EGT2_YEAST
ID EGT2_YEAST Reviewed; 1041 AA.
AC P42835; D6W0M0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein EGT2;
DE AltName: Full=Early G1 transcript 2;
DE Flags: Precursor;
GN Name=EGT2; OrderedLocusNames=YNL327W; ORFNames=N0320;
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], INDUCTION, AND FUNCTION.
RX PubMed=8668141; DOI=10.1128/mcb.16.7.3264;
RA Kovacech B., Nasmyth K., Schuster T.;
RT "EGT2 gene transcription is induced predominantly by Swi5 in early G1.";
RL Mol. Cell. Biol. 16:3264-3274(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7645347; DOI=10.1002/yea.320110606;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
RT identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames.";
RL Yeast 11:567-572(1995).
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, AND SEQUENCE REVISION TO 577.
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.
RX PubMed=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15452134; DOI=10.1074/jbc.m405232200;
RA Fujita M., Yoko-o T., Okamoto M., Jigami Y.;
RT "GPI7 involved in glycosylphosphatidylinositol biosynthesis is essential
RT for yeast cell separation.";
RL J. Biol. Chem. 279:51869-51879(2004).
RN [7]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Seems to be involved in the correct timing of cell separation
CC after cytokinesis, as separation of mutant daughter cells is delayed.
CC Could either be an enzyme necessary for glucans-degradation of the cell
CC wall at the neck region between mother and daughter cells or a
CC regulatory protein controlling this metabolic step.
CC {ECO:0000269|PubMed:8668141}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:15452134,
CC ECO:0000305|PubMed:9613572}. Membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}. Note=Localizes to the septum of dividing cells.
CC -!- INDUCTION: Exclusively expressed between the end of mitosis and early
CC G1; inactivated before cells pass start. {ECO:0000269|PubMed:8668141}.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
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DR EMBL; Z46259; CAA86371.1; -; Genomic_DNA.
DR EMBL; Z71603; CAA96259.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10236.2; -; Genomic_DNA.
DR PIR; S55862; S55862.
DR RefSeq; NP_014072.2; NM_001183165.2.
DR AlphaFoldDB; P42835; -.
DR SMR; P42835; -.
DR BioGRID; 35514; 55.
DR DIP; DIP-4267N; -.
DR MINT; P42835; -.
DR STRING; 4932.YNL327W; -.
DR MaxQB; P42835; -.
DR PaxDb; P42835; -.
DR PRIDE; P42835; -.
DR EnsemblFungi; YNL327W_mRNA; YNL327W; YNL327W.
DR GeneID; 855389; -.
DR KEGG; sce:YNL327W; -.
DR SGD; S000005271; EGT2.
DR VEuPathDB; FungiDB:YNL327W; -.
DR eggNOG; ENOG502RXY0; Eukaryota.
DR HOGENOM; CLU_317886_0_0_1; -.
DR InParanoid; P42835; -.
DR OMA; QYAQHTS; -.
DR BioCyc; YEAST:G3O-33311-MON; -.
DR PRO; PR:P42835; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42835; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030428; C:cell septum; IDA:SGD.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0008810; F:cellulase activity; TAS:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell wall; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Mitosis; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1020
FT /note="Protein EGT2"
FT /id="PRO_0000021159"
FT PROPEP 1021..1041
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372451"
FT REPEAT 457..492
FT /note="1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 577..606
FT /note="2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 613..647
FT /note="3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 716..745
FT /note="4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 773..802
FT /note="5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 811..840
FT /note="6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 849..886
FT /note="7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 887..924
FT /note="8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 925..962
FT /note="9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 388..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..962
FT /note="9 X approximate repeats"
FT LIPID 1020
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 577
FT /note="T -> A (in Ref. 1, 2; CAA96259 and 3; CAA86371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1041 AA; 108525 MW; 64C987E1376581FA CRC64;
MNKLLLHLVR VISILGLANA LTQTQPILKD IQITDSYTKT KECTDPDHWF IIEGQLSIPK
GSQQNITFQV PDAFSSFPQE PFSIKHNSNS VATISRPDKS TNNFTISIPE KSSEDITTTF
NFLAQLTSDA KSKVTEPKSI VYSFYSENTM FNDVIDYVAK NTSAITTDGG IYKTNNTAWF
TVDLPMRTFR NPVYLTSQTS SSSDYVFDTS LTKFEVVTAV DSFNEPINAI PYTTVHDYST
EDEIRCLFNS TISGGLYFRV TYFTKKLSTS SISNTVELTY PDEGTSVRLL GKRDTSTTLA
SELYSESAAN IDSTTSDDTT SSDAAITPTY SNSTLSSYTS QSSAIPEVAV TASLSSGILS
STVDGASTSA DASMSAVSTV SSSSEQASSS SISLSAPSSS NSTFTTPSSS LSATETYSII
SSASISVTQA SYIDNSTTTA VTQSTSTIAV SSAEKLSSTL SYTSNVTISV SSATQHTTTP
SYVSNSTTLS SSSVLESVIS SPYLANTTVS GASSASQSTN PPYVSNSTTS SATQLATIAP
FAINITGTSI SSSITNTSSV SSTTSSLSSG PFVSNTTVAS GSYILTTTTE SAQLTEIGSL
IPISTITTST TTSGTDKTGS NKVASSTEIA QSIVNNSSLS VSTINTNAAT AAANARNATF
THATHSGSLQ PSYHSSSLLS STIDTKVTTA TTSTSRDGSS SLAFTTGLNQ SVVTGTDKSD
TYSVISSTES AQVTEYDSLL PISTLKPTVV TGTSRNSTFS MVSSTKLTEA TATDKGDAYS
VISSTQSAQV TEYGSMLPIS TLETPTVIMS TDESGYFTLT TCTESGQATE YGSLIPISTL
DGSVIYTFTG ESVVVGYSTT VGAAQYAQHT SLVPVSTIKG SKTSLSTEES VVAGYSTTVG
AAQYAQHTSL VPVSTIKGSK TSLSTEESVV AGYSTTVDSA QYAEHTNLVA IDTLKTSTFQ
KATATEVCVT CTALSSPHSA TLDAGTTISL PTSSSTSLST IITWYSSSTI KPPSISTYSG
AAGQLTIRIG SLLLGLISFL L
