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Q03640

- TCB3_YEAST

UniProt

Q03640 - TCB3_YEAST

Protein

Tricalbin-3

Gene

TCB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    May play a role in membrane trafficking.2 Publications

    Cofactori

    Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1150 – 11501Calcium 1By similarity
    Metal bindingi1150 – 11501Calcium 2By similarity
    Metal bindingi1156 – 11561Calcium 1By similarity
    Metal bindingi1204 – 12041Calcium 1By similarity
    Metal bindingi1204 – 12041Calcium 2By similarity
    Metal bindingi1206 – 12061Calcium 1By similarity
    Metal bindingi1206 – 12061Calcium 2By similarity
    Metal bindingi1206 – 12061Calcium 3By similarity
    Metal bindingi1212 – 12121Calcium 2By similarity
    Metal bindingi1212 – 12121Calcium 3By similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB-KW
    2. lipid binding Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. endoplasmic reticulum membrane organization Source: SGD
    2. regulation of phosphatidylinositol dephosphorylation Source: SGD

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding, Lipid-binding, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32666-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tricalbin-3
    Gene namesi
    Name:TCB3
    Ordered Locus Names:YML072C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML072c.
    SGDiS000004537. TCB3.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. cellular bud Source: SGD
    2. cortical endoplasmic reticulum Source: SGD
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15451545Tricalbin-3PRO_0000203249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei112 – 1121Phosphoserine1 Publication
    Modified residuei1340 – 13401Phosphoserine1 Publication
    Modified residuei1342 – 13421Phosphoserine1 Publication
    Modified residuei1346 – 13461Phosphoserine1 Publication
    Modified residuei1350 – 13501Phosphothreonine4 Publications
    Modified residuei1354 – 13541Phosphoserine1 Publication
    Modified residuei1400 – 14001Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03640.
    PaxDbiQ03640.
    PeptideAtlasiQ03640.

    Expressioni

    Gene expression databases

    GenevestigatoriQ03640.

    Interactioni

    Subunit structurei

    Interacts with TCB2 via its C-terminal domain.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself1EBI-27872,EBI-27872
    DIP5P533881EBI-27872,EBI-5904
    DUR3P334131EBI-27872,EBI-2060312
    FLC1Q089671EBI-27872,EBI-36673
    FMP45Q076511EBI-27872,EBI-2051056
    FTR1P400881EBI-27872,EBI-7138
    GPA2P108231EBI-27872,EBI-7382
    HNM1P198071EBI-27872,EBI-8409
    HSP30P256191EBI-27872,EBI-8563
    HXT1P324651EBI-27872,EBI-8759
    HXT2P235851EBI-27872,EBI-2054100
    HXT3P324661EBI-27872,EBI-8770
    HXT5P386951EBI-27872,EBI-8778
    HXT7P390041EBI-27872,EBI-8790
    IST2P382501EBI-27872,EBI-21520
    ITR1P306051EBI-27872,EBI-2050956
    MEP1P402601EBI-27872,EBI-10714
    MEP3P533901EBI-27872,EBI-10729
    MID2P360271EBI-27872,EBI-10901
    MUP1P502761EBI-27872,EBI-11624
    OSH7P387551EBI-27872,EBI-12641
    PDR12Q027851EBI-27872,EBI-13065
    PHO84P252971EBI-27872,EBI-13320
    PIS1P061971EBI-27872,EBI-13458
    PLM2Q043831EBI-27872,EBI-2079237
    PMP2P409751EBI-27872,EBI-2043041
    PMP3P872841EBI-27872,EBI-13555
    PST2Q123351EBI-27872,EBI-14064
    QDR2P404741EBI-27872,EBI-25203
    RFS1P382341EBI-27872,EBI-21445
    RIM1P324451EBI-27872,EBI-15206
    RSN1Q035161EBI-27872,EBI-27593
    RTN1Q049471EBI-27872,EBI-38020
    SDS23P531721EBI-27872,EBI-23782
    SFK1P357351EBI-27872,EBI-26678
    SNQ2P325681EBI-27872,EBI-17590
    TCB1Q124661EBI-27872,EBI-34614
    TCB2P482311EBI-27872,EBI-28779
    TPO1Q078241EBI-27872,EBI-38106
    TPO2P532831EBI-27872,EBI-2044753
    TPO3Q064511EBI-27872,EBI-34275
    TPO4Q122561EBI-27872,EBI-37213
    VHT1P532411EBI-27872,EBI-20297
    WSC2P538321EBI-27872,EBI-2055941
    WSC3Q122151EBI-27872,EBI-20551
    YBL029C-AQ3E7561EBI-27872,EBI-2044812
    YLR326WQ061701EBI-27872,EBI-35994
    YLR413WQ066891EBI-27872,EBI-38659
    YOP1Q124021EBI-27872,EBI-37092
    YOR1P530491EBI-27872,EBI-29324

    Protein-protein interaction databases

    BioGridi35069. 88 interactions.
    DIPiDIP-6589N.
    IntActiQ03640. 62 interactions.
    MINTiMINT-667993.
    STRINGi4932.YML072C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03640.
    SMRiQ03640. Positions 478-736, 1053-1223.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 206206CytoplasmicBy similarityAdd
    BLAST
    Topological domaini228 – 2281ExtracellularBy similarity
    Topological domaini250 – 15451296CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei207 – 22721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei229 – 24921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini478 – 580103C2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini785 – 88197C2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1121 – 121898C2 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili620 – 66041Sequence AnalysisAdd
    BLAST
    Coiled coili937 – 97236Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1316 – 140489Ser-richAdd
    BLAST

    Domaini

    The C-terminal C2 domain shows Ca2+-dependent phospholipid binding. It binds to phosphatidylserine, phosphatidylinositol and various phosphoinositides. The other C2 domains do not retain all 5 conserved Asp residues found in calcium-binding C2 domains.

    Sequence similaritiesi

    Belongs to the tricalbin family.Curated
    Contains 3 C2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5038.
    GeneTreeiENSGT00730000113103.
    HOGENOMiHOG000093250.
    OMAiFWVIYMP.
    OrthoDBiEOG7TQV86.

    Family and domain databases

    Gene3Di2.60.40.150. 4 hits.
    InterProiIPR000008. C2_dom.
    IPR017147. Tricalbin.
    [Graphical view]
    PfamiPF00168. C2. 5 hits.
    [Graphical view]
    PIRSFiPIRSF037232. Tricalbin. 1 hit.
    SMARTiSM00239. C2. 5 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 5 hits.
    PROSITEiPS50004. C2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q03640-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGIKAQVHP PPDSTLFHEE EKKKVGGNLP QKVINQQERG SDHAPSGHHQ     50
    YHQLINHDAN DTKTSNSVSD VSKGQKTADS NPEGKKQSSK DIFVASSAQK 100
    TNQLPGPNPQ GSIGAVPLEG LRPKEFRSAP SRKPNKFDTS ITKPGVLDDL 150
    GKLDEKDIKE KFHLDSDDKL FPWQNVGEFH ASGKGSPNTK MSRVIKAYIL 200
    ENFYNDWYCN IATVLGTCFF SWLFAYIGFS WWSMIFIFLG TATVYNAEYT 250
    RFNRNIRDDL KRVTVEETLS DRVESTTWLN SFLSKFWVIY MPVLSQQVKD 300
    NVNPQLAGVA PGYGIDALAI DEFTLGSKAP TIKGIKSYTK TGKNTVEMDW 350
    SFAFTPSDVS DMTATEAREK INPKISLGVT LGKSFVSKTM PILVEDINVA 400
    GKMRIKVEFG KAFPNIKIVS LQLLEPPLID FALKPIGGDT LGLDVMSFLP 450
    GLKSFVKNII NSNIGPMLFP PNHLDINVED IMAAQSKEAI GVLAVTIASA 500
    DSLKGSDFIT NTVDPYIVMT TEDAVPGTDE EVRTSIKSNV KNPRWNETKY 550
    LLLNTLEQKL NLKCFDFNDV RKDTVIGDLQ LDLADLLQNP VLDNQTAELR 600
    SGTKSKGILH YSLHWFPVKE DKSEEKAVER AEAKAKGKKE DENEDTTEKE 650
    EDENEESSQT DVGIAKITLQ KVKYLDTTSS MTGSLSPCAE LFIDGQKVKS 700
    YRTLRRINEP SWNETIEVLV PSKSNSKFVL KIFDDRMNGK ALICEYSSSL 750
    DDIMTTLDTA QEFVKGSPQG DIYLDVSWKS IEMTGAFAAA NSVSEPIGCI 800
    KLDVKDAIIK GDLSGVGDVD PYYTVSLNRR VLYKSIYHSD TDHPIFDNST 850
    YVPIFSPNQI LTLEFHDYQK IGKDRFIGSV QIPTSNVFKK DPKSGKYVGN 900
    NGKEEISKLK LKDHEHKVTE SIVNVSTTFI PINLVYSPEE LVNVEKLEKE 950
    LKEKKKKFEA TQEENEQEME KNPKEWEVAE IEDPFDSDEK KINRKAKLSL 1000
    NELIKQKSGI LSMQILEGTL SPSSAYLEIL ADDISYPVFI CMKPSQGKLN 1050
    SEMANIFIRD LNYSKLHFRV SKKHIAKDSD DVISETSYST LKLLKQAYEE 1100
    PMWLNFNGSK MKVRFLYTPT SVKLPSSESV EDTGYLNIKL ISGHGLKSAD 1150
    RNGYSDPFVH IFVNDKKVFK SNIKKKTLDP VWNEDAKIPI LSRSKNQVIF 1200
    NVLDWDRAGD NDDLGQASLD VSSLEVGKTY NWNLNLNTQG SIKLQGSFNP 1250
    EYIKPSFDIV KGGITDKPMK IASGAAHATV GIAGTGIGAA TGVATGGLKK 1300
    GGHLLKSLGG NPMKRSKSSN GNESNGAKKS SEKKSFDRRS PSNLNSTSVT 1350
    PRASLDYDPS VPNTSYAPVQ SASPVVKPTD NTSSSSNKKD TPSSNSRGHS 1400
    RASSFARTLA PHGTYNGFIT VVAAENVAKH VQIKISLTQG GRLKHIYKTK 1450
    SQKANNDGVA VFDEECSFKA SPEANLVLGA ISHQRLSRDK DLGIAQINLG 1500
    DPQIQQDGQI SVKLGDGHLI VKINYGKDKN GQVPPVPEVP QEYTQ 1545
    Length:1,545
    Mass (Da):171,076
    Last modified:November 1, 1997 - v1
    Checksum:i77A0AE57F9259784
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46373 Genomic DNA. Translation: CAA86506.1.
    BK006946 Genomic DNA. Translation: DAA09825.1.
    PIRiS48824.
    RefSeqiNP_013639.1. NM_001182431.1.

    Genome annotation databases

    EnsemblFungiiYML072C; YML072C; YML072C.
    GeneIDi854903.
    KEGGisce:YML072C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46373 Genomic DNA. Translation: CAA86506.1 .
    BK006946 Genomic DNA. Translation: DAA09825.1 .
    PIRi S48824.
    RefSeqi NP_013639.1. NM_001182431.1.

    3D structure databases

    ProteinModelPortali Q03640.
    SMRi Q03640. Positions 478-736, 1053-1223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35069. 88 interactions.
    DIPi DIP-6589N.
    IntActi Q03640. 62 interactions.
    MINTi MINT-667993.
    STRINGi 4932.YML072C.

    Proteomic databases

    MaxQBi Q03640.
    PaxDbi Q03640.
    PeptideAtlasi Q03640.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML072C ; YML072C ; YML072C .
    GeneIDi 854903.
    KEGGi sce:YML072C.

    Organism-specific databases

    CYGDi YML072c.
    SGDi S000004537. TCB3.

    Phylogenomic databases

    eggNOGi COG5038.
    GeneTreei ENSGT00730000113103.
    HOGENOMi HOG000093250.
    OMAi FWVIYMP.
    OrthoDBi EOG7TQV86.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32666-MONOMER.

    Miscellaneous databases

    NextBioi 977885.

    Gene expression databases

    Genevestigatori Q03640.

    Family and domain databases

    Gene3Di 2.60.40.150. 4 hits.
    InterProi IPR000008. C2_dom.
    IPR017147. Tricalbin.
    [Graphical view ]
    Pfami PF00168. C2. 5 hits.
    [Graphical view ]
    PIRSFi PIRSF037232. Tricalbin. 1 hit.
    SMARTi SM00239. C2. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 5 hits.
    PROSITEi PS50004. C2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "The tricalbin C2 domains: lipid-binding properties of a novel, synaptotagmin-like yeast protein family."
      Schulz T.A., Creutz C.E.
      Biochemistry 43:3987-3995(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
    6. "Characterization of the yeast tricalbins: membrane-bound multi-C2-domain proteins that form complexes involved in membrane trafficking."
      Creutz C.E., Snyder S.L., Schulz T.A.
      Cell. Mol. Life Sci. 61:1208-1220(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TCB2.
    7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-112 AND THR-1350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1340; SER-1342; SER-1346; THR-1350; SER-1354 AND SER-1400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTCB3_YEAST
    AccessioniPrimary (citable) accession number: Q03640
    Secondary accession number(s): D6VZA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4280 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3