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Q03640 (TCB3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tricalbin-3
Gene names
Name:TCB3
Ordered Locus Names:YML072C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length1545 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in membrane trafficking. Ref.6 Ref.7

Cofactor

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

Subunit structure

Interacts with TCB2 via its C-terminal domain. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity Ref.4.

Domain

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.

Miscellaneous

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

Sequence similarities

Belongs to the tricalbin family.

Contains 3 C2 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15451545Tricalbin-3
PRO_0000203249

Regions

Topological domain1 – 206206Cytoplasmic By similarity
Transmembrane207 – 22721Helical; Potential
Topological domain2281Extracellular By similarity
Transmembrane229 – 24921Helical; Potential
Topological domain250 – 15451296Cytoplasmic By similarity
Domain478 – 580103C2 1
Domain785 – 88197C2 2
Domain1121 – 121898C2 3
Coiled coil620 – 66041 Potential
Coiled coil937 – 97236 Potential
Compositional bias1316 – 140489Ser-rich

Sites

Metal binding11501Calcium 1 By similarity
Metal binding11501Calcium 2 By similarity
Metal binding11561Calcium 1 By similarity
Metal binding12041Calcium 1 By similarity
Metal binding12041Calcium 2 By similarity
Metal binding12061Calcium 1 By similarity
Metal binding12061Calcium 2 By similarity
Metal binding12061Calcium 3 By similarity
Metal binding12121Calcium 2 By similarity
Metal binding12121Calcium 3 By similarity

Amino acid modifications

Modified residue671Phosphoserine Ref.12
Modified residue1121Phosphoserine Ref.11 Ref.12
Modified residue12731Phosphoserine Ref.12
Modified residue13351Phosphoserine Ref.12
Modified residue13401Phosphoserine Ref.11 Ref.12
Modified residue13421Phosphoserine Ref.3 Ref.11 Ref.12
Modified residue13461Phosphoserine Ref.12
Modified residue13501Phosphothreonine Ref.3 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q03640 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 77A0AE57F9259784

FASTA1,545171,076
        10         20         30         40         50         60 
MTGIKAQVHP PPDSTLFHEE EKKKVGGNLP QKVINQQERG SDHAPSGHHQ YHQLINHDAN 

        70         80         90        100        110        120 
DTKTSNSVSD VSKGQKTADS NPEGKKQSSK DIFVASSAQK TNQLPGPNPQ GSIGAVPLEG 

       130        140        150        160        170        180 
LRPKEFRSAP SRKPNKFDTS ITKPGVLDDL GKLDEKDIKE KFHLDSDDKL FPWQNVGEFH 

       190        200        210        220        230        240 
ASGKGSPNTK MSRVIKAYIL ENFYNDWYCN IATVLGTCFF SWLFAYIGFS WWSMIFIFLG 

       250        260        270        280        290        300 
TATVYNAEYT RFNRNIRDDL KRVTVEETLS DRVESTTWLN SFLSKFWVIY MPVLSQQVKD 

       310        320        330        340        350        360 
NVNPQLAGVA PGYGIDALAI DEFTLGSKAP TIKGIKSYTK TGKNTVEMDW SFAFTPSDVS 

       370        380        390        400        410        420 
DMTATEAREK INPKISLGVT LGKSFVSKTM PILVEDINVA GKMRIKVEFG KAFPNIKIVS 

       430        440        450        460        470        480 
LQLLEPPLID FALKPIGGDT LGLDVMSFLP GLKSFVKNII NSNIGPMLFP PNHLDINVED 

       490        500        510        520        530        540 
IMAAQSKEAI GVLAVTIASA DSLKGSDFIT NTVDPYIVMT TEDAVPGTDE EVRTSIKSNV 

       550        560        570        580        590        600 
KNPRWNETKY LLLNTLEQKL NLKCFDFNDV RKDTVIGDLQ LDLADLLQNP VLDNQTAELR 

       610        620        630        640        650        660 
SGTKSKGILH YSLHWFPVKE DKSEEKAVER AEAKAKGKKE DENEDTTEKE EDENEESSQT 

       670        680        690        700        710        720 
DVGIAKITLQ KVKYLDTTSS MTGSLSPCAE LFIDGQKVKS YRTLRRINEP SWNETIEVLV 

       730        740        750        760        770        780 
PSKSNSKFVL KIFDDRMNGK ALICEYSSSL DDIMTTLDTA QEFVKGSPQG DIYLDVSWKS 

       790        800        810        820        830        840 
IEMTGAFAAA NSVSEPIGCI KLDVKDAIIK GDLSGVGDVD PYYTVSLNRR VLYKSIYHSD 

       850        860        870        880        890        900 
TDHPIFDNST YVPIFSPNQI LTLEFHDYQK IGKDRFIGSV QIPTSNVFKK DPKSGKYVGN 

       910        920        930        940        950        960 
NGKEEISKLK LKDHEHKVTE SIVNVSTTFI PINLVYSPEE LVNVEKLEKE LKEKKKKFEA 

       970        980        990       1000       1010       1020 
TQEENEQEME KNPKEWEVAE IEDPFDSDEK KINRKAKLSL NELIKQKSGI LSMQILEGTL 

      1030       1040       1050       1060       1070       1080 
SPSSAYLEIL ADDISYPVFI CMKPSQGKLN SEMANIFIRD LNYSKLHFRV SKKHIAKDSD 

      1090       1100       1110       1120       1130       1140 
DVISETSYST LKLLKQAYEE PMWLNFNGSK MKVRFLYTPT SVKLPSSESV EDTGYLNIKL 

      1150       1160       1170       1180       1190       1200 
ISGHGLKSAD RNGYSDPFVH IFVNDKKVFK SNIKKKTLDP VWNEDAKIPI LSRSKNQVIF 

      1210       1220       1230       1240       1250       1260 
NVLDWDRAGD NDDLGQASLD VSSLEVGKTY NWNLNLNTQG SIKLQGSFNP EYIKPSFDIV 

      1270       1280       1290       1300       1310       1320 
KGGITDKPMK IASGAAHATV GIAGTGIGAA TGVATGGLKK GGHLLKSLGG NPMKRSKSSN 

      1330       1340       1350       1360       1370       1380 
GNESNGAKKS SEKKSFDRRS PSNLNSTSVT PRASLDYDPS VPNTSYAPVQ SASPVVKPTD 

      1390       1400       1410       1420       1430       1440 
NTSSSSNKKD TPSSNSRGHS RASSFARTLA PHGTYNGFIT VVAAENVAKH VQIKISLTQG 

      1450       1460       1470       1480       1490       1500 
GRLKHIYKTK SQKANNDGVA VFDEECSFKA SPEANLVLGA ISHQRLSRDK DLGIAQINLG 

      1510       1520       1530       1540 
DPQIQQDGQI SVKLGDGHLI VKINYGKDKN GQVPPVPEVP QEYTQ

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND THR-1350, MASS SPECTROMETRY.
Strain: 2124.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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.
[7]"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.
[8]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, MASS SPECTROMETRY.
Strain: YAL6B.
[9]"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, MASS SPECTROMETRY.
Strain: ADR376.
[10]"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, MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-1340; SER-1342 AND THR-1350, MASS SPECTROMETRY.
[12]"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; SER-1273; SER-1335; SER-1340; SER-1342; SER-1346 AND THR-1350, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z46373 Genomic DNA. Translation: CAA86506.1.
BK006946 Genomic DNA. Translation: DAA09825.1.
PIRS48824.
RefSeqNP_013639.1. NM_001182431.1.

3D structure databases

ProteinModelPortalQ03640.
SMRQ03640. Positions 1053-1223.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6589N.
IntActQ03640. 62 interactions.
MINTMINT-667993.
STRING4932.YML072C.

Proteomic databases

PaxDbQ03640.
PeptideAtlasQ03640.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML072C; YML072C; YML072C.
GeneID854903.
KEGGsce:YML072C.

Organism-specific databases

CYGDYML072c.
SGDS000004537. TCB3.

Phylogenomic databases

eggNOGCOG5038.
GeneTreeENSGT00550000074417.
HOGENOMHOG000093250.
OMASESINNM.
OrthoDBEOG4HDX2K.

Gene expression databases

GenevestigatorQ03640.
GermOnlineYML072C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR017147. Tricalbin.
[Graphical view]
PfamPF00168. C2. 5 hits.
[Graphical view]
PIRSFPIRSF037232. Tricalbin. 1 hit.
SMARTSM00239. C2. 5 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 5 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio977885.

Entry information

Entry nameTCB3_YEAST
AccessionPrimary (citable) accession number: Q03640
Secondary accession number(s): D6VZA1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents