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Protein

Tricalbin-3

Gene

TCB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in membrane trafficking.2 Publications

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domains.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

  • calcium-dependent phospholipid binding Source: UniProtKB-KW
  • lipid binding Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • endoplasmic reticulum membrane organization Source: SGD
  • regulation of phosphatidylinositol dephosphorylation Source: SGD
Complete GO annotation...

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML072C.
SGDiS000004537. TCB3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 206206CytoplasmicBy similarityAdd
BLAST
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Topological domaini228 – 2281ExtracellularBy similarity
Transmembranei229 – 24921HelicalSequence analysisAdd
BLAST
Topological domaini250 – 15451296CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • cellular bud Source: SGD
  • cortical endoplasmic reticulum Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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 – 671PhosphoserineCombined sources
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei1340 – 13401PhosphoserineCombined sources
Modified residuei1342 – 13421PhosphoserineCombined sources
Modified residuei1346 – 13461PhosphoserineCombined sources
Modified residuei1350 – 13501PhosphothreonineCombined sources
Modified residuei1354 – 13541PhosphoserineCombined sources
Modified residuei1400 – 14001PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03640.
PeptideAtlasiQ03640.

PTM databases

iPTMnetiQ03640.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi35069. 89 interactions.
DIPiDIP-6589N.
IntActiQ03640. 62 interactions.
MINTiMINT-667993.

Structurei

3D structure databases

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

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

GeneTreeiENSGT00730000113103.
HOGENOMiHOG000093250.
InParanoidiQ03640.
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

        10         20         30         40         50
MTGIKAQVHP PPDSTLFHEE EKKKVGGNLP QKVINQQERG SDHAPSGHHQ
60 70 80 90 100
YHQLINHDAN DTKTSNSVSD VSKGQKTADS NPEGKKQSSK DIFVASSAQK
110 120 130 140 150
TNQLPGPNPQ GSIGAVPLEG LRPKEFRSAP SRKPNKFDTS ITKPGVLDDL
160 170 180 190 200
GKLDEKDIKE KFHLDSDDKL FPWQNVGEFH ASGKGSPNTK MSRVIKAYIL
210 220 230 240 250
ENFYNDWYCN IATVLGTCFF SWLFAYIGFS WWSMIFIFLG TATVYNAEYT
260 270 280 290 300
RFNRNIRDDL KRVTVEETLS DRVESTTWLN SFLSKFWVIY MPVLSQQVKD
310 320 330 340 350
NVNPQLAGVA PGYGIDALAI DEFTLGSKAP TIKGIKSYTK TGKNTVEMDW
360 370 380 390 400
SFAFTPSDVS DMTATEAREK INPKISLGVT LGKSFVSKTM PILVEDINVA
410 420 430 440 450
GKMRIKVEFG KAFPNIKIVS LQLLEPPLID FALKPIGGDT LGLDVMSFLP
460 470 480 490 500
GLKSFVKNII NSNIGPMLFP PNHLDINVED IMAAQSKEAI GVLAVTIASA
510 520 530 540 550
DSLKGSDFIT NTVDPYIVMT TEDAVPGTDE EVRTSIKSNV KNPRWNETKY
560 570 580 590 600
LLLNTLEQKL NLKCFDFNDV RKDTVIGDLQ LDLADLLQNP VLDNQTAELR
610 620 630 640 650
SGTKSKGILH YSLHWFPVKE DKSEEKAVER AEAKAKGKKE DENEDTTEKE
660 670 680 690 700
EDENEESSQT DVGIAKITLQ KVKYLDTTSS MTGSLSPCAE LFIDGQKVKS
710 720 730 740 750
YRTLRRINEP SWNETIEVLV PSKSNSKFVL KIFDDRMNGK ALICEYSSSL
760 770 780 790 800
DDIMTTLDTA QEFVKGSPQG DIYLDVSWKS IEMTGAFAAA NSVSEPIGCI
810 820 830 840 850
KLDVKDAIIK GDLSGVGDVD PYYTVSLNRR VLYKSIYHSD TDHPIFDNST
860 870 880 890 900
YVPIFSPNQI LTLEFHDYQK IGKDRFIGSV QIPTSNVFKK DPKSGKYVGN
910 920 930 940 950
NGKEEISKLK LKDHEHKVTE SIVNVSTTFI PINLVYSPEE LVNVEKLEKE
960 970 980 990 1000
LKEKKKKFEA TQEENEQEME KNPKEWEVAE IEDPFDSDEK KINRKAKLSL
1010 1020 1030 1040 1050
NELIKQKSGI LSMQILEGTL SPSSAYLEIL ADDISYPVFI CMKPSQGKLN
1060 1070 1080 1090 1100
SEMANIFIRD LNYSKLHFRV SKKHIAKDSD DVISETSYST LKLLKQAYEE
1110 1120 1130 1140 1150
PMWLNFNGSK MKVRFLYTPT SVKLPSSESV EDTGYLNIKL ISGHGLKSAD
1160 1170 1180 1190 1200
RNGYSDPFVH IFVNDKKVFK SNIKKKTLDP VWNEDAKIPI LSRSKNQVIF
1210 1220 1230 1240 1250
NVLDWDRAGD NDDLGQASLD VSSLEVGKTY NWNLNLNTQG SIKLQGSFNP
1260 1270 1280 1290 1300
EYIKPSFDIV KGGITDKPMK IASGAAHATV GIAGTGIGAA TGVATGGLKK
1310 1320 1330 1340 1350
GGHLLKSLGG NPMKRSKSSN GNESNGAKKS SEKKSFDRRS PSNLNSTSVT
1360 1370 1380 1390 1400
PRASLDYDPS VPNTSYAPVQ SASPVVKPTD NTSSSSNKKD TPSSNSRGHS
1410 1420 1430 1440 1450
RASSFARTLA PHGTYNGFIT VVAAENVAKH VQIKISLTQG GRLKHIYKTK
1460 1470 1480 1490 1500
SQKANNDGVA VFDEECSFKA SPEANLVLGA ISHQRLSRDK DLGIAQINLG
1510 1520 1530 1540
DPQIQQDGQI SVKLGDGHLI VKINYGKDKN GQVPPVPEVP QEYTQ
Length:1,545
Mass (Da):171,076
Last modified:November 1, 1997 - v1
Checksum:i77A0AE57F9259784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Z46373 Genomic DNA. Translation: CAA86506.1.
BK006946 Genomic DNA. Translation: DAA09825.1.
PIRiS48824.
RefSeqiNP_013639.1. NM_001182431.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi35069. 89 interactions.
DIPiDIP-6589N.
IntActiQ03640. 62 interactions.
MINTiMINT-667993.

PTM databases

iPTMnetiQ03640.

Proteomic databases

MaxQBiQ03640.
PeptideAtlasiQ03640.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YML072C.
SGDiS000004537. TCB3.

Phylogenomic databases

GeneTreeiENSGT00730000113103.
HOGENOMiHOG000093250.
InParanoidiQ03640.
OMAiFWVIYMP.
OrthoDBiEOG7TQV86.

Enzyme and pathway databases

BioCyciYEAST:G3O-32666-MONOMER.

Miscellaneous databases

PROiQ03640.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 8, 2016
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.