BBC1_YEAST
ID BBC1_YEAST Reviewed; 1157 AA.
AC P47068; D6VWG0; P47067; Q8X1F4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Myosin tail region-interacting protein MTI1;
DE AltName: Full=Protein BBC1;
GN Name=BBC1; Synonyms=MTI1; OrderedLocusNames=YJL020C;
GN ORFNames=J1286, J1305, YJL021C;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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] OF 699-765, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11901111; DOI=10.1093/genetics/160.3.923;
RA Mochida J., Yamamoto T., Fujimura-Kamada K., Tanaka K.;
RT "The novel adaptor protein, Mti1p, and Vrp1p, a homolog of Wiskott-Aldrich
RT syndrome protein-interacting protein (WIP), may antagonistically regulate
RT type I myosins in Saccharomyces cerevisiae.";
RL Genetics 160:923-934(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1157.
RA Pohl T.M., Aljinovic G.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-158; SER-166;
RP SER-565; SER-621; SER-631; SER-634; SER-638; THR-894 AND THR-895, AND
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-158 AND SER-889, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-166; SER-565 AND
RP SER-647, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-158; SER-166;
RP SER-565; SER-621; SER-631; SER-634; THR-636; SER-638; SER-647; THR-850;
RP THR-894 AND THR-895, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1012, 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: Involved in the regulation of actin cytoskeleton.
CC {ECO:0000269|PubMed:11901111}.
CC -!- SUBUNIT: Binds to the SH3 domains of the type I myosins MYO3 and MYO5.
CC {ECO:0000269|PubMed:11901111}.
CC -!- INTERACTION:
CC P47068; P40563: AIM21; NbExp=8; IntAct=EBI-3437, EBI-25376;
CC P47068; P53933: APP1; NbExp=3; IntAct=EBI-3437, EBI-28798;
CC P47068; P38822: BZZ1; NbExp=2; IntAct=EBI-3437, EBI-3889;
CC P47068; P36006: MYO3; NbExp=5; IntAct=EBI-3437, EBI-11670;
CC P47068; Q04439: MYO5; NbExp=6; IntAct=EBI-3437, EBI-11687;
CC P47068; Q06833: NVJ2; NbExp=2; IntAct=EBI-3437, EBI-37290;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11901111}. Note=Colocalizes with cortical actin
CC patches.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA89311.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA89312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z49295; CAA89311.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z49296; CAA89312.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF373805; AAL57239.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08776.1; -; Genomic_DNA.
DR PIR; S56791; S56791.
DR PIR; S56792; S56792.
DR RefSeq; NP_012514.2; NM_001181454.1.
DR PDB; 1TG0; X-ray; 0.97 A; A=1-68.
DR PDB; 1WDX; X-ray; 2.50 A; A/B/C/D=1-68.
DR PDB; 1ZUK; X-ray; 1.90 A; A/B=1-68.
DR PDB; 2DYF; NMR; -; B=796-802.
DR PDBsum; 1TG0; -.
DR PDBsum; 1WDX; -.
DR PDBsum; 1ZUK; -.
DR PDBsum; 2DYF; -.
DR AlphaFoldDB; P47068; -.
DR SMR; P47068; -.
DR BioGRID; 33738; 193.
DR DIP; DIP-6279N; -.
DR IntAct; P47068; 79.
DR MINT; P47068; -.
DR STRING; 4932.YJL020C; -.
DR MoonDB; P47068; Predicted.
DR iPTMnet; P47068; -.
DR MaxQB; P47068; -.
DR PaxDb; P47068; -.
DR PRIDE; P47068; -.
DR EnsemblFungi; YJL020C_mRNA; YJL020C; YJL020C.
DR GeneID; 853433; -.
DR KEGG; sce:YJL020C; -.
DR SGD; S000003557; BBC1.
DR VEuPathDB; FungiDB:YJL020C; -.
DR eggNOG; ENOG502QQMM; Eukaryota.
DR HOGENOM; CLU_003021_0_0_1; -.
DR InParanoid; P47068; -.
DR OMA; IEDNQWY; -.
DR BioCyc; YEAST:G3O-31492-MON; -.
DR EvolutionaryTrace; P47068; -.
DR PRO; PR:P47068; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47068; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0017024; F:myosin I binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IGI:UniProtKB.
DR CDD; cd11887; SH3_Bbc1; 1.
DR InterPro; IPR030506; Mti1.
DR InterPro; IPR035552; Mti1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15629:SF32; PTHR15629:SF32; 2.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Phosphoprotein; Reference proteome; SH3 domain; Ubl conjugation.
FT CHAIN 1..1157
FT /note="Myosin tail region-interacting protein MTI1"
FT /id="PRO_0000064839"
FT DOMAIN 5..69
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 68..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..301
FT /evidence="ECO:0000255"
FT COILED 356..430
FT /evidence="ECO:0000255"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 850
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 895
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 1012
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:1TG0"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1WDX"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:1TG0"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:1TG0"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1TG0"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1TG0"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1TG0"
SQ SEQUENCE 1157 AA; 128297 MW; 88A5899B89CCE8ED CRC64;
MSEPEVPFKV VAQFPYKSDY EDDLNFEKDQ EIIVTSVEDA EWYFGEYQDS NGDVIEGIFP
KSFVAVQGSE VGKEAESSPN TGSTEQRTIQ PEVEQKDLPE PISPETKKET LSGPVPVPAA
TVPVPAATVP VPAATAVSAQ VQHDSSSGNG ERKVPMDSPK LKARLSMFNQ DITEQVPLPK
STHLDLENIP VKKTIVADAP KYYVPPGIPT NDTSNLERKK SLKENEKKIV PEPINRAQVE
SGRIETENDQ LKKDLPQMSL KERIALLQEQ QRLQAAREEE LLRKKAKLEQ EHERSAVNKN
EPYTETEEAE ENEKTEPKPE FTPETEHNEE PQMELLAHKE ITKTSREADE GTNDIEKEQF
LDEYTKENQK VEESQADEAR GENVAEESEI GYGHEDREGD NDEEKEEEDS EENRRAALRE
RMAKLSGASR FGAPVGFNPF GMASGVGNKP SEEPKKKQHK EKEEEEPEQL QELPRAIPVM
PFVDPSSNPF FRKSNLSEKN QPTETKTLDP HATTEHEQKQ EHGTHAYHNL AAVDNAHPEY
SDHDSDEDTD DHEFEDANDG LRKHSMVEQA FQIGNNESEN VNSGEKIYPQ EPPISHRTAE
VSHDIENSSQ NTTGNVLPVS SPQTRVARNG SINSLTKSIS GENRRKSINE YHDTVSTNSS
ALTETAQDIS MAAPAAPVLS KVSHPEDKVP PHPVPSAPSA PPVPSAPSVP SAPPVPPAPP
ALSAPSVPPV PPVPPVSSAP PALSAPSIPP VPPTPPAPPA PPAPLALPKH NEVEEHVKSS
APLPPVSEEY HPMPNTAPPL PRAPPVPPAT FEFDSEPTAT HSHTAPSPPP HQNVTASTPS
MMSTQQRVPT SVLSGAEKES RTLPPHVPSL TNRPVDSFHE SDTTPKVASI RRSTTHDVGE
ISNNVKIEFN AQERWWINKS APPAISNLKL NFLMEIDDHF ISKRLHQKWV VRDFYFLFEN
YSQLRFSLTF NSTSPEKTVT TLQERFPSPV ETQSARILDE YAQRFNAKVV EKSHSLINSH
IGAKNFVSQI VSEFKDEVIQ PIGARTFGAT ILSYKPEEGI EQLMKSLQKI KPGDILVIRK
AKFEAHKKIG KNEIINVGMD SAAPYSSVVT DYDFTKNKFR VIENHEGKII QNSYKLSHMK
SGKLKVFRIV ARGYVGW
