TCB1_YEAST
ID TCB1_YEAST Reviewed; 1186 AA.
AC Q12466; D6W2E8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Tricalbin-1;
GN Name=TCB1; OrderedLocusNames=YOR086C; ORFNames=YOR3141c;
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 [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, AND IDENTIFICATION BY
RP 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-1000, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194}.
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 6140 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; X94335; CAA64008.1; -; Genomic_DNA.
DR EMBL; Z74994; CAA99281.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10864.1; -; Genomic_DNA.
DR PIR; S61647; S61647.
DR RefSeq; NP_014729.1; NM_001183505.1.
DR AlphaFoldDB; Q12466; -.
DR SMR; Q12466; -.
DR BioGRID; 34484; 138.
DR DIP; DIP-6292N; -.
DR IntAct; Q12466; 6.
DR MINT; Q12466; -.
DR STRING; 4932.YOR086C; -.
DR CarbonylDB; Q12466; -.
DR iPTMnet; Q12466; -.
DR MaxQB; Q12466; -.
DR PaxDb; Q12466; -.
DR PRIDE; Q12466; -.
DR EnsemblFungi; YOR086C_mRNA; YOR086C; YOR086C.
DR GeneID; 854253; -.
DR KEGG; sce:YOR086C; -.
DR SGD; S000005612; TCB1.
DR VEuPathDB; FungiDB:YOR086C; -.
DR eggNOG; KOG1012; Eukaryota.
DR GeneTree; ENSGT00940000176636; -.
DR HOGENOM; CLU_001661_1_1_1; -.
DR InParanoid; Q12466; -.
DR OMA; GWTGDVM; -.
DR BioCyc; YEAST:G3O-33621-MON; -.
DR PRO; PR:Q12466; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12466; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0005886; C:plasma membrane; 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; -; 3.
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; 4.
DR PIRSF; PIRSF037232; Tricalbin; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 4.
DR SUPFAM; SSF49562; SSF49562; 4.
DR PROSITE; PS50004; C2; 4.
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..1186
FT /note="Tricalbin-1"
FT /id="PRO_0000252271"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..1186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 172..375
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 366..487
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 512..636
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 640..757
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 976..1094
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 795..822
FT /evidence="ECO:0000255"
FT COMPBIAS 28..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1008
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1008
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1014
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1064
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1064
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1066
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1066
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1066
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1069
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1072
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1072
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1186 AA; 133576 MW; 1CD852549A6D82B1 CRC64;
MAKEDTGVTA PKKPETAQVA NINGIDKLEP PKTKEETESS KSVSSEKAAH ASDESFKRSI
HEASYVGWKQ IGGWEDKDEL TLDDELMDMT RETFLDNIIP DSLYGDWYHS VAIFFIGGVA
SFALGHYKFS MGSAFFVIVI TSLLYRTSAK KYRGSIRELV QKEFTVQKVE NDYESLEWLN
AFLDKYWPIL EPSVSQLIVQ QANEQMATNE AIPKFITQLW IDELTLGVKP PRVDLVKTFQ
NTASDVVVMD WGISFTPHDL CDMSAKQVRN YVNELAVVKA KIFGITIPVS VSDIAFKAHA
RVKFKLMTPF PHVETVNIQL LKVPDFDFVA TLFGRSIFNW EILAIPGLMT LIQKMAKKYM
GPILLPPFSL QLNIPQLLSG SNLSIGILEI TVKNAKGLKR TSSILNESID PYLSFEFNDI
SIAKTRTVRD TLNPVWDETL YVLLNSFTDP LTISVYDKRA KLKDKVLGRI QYNLNTLHDK
TTQRNLKAQF LRNSKPVGEL TFDLRFFPTL EEKKLPDGSV EELPDLNTGI AKVVVEEGSR
FAEEEQKVTA YVEVYLNAKL VLTTGKATDT GTLKWNSDYE AVIADRRKTR YKFVVKDGKG
EEIGSTIQTL NDLIDRSQVN KNLIPLKNQK GDIKITTYWR PVRLEIGSNS VAYTPPIGAI
RVFIEKANDL RNLEKFGTID PYCKVLVNGL SKGRTDFKSQ TLNPVWNQVI YVAVTSPNQR
ITLQCMDVET VNKDRSLGEF NVNVQDLFKK DENDKYEETI DEKAKVGRLV MPKKKPKGTI
TYYTSFYPAL PVLTLEEIQD LDKVNKKKKA LELRKSAIDE KKISKEDKAK FDQEWNEVKE
LEDMYSNRQK LDLPELLQYN QGVLAVTVLN GELPDSGLYV QAFFDDNGHP RFVSPRIPSR
IVKNGWSGDV IIKELDKSIT TFRVAKNKNY NRVEKCVCEV ELPTQELVKN CYYKPSILHL
SGEGSAKLML QISWFPIDTK QLPANDLITN SGDLTIMSRS AENLIASDLN GYSDPYLKYY
INNEEDCAYK TKVVKKTLNP KWNDEGTIQI NNRLNDVLRI KVMDWDSTSA DDTIGTAEIP
LNKVKVEGTT ELDVPVEGLE NAGQDGGMLH LAFSFKPRYT ISVSKREKKV GDIASKGLGT
GLKAGTTVIG GGVGAIGKIK KGVFGGLGSL TNHKKNHEMG EEETKF
