Tricalbin-3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q03640 (TCB3_YEAST)

Last modified November 24, 2009. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Tricalbin-3

Gene names

Name:	TCB3
Ordered Locus Names:	YML072C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	1545 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	May play a role in membrane trafficking. Ref.5 Ref.6
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.6
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
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. Ref.4
Sequence similarities	Belongs to the tricalbin family. Contains 3 C2 domains.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Coiled coil Repeat Transmembrane
Ligand	Calcium Calcium/phospholipid-binding Lipid-binding Metal-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cellular bud Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: SGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-27872,EBI-27872
	P40474	1	EBI-27872,EBI-25203
	Q06170	1	EBI-27872,EBI-35994
	Q06689	1	EBI-27872,EBI-38659
DIP5	P53388	1	EBI-27872,EBI-5904
DUR3	P33413	1	EBI-27872,EBI-2060312
FLC1	Q08967	1	EBI-27872,EBI-36673
FMP45	Q07651	1	EBI-27872,EBI-2051056
FTR1	P40088	1	EBI-27872,EBI-7138
GPA2	P10823	1	EBI-27872,EBI-7382
HNM1	P19807	1	EBI-27872,EBI-8409
HSP30	P25619	1	EBI-27872,EBI-8563
HXT1	P32465	1	EBI-27872,EBI-8759
HXT2	P23585	1	EBI-27872,EBI-2054100
HXT3	P32466	1	EBI-27872,EBI-8770
HXT5	P38695	1	EBI-27872,EBI-8778
HXT7	P39004	1	EBI-27872,EBI-8790
IST2	P38250	1	EBI-27872,EBI-21520
ITR1	P30605	1	EBI-27872,EBI-2050956
MEP1	P40260	1	EBI-27872,EBI-10714
MEP3	P53390	1	EBI-27872,EBI-10729
MID2	P36027	1	EBI-27872,EBI-10901
MUP1	P50276	1	EBI-27872,EBI-11624
OSH7	P38755	1	EBI-27872,EBI-12641
PDR12	Q02785	1	EBI-27872,EBI-13065
PHO84	P25297	1	EBI-27872,EBI-13320
PIS1	P06197	1	EBI-27872,EBI-13458
PLM2	Q04383	1	EBI-27872,EBI-2079237
PMP2	P40975	1	EBI-27872,EBI-2043041
PMP3	P87284	1	EBI-27872,EBI-13555
PST2	Q12335	1	EBI-27872,EBI-14064
RFS1	P38234	1	EBI-27872,EBI-21445
RIM1	P32445	1	EBI-27872,EBI-15206
RSN1	Q03516	1	EBI-27872,EBI-27593
RTN1	Q04947	1	EBI-27872,EBI-38020
SDS23	P53172	1	EBI-27872,EBI-23782
SFK1	P35735	1	EBI-27872,EBI-26678
SNQ2	P32568	1	EBI-27872,EBI-17590
TCB1	Q12466	1	EBI-27872,EBI-34614
TCB2	P48231	1	EBI-27872,EBI-28779
TPO1	Q07824	1	EBI-27872,EBI-38106
TPO2	P53283	1	EBI-27872,EBI-2044753
TPO3	Q06451	1	EBI-27872,EBI-34275
TPO4	Q12256	1	EBI-27872,EBI-37213
VHT1	P53241	1	EBI-27872,EBI-20297
WSC2	P53832	1	EBI-27872,EBI-2055941
WSC3	Q12215	1	EBI-27872,EBI-20551
YBL029C-A	Q3E756	1	EBI-27872,EBI-2044812
YOP1	Q12402	1	EBI-27872,EBI-37092
YOR1	P53049	1	EBI-27872,EBI-29324

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1545

1545

Tricalbin-3

PRO_0000203249

Regions

Topological domain

1 – 206

206

Cytoplasmic By similarity

Transmembrane

207 – 227

Potential

Topological domain

228

Extracellular By similarity

Transmembrane

229 – 249

Potential

Topological domain

250 – 1545

1296

Cytoplasmic By similarity

Domain

478 – 580

103

C2 1

Domain

785 – 881

C2 2

Domain

1121 – 1218

C2 3

Coiled coil

620 – 660

Potential

Coiled coil

937 – 972

Potential

Compositional bias

1316 – 1404

Ser-rich

Sites

Metal binding

1150

Calcium 1 By similarity

Metal binding

1150

Calcium 2 By similarity

Metal binding

1156

Calcium 1 By similarity

Metal binding

1204

Calcium 1 By similarity

Metal binding

1204

Calcium 2 By similarity

Metal binding

1206

Calcium 1 By similarity

Metal binding

1206

Calcium 2 By similarity

Metal binding

1206

Calcium 3 By similarity

Metal binding

1212

Calcium 2 By similarity

Metal binding

1212

Calcium 3 By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.11

Modified residue

112

Phosphoserine Ref.11 Ref.10

Modified residue

1273

Phosphoserine Ref.11

Modified residue

1335

Phosphoserine Ref.11

Modified residue

1340

Phosphoserine Ref.11 Ref.10

Modified residue

1342

Phosphoserine Ref.11 Ref.10 Ref.2

Modified residue

1346

Phosphoserine Ref.11

Modified residue

1350

Phosphothreonine Ref.11 Ref.10 Ref.2 Ref.7 Ref.8 Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

Q03640-1 [UniParc].

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

FASTA

1,545

171,076

        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

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References

	« Hide 'large scale' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"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: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1342 AND THR-1350, MASS SPECTROMETRY.
[3]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"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: 14562106] [Abstract] 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: 15049706] [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: 15141306] [Abstract] Cited for: FUNCTION, INTERACTION WITH TCB2.
[7]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, MASS SPECTROMETRY.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, MASS SPECTROMETRY.
[9]	"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: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, MASS SPECTROMETRY.
[10]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-1340; SER-1342 AND THR-1350, MASS SPECTROMETRY.
[11]	"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: 18407956] [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.

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Cross-references

Sequence databases
	Z46373 Genomic DNA. Translation: CAA86506.1.
PIR	S48824.
RefSeq	NP_013639.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6589N.
IntAct	Q03640. 79 interactions.
STRING	Q03640.
Proteomic databases
PeptideAtlas	Q03640.
Genome annotation databases
Ensembl	YML072C; YML072C; YML072C; Saccharomyces cerevisiae. [Genome view]
GeneID	854903.
KEGG	sce:YML072C.
NMPDR	fig\|4932.3.peg.4676.
Organism-specific databases
CYGD	YML072c.
SGD	S000004537. TCB3.
Phylogenomic databases
HOGENOM	Q03640.
OMA	GKDRSLG
OrthoDB	EOG9V9W6X
Gene expression databases
ArrayExpress	Q03640.
Genevestigator	Q03640.
GermOnline	YML072C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_reg_CaLB. IPR018029. C2_membr_targeting. IPR017147. Tricalbin. [Graphical view]
Pfam	PF00168. C2. 4 hits. [Graphical view]
PIRSF	PIRSF037232. Tricalbin. 1 hit.
SMART	SM00239. C2. 5 hits. [Graphical view]
PROSITE	PS50004. C2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977885.

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Entry information

Entry name

TCB3_YEAST

Accession

Primary (citable) accession number: Q03640

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents