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   27-MAR-2024, entry version 187.
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).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=35015055; DOI=10.1083/jcb.202111095;
RA   Toulmay A., Whittle F.B., Yang J., Bai X., Diarra J., Banerjee S.,
RA   Levine T.P., Golden A., Prinz W.A.;
RT   "Vps13-like proteins provide phosphatidylethanolamine for GPI anchor
RT   synthesis in the ER.";
RL   J. Cell Biol. 221:0-0(2022).
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; Evidence={ECO:0000255|PROSITE-
CC         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       ECO:0000269|PubMed:35015055}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:35015055}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=More enriched in the cortical
CC       endoplasmic reticulum (ER) that is closely apposed to the cell membrane
CC       than in the perinuclear ER or internal ER tubules that connect the
CC       nucleus to the 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; 367.
DR   DIP; DIP-6589N; -.
DR   IntAct; Q03640; 66.
DR   MINT; Q03640; -.
DR   STRING; 4932.YML072C; -.
DR   TCDB; 9.A.57.1.12; the extended-synaptotagmin (e-syt) family.
DR   GlyGen; Q03640; 9 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; Q03640; -.
DR   MaxQB; Q03640; -.
DR   PaxDb; 4932-YML072C; -.
DR   PeptideAtlas; Q03640; -.
DR   EnsemblFungi; YML072C_mRNA; YML072C; YML072C.
DR   GeneID; 854903; -.
DR   KEGG; sce:YML072C; -.
DR   AGR; SGD:S000004537; -.
DR   SGD; S000004537; TCB3.
DR   VEuPathDB; FungiDB:YML072C; -.
DR   eggNOG; KOG1012; Eukaryota.
DR   HOGENOM; CLU_001661_1_1_1; -.
DR   InParanoid; Q03640; -.
DR   OMA; DHFYGDW; -.
DR   OrthoDB; 2787577at2759; -.
DR   BioCyc; YEAST:G3O-32666-MONOMER; -.
DR   BioGRID-ORCS; 854903; 4 hits in 10 CRISPR screens.
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:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   CDD; cd21678; SMP_TCB; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 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   PANTHER; PTHR46980; TRICALBIN-1-RELATED; 1.
DR   PANTHER; PTHR46980:SF1; TRICALBIN-3; 1.
DR   Pfam; PF00168; C2; 5.
DR   PIRSF; PIRSF037232; Tricalbin; 1.
DR   SMART; SM00239; C2; 5.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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
//