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   04-NOV-2026, entry version 203.
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=9; 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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   SMR; P47068; -.
DR   BioGRID; 33738; 206.
DR   DIP; DIP-6279N; -.
DR   IntAct; P47068; 82.
DR   STRING; 4932.YJL020C; -.
DR   MoonDB; P47068; Predicted.
DR   GlyCosmos; P47068; 4 sites, 1 glycan.
DR   GlyGen; P47068; 12 sites, 1 O-linked glycan (11 sites).
DR   iPTMnet; P47068; -.
DR   PaxDb; 4932-YJL020C; -.
DR   PeptideAtlas; P47068; -.
DR   EnsemblFungi; YJL020C_mRNA; YJL020C; YJL020C.
DR   GeneID; 853433; -.
DR   KEGG; sce:YJL020C; -.
DR   VEuPathDB; FungiDB:YJL020C; -.
DR   AGR; SGD:S000003557; -.
DR   SGD; S000003557; BBC1.
DR   eggNOG; ENOG502QQMM; Eukaryota.
DR   HOGENOM; CLU_003021_0_0_1; -.
DR   InParanoid; P47068; -.
DR   OMA; AAGSQWW; -.
DR   OrthoDB; 207120at2759; -.
DR   BioCyc; YEAST:G3O-31492-MONOMER; -.
DR   EvolutionaryTrace; P47068; -.
DR   PRO; PR:P47068; -.
DR   CDD; cd11887; SH3_Bbc1; 1.
DR   FunFam; 2.30.30.40:FF:000316; Myosin tail region-interacting protein MTI1; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR057402; AIM3_BBC1_C.
DR   InterPro; IPR035552; Mti1_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR46026; RHO-TYPE GUANINE NUCLEOTIDE EXCHANGE FACTOR, ISOFORM F; 1.
DR   PANTHER; PTHR46026:SF1; RHO-TYPE GUANINE NUCLEOTIDE EXCHANGE FACTOR, ISOFORM F; 1.
DR   Pfam; PF25459; AIM3_BBC1_C; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0017024; F:myosin I binding; IPI:UniProtKB.
DR   GO; GO:0032032; F:myosin I tail binding; IDA:SGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR   GO; GO:0007010; P:cytoskeleton organization; IGI:UniProtKB.
DR   GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47068; protein.
DR   BioGRID-ORCS; 853433; 8 hits in 10 CRISPR screens.
DR   AlphaFoldDB; P47068; -.
DR   MDposit; P47068; -.
DR   FunCoup; P47068; 261.
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        77..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..149
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..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..411
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..558
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..585
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..668
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..738
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..765
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..808
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..853
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"
FT   HELIX           798..801
FT                   /evidence="ECO:0007829|PDB:2DYF"
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
//