TCB2_YEAST
ID TCB2_YEAST Reviewed; 1178 AA.
AC P48231; D6W192; Q45TY9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tricalbin-2;
GN Name=TCB2; OrderedLocusNames=YNL087W; ORFNames=N2250;
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], AND VARIANTS 11-GLU--VAL-13; SER-121;
RP GLY-528; 691-MET-LYS-692 AND ARG-1159.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, AND LIPID-BINDING.
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TCB1 AND TCB3.
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 [9]
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 SUBCELLULAR LOCATION, AND DOMAIN.
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 -!- SUBUNIT: Interacts with TCB1 and TCB3 via its C-terminal domain.
CC {ECO:0000269|PubMed:15141306}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15141306}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22250200}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Traffics from the cell surface to intracellular
CC vesicles near the vacuole (PubMed:15141306). More enriched in the
CC cortical endoplasmic reticulum (ER) that is closely apposed to the cell
CC membrane than in the perinuclear ER or internal ER tubules that connect
CC the nucleus to the cortical ER (PubMed:22250200).
CC {ECO:0000269|PubMed:15141306, 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, ECO:0000269|PubMed:22250200}.
CC -!- DOMAIN: The C2 domains show Ca(2+)-independent phospholipid binding.
CC None of the C2 domains retains all 5 conserved Asp residues found in
CC calcium-binding C2 domains.
CC -!- MISCELLANEOUS: Present with 2630 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; DQ115393; AAZ22521.1; -; Genomic_DNA.
DR EMBL; X89016; CAA61423.1; -; Genomic_DNA.
DR EMBL; Z71363; CAA95963.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10458.1; -; Genomic_DNA.
DR PIR; S57535; S57535.
DR RefSeq; NP_014312.1; NM_001182925.1.
DR AlphaFoldDB; P48231; -.
DR SMR; P48231; -.
DR BioGRID; 35736; 102.
DR DIP; DIP-2709N; -.
DR IntAct; P48231; 6.
DR MINT; P48231; -.
DR STRING; 4932.YNL087W; -.
DR iPTMnet; P48231; -.
DR MaxQB; P48231; -.
DR PaxDb; P48231; -.
DR PRIDE; P48231; -.
DR EnsemblFungi; YNL087W_mRNA; YNL087W; YNL087W.
DR GeneID; 855637; -.
DR KEGG; sce:YNL087W; -.
DR SGD; S000005031; TCB2.
DR VEuPathDB; FungiDB:YNL087W; -.
DR eggNOG; KOG1012; Eukaryota.
DR GeneTree; ENSGT00940000176636; -.
DR HOGENOM; CLU_001661_1_0_1; -.
DR InParanoid; P48231; -.
DR OMA; TWNEIHY; -.
DR BioCyc; YEAST:G3O-33116-MON; -.
DR PRO; PR:P48231; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P48231; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; IDA: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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
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 Cell membrane; Coiled coil; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1178
FT /note="Tricalbin-2"
FT /id="PRO_0000203444"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 164..367
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 358..481
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 504..628
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 632..749
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 962..1086
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 784..821
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12466"
FT VARIANT 11..13
FT /note="DQI -> EQV (in strain: SK1)"
FT VARIANT 121
FT /note="F -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 528
FT /note="R -> G (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 691..692
FT /note="IE -> MK (in strain: SK1)"
FT VARIANT 1159
FT /note="G -> R (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
SQ SEQUENCE 1178 AA; 132509 MW; 6597DE191C739F41 CRC64;
MSPNSSKTRT DQISSMPGIN EATKVESKNV VKDAVPIKSE VETNGTSIVR EKQDPSYVGW
KQVGGWEEKD ELTSEDLLVD VNKDTFLGNL LPDKFYGDWY HEVAILIIAG LCSFVLGYFK
FSLASVLIVM LTTGMLYRTS SKKYRESLRD LAQKEQTVEK ITSDYESVEW LNTFLDKYWP
IIEPSVSQQI VDGTNTALSE NVAIPKFIKA IWLDQFTLGV KPPRIDAIKT FQNTKSDVVV
MDVCLSFTPH DMSDLDAKQC RNYVNSNVVL KAKIFGMDIP VSVADIFFQV FVRFRFQLMT
TLPLVETINI QLLEVPEVDF ISRLLGNSVF NWEILAIPGL MRLIQKMAFK YLSPVLLPPF
SLQLNIPQLL SKTGLPIGVL EIKVKNAHGL RKLVGMIKKT VDPYLTFELS GKIVGKTKVF
KNSANPVWNE SIYILLQSFT DPLTIAVYDK RETLSDKKMG TVIFNLNKLH ANHYHKNEKV
HFLRNSKPVG ELTFDLRFFP TIEPKKLLNG DEEPLPDMNT GITKITIREL KGLDELSDKK
FVFAELYVNA ELVMTTKKEK RTAHLKWNSD YYSVVTDRRK TICRFVLKDQ SGKVISSSVQ
PLNHLIDRTE VNKEWIPLRN GKGELKVTTY WRPVDIDLGL KSVGYTTPIG MLRVFINKAE
NLRNPDSLGK ISPYAKVSVN GVARGRTNER IETLNPIWNQ SIYVSVTSPL QKVSIDCFGI
DTNGDDHNLG SLNIQTQNIY HKDNDDKYTI FIDNAPRTGN LIGKKGVKGT VTYYLSFYPV
VPVLSLEEAK EVDEINEKKD KLEKQKSTLD DKNISKEEKE RIKKEEFRLT EKYDMYSYKM
KLDLDELLQY NAGVLGVTVL GGELPQPGLY VQTFFDSCGY AAITSAKNAI RTIKTGWSGD
FMIKELEWSV TTFRVTKTKD ANKAENFICE VNIPTIELVR NCYYKPSVLN LIGKKSAKLL
VQVSWFPVTA TELPQSDLIT NSGDLKITAK SAENLIGVNK NGYSDPYVEF FLNEKSTSPF
FKTAVQKKTL NPTWNESKTI EVSNRVNDYL TINVKDYEST NSNRSIGKAV VPLSTIDPES
DTTFNIPLVG PKGEDGGVLH LEFEFEPRYT TNVVKREAGL GNFATKGLGT GIKAGSTVFA
LGTNVVSTGL GTIDKVKAGV FGGKKSTTTG DKKSEEKQ
