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   27-MAR-2024, entry version 186.
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; 208.
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; 4932-YHR114W; -.
DR   PeptideAtlas; P38822; -.
DR   EnsemblFungi; YHR114W_mRNA; YHR114W; YHR114W.
DR   GeneID; 856514; -.
DR   KEGG; sce:YHR114W; -.
DR   AGR; SGD:S000001156; -.
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   OrthoDB; 4260488at2759; -.
DR   BioCyc; YEAST:G3O-31156-MONOMER; -.
DR   BioGRID-ORCS; 856514; 0 hits in 10 CRISPR screens.
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:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0009651; P:response to salt stress; IGI:SGD.
DR   CDD; cd11778; SH3_Bzz1_2; 1.
DR   CDD; cd11777; SH3_CIP4_Bzz1_like; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
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   PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
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; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//