoskeleton after NaCl stress. {ECO:0000269|PubMed:12391157,
CC ECO:0000269|PubMed:16231105}.
CC -!- SUBUNIT: Interacts with LAS17 and MYO5. {ECO:0000269|PubMed:12391157}.
CC -!- INTERACTION:
CC P38822; P40563: AIM21; NbExp=7; IntAct=EBI-3889, EBI-25376;
CC P38822; P38266: AIM3; NbExp=2; IntAct=EBI-3889, EBI-21584;
CC P38822; P53933: APP1; NbExp=14; IntAct=EBI-3889, EBI-28798;
CC P38822; P47068: BBC1; NbExp=2; IntAct=EBI-3889, EBI-3437;
CC P38822; Q12446: LAS17; NbExp=17; IntAct=EBI-3889, EBI-10022;
CC P38822; Q12342: LDB17; NbExp=4; IntAct=EBI-3889, EBI-38872;
CC P38822; Q04439: MYO5; NbExp=5; IntAct=EBI-3889, EBI-11687;
CC P38822; P40453: UBP7; NbExp=3; IntAct=EBI-3889, EBI-19857;
CC P38822; Q08989: YPL277C; NbExp=2; IntAct=EBI-3889, EBI-38031;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:12391157}. Note=localizes in cortical actin patches
CC in a LAS17-dependent manner.
CC -!- MISCELLANEOUS: Present with 5440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BZZ1 family. {ECO:0000305}.
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DR EMBL; U00059; AAB68850.1; -; Genomic_DNA.
DR EMBL; AY558108; AAS56434.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06808.1; -; Genomic_DNA.
DR PIR; S48956; S48956.
DR RefSeq; NP_011982.1; NM_001179244.1.
DR PDB; 1ZUU; X-ray; 0.97 A; A=498-552.
DR PDB; 2A28; X-ray; 1.07 A; A/B/C/D=582-633.
DR PDBsum; 1ZUU; -.
DR PDBsum; 2A28; -.
DR AlphaFoldDB; P38822; -.
DR SMR; P38822; -.
DR BioGRID; 36547; 203.
DR DIP; DIP-2143N; -.
DR IntAct; P38822; 84.
DR MINT; P38822; -.
DR STRING; 4932.YHR114W; -.
DR MoonDB; P38822; Predicted.
DR iPTMnet; P38822; -.
DR MaxQB; P38822; -.
DR PaxDb; P38822; -.
DR PRIDE; P38822; -.
DR EnsemblFungi; YHR114W_mRNA; YHR114W; YHR114W.
DR GeneID; 856514; -.
DR KEGG; sce:YHR114W; -.
DR SGD; S000001156; BZZ1.
DR VEuPathDB; FungiDB:YHR114W; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR HOGENOM; CLU_015390_1_0_1; -.
DR InParanoid; P38822; -.
DR OMA; YADGWWE; -.
DR BioCyc; YEAST:G3O-31156-MON; -.
DR EvolutionaryTrace; P38822; -.
DR PRO; PR:P38822; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38822; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IPI:SGD.
DR GO; GO:0045010; P:actin nucleation; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0009651; P:response to salt stress; IGI:SGD.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..633
FT /note="Protein BZZ1"
FT /id="PRO_0000065033"
FT DOMAIN 5..271
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 493..555
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 577..633
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 429..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..210
FT /evidence="ECO:0000255"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 196
FT /note="E -> G (in Ref. 3; AAS56434)"
FT /evidence="ECO:0000305"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:1ZUU"
FT STRAND 527..536
FT /evidence="ECO:0007829|PDB:1ZUU"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:1ZUU"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:1ZUU"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:1ZUU"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:2A28"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:2A28"
FT STRAND 612..620
FT /evidence="ECO:0007829|PDB:2A28"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:2A28"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:2A28"
SQ SEQUENCE 633 AA; 71171 MW; 5C73DACC69611B41 CRC64;
MSADLSIGNE IKDSFKETHK WVQNNLKWLK DIEQFYRERA KLEKDYSERL SRLSAEYFNK
KSSTSVPISV GDTPTTTPGS IEAAGVVAWN EILSQTDMIS KDHDQLSTDF ENHVANQLSG
LFTKLDMTLS KINGFNNDMV NKKDNIYHEL EKAKKDYDEA CSTMEMARNR YTKASNDRNK
KKLDEKEMEM NKCKNEYLIK INQANRTKDK YYFQDVPEVL DLLQDVNEAK TLFLNDLWLK
AASVENDLGA NVSKRLQAAN SVVKQNKPSL NTAIFIKHNL KNWKEPQDFV YKPSPVWHDD
EKFAVPSSLE VEDLRIKLAK AENDYNSLQD KTQNELSKLS TLNKIKHEMK TNEDNINATK
FYDTLKEYLN VVSPFTSHET LKLQAEVQIE SIQNNVPEEY DLSTDNIDLS KTKKKSGIFS
KFKHNILNVD SKPSSGGSTG NGNGGPLHIT SLFNTSRRTR LGSAPNNAGE DSDNNSIRTT
STNNTKKTTQ NSSDDGKNKV LYAYVQKDDD EITITPGDKI SLVARDTGSG WTKINNDTTG
ETGLVPTTYI RISSAATVKA NDRGPAPEVP PPRRSTLPVR TMEAIYAYEA QGDDEISIDP
GDIITVIRGD DGSGWTYGEC DGLKGLFPTS YCK
