TCB3_YEAST
ID TCB3_YEAST Reviewed; 1545 AA.
AC Q03640; D6VZA1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Tricalbin-3;
GN Name=TCB3; OrderedLocusNames=YML072C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, AND CALCIUM-DEPENDENT BINDING TO PHOSPHOLIPIDS.
RX PubMed=15049706; DOI=10.1021/bi036082w;
RA Schulz T.A., Creutz C.E.;
RT "The tricalbin C2 domains: lipid-binding properties of a novel,
RT synaptotagmin-like yeast protein family.";
RL Biochemistry 43:3987-3995(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH TCB2.
RX PubMed=15141306; DOI=10.1007/s00018-004-4029-8;
RA Creutz C.E., Snyder S.L., Schulz T.A.;
RT "Characterization of the yeast tricalbins: membrane-bound multi-C2-domain
RT proteins that form complexes involved in membrane trafficking.";
RL Cell. Mol. Life Sci. 61:1208-1220(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-112 AND THR-1350, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1340; SER-1342; SER-1346;
RP THR-1350; SER-1354 AND SER-1400, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22250200; DOI=10.1242/jcs.085118;
RA Toulmay A., Prinz W.A.;
RT "A conserved membrane-binding domain targets proteins to organelle contact
RT sites.";
RL J. Cell Sci. 125:49-58(2012).
CC -!- FUNCTION: May play a role in membrane trafficking.
CC {ECO:0000269|PubMed:15049706, ECO:0000269|PubMed:15141306}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250};
CC -!- SUBUNIT: Interacts with TCB2 via its C-terminal domain.
CC {ECO:0000269|PubMed:15141306}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:22250200}; Multi-pass membrane protein
CC {ECO:0000255}. Note=More enriched in the cortical endoplasmic reticulum
CC (ER) that is closely apposed to the cell membrane than in the
CC perinuclear ER or internal ER tubules that connect the nucleus to the
CC cortical ER. {ECO:0000269|PubMed:22250200}.
CC -!- DOMAIN: The C-terminal C2 domain shows Ca(2+)-dependent phospholipid
CC binding. It binds to phosphatidylserine, phosphatidylinositol and
CC various phosphoinositides. The other C2 domains do not retain all 5
CC conserved Asp residues found in calcium-binding C2 domains.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tricalbin family. {ECO:0000305}.
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DR EMBL; Z46373; CAA86506.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09825.1; -; Genomic_DNA.
DR PIR; S48824; S48824.
DR RefSeq; NP_013639.1; NM_001182431.1.
DR AlphaFoldDB; Q03640; -.
DR SMR; Q03640; -.
DR BioGRID; 35069; 358.
DR DIP; DIP-6589N; -.
DR IntAct; Q03640; 66.
DR MINT; Q03640; -.
DR STRING; 4932.YML072C; -.
DR iPTMnet; Q03640; -.
DR MaxQB; Q03640; -.
DR PaxDb; Q03640; -.
DR PRIDE; Q03640; -.
DR EnsemblFungi; YML072C_mRNA; YML072C; YML072C.
DR GeneID; 854903; -.
DR KEGG; sce:YML072C; -.
DR SGD; S000004537; TCB3.
DR VEuPathDB; FungiDB:YML072C; -.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_001661_1_1_1; -.
DR InParanoid; Q03640; -.
DR OMA; YMPVLSQ; -.
DR BioCyc; YEAST:G3O-32666-MON; -.
DR PRO; PR:Q03640; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03640; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IGI:SGD.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IGI:SGD.
DR CDD; cd04044; C2A_Tricalbin-like; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd04045; C2C_Tricalbin-like; 1.
DR CDD; cd04040; C2D_Tricalbin-like; 1.
DR Gene3D; 2.60.40.150; -; 4.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037761; C2A_Tricalbin.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR037762; C2C_Tricalbin.
DR InterPro; IPR037756; C2D_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR017147; Tricalbin.
DR Pfam; PF00168; C2; 5.
DR PIRSF; PIRSF037232; Tricalbin; 1.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; SSF49562; 5.
DR PROSITE; PS50004; C2; 5.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium/phospholipid-binding; Cell membrane; Coiled coil;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1545
FT /note="Tricalbin-3"
FT /id="PRO_0000203249"
FT TOPO_DOM 1..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..1545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 272..479
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 470..596
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 646..763
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 783..897
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1119..1234
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1396..1514
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 620..660
FT /evidence="ECO:0000255"
FT COILED 937..972
FT /evidence="ECO:0000255"
FT COMPBIAS 57..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:17761666, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1545 AA; 171076 MW; 77A0AE57F9259784 CRC64;
MTGIKAQVHP PPDSTLFHEE EKKKVGGNLP QKVINQQERG SDHAPSGHHQ YHQLINHDAN
DTKTSNSVSD VSKGQKTADS NPEGKKQSSK DIFVASSAQK TNQLPGPNPQ GSIGAVPLEG
LRPKEFRSAP SRKPNKFDTS ITKPGVLDDL GKLDEKDIKE KFHLDSDDKL FPWQNVGEFH
ASGKGSPNTK MSRVIKAYIL ENFYNDWYCN IATVLGTCFF SWLFAYIGFS WWSMIFIFLG
TATVYNAEYT RFNRNIRDDL KRVTVEETLS DRVESTTWLN SFLSKFWVIY MPVLSQQVKD
NVNPQLAGVA PGYGIDALAI DEFTLGSKAP TIKGIKSYTK TGKNTVEMDW SFAFTPSDVS
DMTATEAREK INPKISLGVT LGKSFVSKTM PILVEDINVA GKMRIKVEFG KAFPNIKIVS
LQLLEPPLID FALKPIGGDT LGLDVMSFLP GLKSFVKNII NSNIGPMLFP PNHLDINVED
IMAAQSKEAI GVLAVTIASA DSLKGSDFIT NTVDPYIVMT TEDAVPGTDE EVRTSIKSNV
KNPRWNETKY LLLNTLEQKL NLKCFDFNDV RKDTVIGDLQ LDLADLLQNP VLDNQTAELR
SGTKSKGILH YSLHWFPVKE DKSEEKAVER AEAKAKGKKE DENEDTTEKE EDENEESSQT
DVGIAKITLQ KVKYLDTTSS MTGSLSPCAE LFIDGQKVKS YRTLRRINEP SWNETIEVLV
PSKSNSKFVL KIFDDRMNGK ALICEYSSSL DDIMTTLDTA QEFVKGSPQG DIYLDVSWKS
IEMTGAFAAA NSVSEPIGCI KLDVKDAIIK GDLSGVGDVD PYYTVSLNRR VLYKSIYHSD
TDHPIFDNST YVPIFSPNQI LTLEFHDYQK IGKDRFIGSV QIPTSNVFKK DPKSGKYVGN
NGKEEISKLK LKDHEHKVTE SIVNVSTTFI PINLVYSPEE LVNVEKLEKE LKEKKKKFEA
TQEENEQEME KNPKEWEVAE IEDPFDSDEK KINRKAKLSL NELIKQKSGI LSMQILEGTL
SPSSAYLEIL ADDISYPVFI CMKPSQGKLN SEMANIFIRD LNYSKLHFRV SKKHIAKDSD
DVISETSYST LKLLKQAYEE PMWLNFNGSK MKVRFLYTPT SVKLPSSESV EDTGYLNIKL
ISGHGLKSAD RNGYSDPFVH IFVNDKKVFK SNIKKKTLDP VWNEDAKIPI LSRSKNQVIF
NVLDWDRAGD NDDLGQASLD VSSLEVGKTY NWNLNLNTQG SIKLQGSFNP EYIKPSFDIV
KGGITDKPMK IASGAAHATV GIAGTGIGAA TGVATGGLKK GGHLLKSLGG NPMKRSKSSN
GNESNGAKKS SEKKSFDRRS PSNLNSTSVT PRASLDYDPS VPNTSYAPVQ SASPVVKPTD
NTSSSSNKKD TPSSNSRGHS RASSFARTLA PHGTYNGFIT VVAAENVAKH VQIKISLTQG
GRLKHIYKTK SQKANNDGVA VFDEECSFKA SPEANLVLGA ISHQRLSRDK DLGIAQINLG
DPQIQQDGQI SVKLGDGHLI VKINYGKDKN GQVPPVPEVP QEYTQ
