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Protein

Tricalbin-1

Gene

TCB1

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 bindingi1008 – 10081Calcium 1By similarity
Metal bindingi1008 – 10081Calcium 2By similarity
Metal bindingi1014 – 10141Calcium 1By similarity
Metal bindingi1064 – 10641Calcium 1By similarity
Metal bindingi1064 – 10641Calcium 2By similarity
Metal bindingi1066 – 10661Calcium 1By similarity
Metal bindingi1066 – 10661Calcium 2By similarity
Metal bindingi1066 – 10661Calcium 3By similarity
Metal bindingi1069 – 10691Calcium 3By similarity
Metal bindingi1072 – 10721Calcium 2By similarity
Metal bindingi1072 – 10721Calcium 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-33621-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Tricalbin-1
Gene namesi
Name:TCB1
Ordered Locus Names:YOR086C
ORF Names:YOR3141c
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR086C.
SGDiS000005612. TCB1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 106106CytoplasmicSequence analysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence analysisAdd
BLAST
Topological domaini128 – 1281ExtracellularSequence analysis
Transmembranei129 – 14921HelicalSequence analysisAdd
BLAST
Topological domaini150 – 11861037CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11861186Tricalbin-1PRO_0000252271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1000 – 10001PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12466.

PTM databases

iPTMnetiQ12466.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi34484. 34 interactions.
DIPiDIP-6292N.
IntActiQ12466. 4 interactions.
MINTiMINT-705548.

Structurei

3D structure databases

ProteinModelPortaliQ12466.
SMRiQ12466. Positions 1003-1082.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini373 – 47199C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini645 – 74197C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini979 – 1078100C2 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili795 – 82228Sequence analysisAdd
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.
HOGENOMiHOG000248700.
InParanoidiQ12466.
OMAiWDEVLYV.
OrthoDBiEOG72JWQH.

Family and domain databases

Gene3Di2.60.40.150. 4 hits.
InterProiIPR000008. C2_dom.
IPR017147. Tricalbin.
[Graphical view]
PfamiPF00168. C2. 4 hits.
[Graphical view]
PIRSFiPIRSF037232. Tricalbin. 1 hit.
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 4 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 4 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEDTGVTA PKKPETAQVA NINGIDKLEP PKTKEETESS KSVSSEKAAH
60 70 80 90 100
ASDESFKRSI HEASYVGWKQ IGGWEDKDEL TLDDELMDMT RETFLDNIIP
110 120 130 140 150
DSLYGDWYHS VAIFFIGGVA SFALGHYKFS MGSAFFVIVI TSLLYRTSAK
160 170 180 190 200
KYRGSIRELV QKEFTVQKVE NDYESLEWLN AFLDKYWPIL EPSVSQLIVQ
210 220 230 240 250
QANEQMATNE AIPKFITQLW IDELTLGVKP PRVDLVKTFQ NTASDVVVMD
260 270 280 290 300
WGISFTPHDL CDMSAKQVRN YVNELAVVKA KIFGITIPVS VSDIAFKAHA
310 320 330 340 350
RVKFKLMTPF PHVETVNIQL LKVPDFDFVA TLFGRSIFNW EILAIPGLMT
360 370 380 390 400
LIQKMAKKYM GPILLPPFSL QLNIPQLLSG SNLSIGILEI TVKNAKGLKR
410 420 430 440 450
TSSILNESID PYLSFEFNDI SIAKTRTVRD TLNPVWDETL YVLLNSFTDP
460 470 480 490 500
LTISVYDKRA KLKDKVLGRI QYNLNTLHDK TTQRNLKAQF LRNSKPVGEL
510 520 530 540 550
TFDLRFFPTL EEKKLPDGSV EELPDLNTGI AKVVVEEGSR FAEEEQKVTA
560 570 580 590 600
YVEVYLNAKL VLTTGKATDT GTLKWNSDYE AVIADRRKTR YKFVVKDGKG
610 620 630 640 650
EEIGSTIQTL NDLIDRSQVN KNLIPLKNQK GDIKITTYWR PVRLEIGSNS
660 670 680 690 700
VAYTPPIGAI RVFIEKANDL RNLEKFGTID PYCKVLVNGL SKGRTDFKSQ
710 720 730 740 750
TLNPVWNQVI YVAVTSPNQR ITLQCMDVET VNKDRSLGEF NVNVQDLFKK
760 770 780 790 800
DENDKYEETI DEKAKVGRLV MPKKKPKGTI TYYTSFYPAL PVLTLEEIQD
810 820 830 840 850
LDKVNKKKKA LELRKSAIDE KKISKEDKAK FDQEWNEVKE LEDMYSNRQK
860 870 880 890 900
LDLPELLQYN QGVLAVTVLN GELPDSGLYV QAFFDDNGHP RFVSPRIPSR
910 920 930 940 950
IVKNGWSGDV IIKELDKSIT TFRVAKNKNY NRVEKCVCEV ELPTQELVKN
960 970 980 990 1000
CYYKPSILHL SGEGSAKLML QISWFPIDTK QLPANDLITN SGDLTIMSRS
1010 1020 1030 1040 1050
AENLIASDLN GYSDPYLKYY INNEEDCAYK TKVVKKTLNP KWNDEGTIQI
1060 1070 1080 1090 1100
NNRLNDVLRI KVMDWDSTSA DDTIGTAEIP LNKVKVEGTT ELDVPVEGLE
1110 1120 1130 1140 1150
NAGQDGGMLH LAFSFKPRYT ISVSKREKKV GDIASKGLGT GLKAGTTVIG
1160 1170 1180
GGVGAIGKIK KGVFGGLGSL TNHKKNHEMG EEETKF
Length:1,186
Mass (Da):133,576
Last modified:November 1, 1996 - v1
Checksum:i1CD852549A6D82B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64008.1.
Z74994 Genomic DNA. Translation: CAA99281.1.
BK006948 Genomic DNA. Translation: DAA10864.1.
PIRiS61647.
RefSeqiNP_014729.1. NM_001183505.1.

Genome annotation databases

EnsemblFungiiYOR086C; YOR086C; YOR086C.
GeneIDi854253.
KEGGisce:YOR086C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64008.1.
Z74994 Genomic DNA. Translation: CAA99281.1.
BK006948 Genomic DNA. Translation: DAA10864.1.
PIRiS61647.
RefSeqiNP_014729.1. NM_001183505.1.

3D structure databases

ProteinModelPortaliQ12466.
SMRiQ12466. Positions 1003-1082.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34484. 34 interactions.
DIPiDIP-6292N.
IntActiQ12466. 4 interactions.
MINTiMINT-705548.

PTM databases

iPTMnetiQ12466.

Proteomic databases

MaxQBiQ12466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR086C; YOR086C; YOR086C.
GeneIDi854253.
KEGGisce:YOR086C.

Organism-specific databases

EuPathDBiFungiDB:YOR086C.
SGDiS000005612. TCB1.

Phylogenomic databases

GeneTreeiENSGT00730000113103.
HOGENOMiHOG000248700.
InParanoidiQ12466.
OMAiWDEVLYV.
OrthoDBiEOG72JWQH.

Enzyme and pathway databases

BioCyciYEAST:G3O-33621-MONOMER.

Miscellaneous databases

PROiQ12466.

Family and domain databases

Gene3Di2.60.40.150. 4 hits.
InterProiIPR000008. C2_dom.
IPR017147. Tricalbin.
[Graphical view]
PfamiPF00168. C2. 4 hits.
[Graphical view]
PIRSFiPIRSF037232. Tricalbin. 1 hit.
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 4 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 4 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. 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. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  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-1000, 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-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCB1_YEAST
AccessioniPrimary (citable) accession number: Q12466
Secondary accession number(s): D6W2E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 126 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 6140 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.