Reviewed, UniProtKB/Swiss-Prot P42835 (EGT2_YEAST)

Names and origin

Protein names

Recommended name:
    Protein EGT2
Alternative name(s):
    Early G1 transcript 2

Gene names

Name:	EGT2
Ordered Locus Names:	YNL327W
ORF Names:	N0320

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1041 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Seems to be involved in the correct timing of cell separation after cytokinesis, as separation of mutant daughter cells is delayed. Could either be an enzyme necessary for glucans-degradation of the cell wall at the neck region between mother and daughter cells or a regulatory protein controlling this metabolic step. Ref.1
Subcellular location	Secreted › cell wall Probable. Membrane; Lipid-anchor › GPI-anchor Potential. Note: Localizes to the septum of dividing cells.
Induction	Exclusively expressed between the end of mitosis and early G1; inactivated before cells pass start. Ref.1
Domain	The number of the intragenic tandem repeats varies between different S.cerevisiae strains.
Post-translational modification	The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cell wall Membrane Secreted
Domain	Repeat Signal
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cytokinesis Ref.1 Inferred from mutant phenotype. Source: SGD mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cellular bud Inferred from direct assay. Source: SGD extracellular region Inferred from electronic annotation. Source: UniProtKB-KW fungal-type cell wall Inferred from direct assay. Source: SGD
Molecular function	cellulase activity Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 1020	1000	Protein EGT2		PRO_0000021159
	Propeptide	1021 – 1041	21	Removed in mature form Potential		PRO_0000372451
Regions
	Repeat	457 – 492	36	1
	Repeat	577 – 606	30	2
	Repeat	613 – 647	35	3
	Repeat	716 – 745	30	4
	Repeat	773 – 802	30	5
	Repeat	811 – 840	30	6
	Repeat	849 – 886	38	7
	Repeat	887 – 924	38	8
	Repeat	925 – 962	38	9
	Region	457 – 962	506	9 X approximate repeats
	Compositional bias	301 – 764	464	Ser-rich
	Compositional bias	403 – 1003	601	Thr-rich
Amino acid modifications
	Lipidation	1020	1	GPI-anchor amidated glycine Potential
	Glycosylation	65	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	249	1	N-linked (GlcNAc...) Potential
	Glycosylation	332	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Glycosylation	435	1	N-linked (GlcNAc...) Potential
	Glycosylation	465	1	N-linked (GlcNAc...) Potential
	Glycosylation	485	1	N-linked (GlcNAc...) Potential
	Glycosylation	506	1	N-linked (GlcNAc...) Potential
	Glycosylation	526	1	N-linked (GlcNAc...) Potential
	Glycosylation	544	1	N-linked (GlcNAc...) Potential
	Glycosylation	556	1	N-linked (GlcNAc...) Potential
	Glycosylation	635	1	N-linked (GlcNAc...) Potential
	Glycosylation	636	1	N-linked (GlcNAc...) Potential
	Glycosylation	657	1	N-linked (GlcNAc...) Potential
	Glycosylation	709	1	N-linked (GlcNAc...) Potential
	Glycosylation	756	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P42835-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 01FECF8EAA8744CD	FASTA	1,041	108,495
	10 20 30 40 50 60 MNKLLLHLVR VISILGLANA LTQTQPILKD IQITDSYTKT KECTDPDHWF IIEGQLSIPK 70 80 90 100 110 120 GSQQNITFQV PDAFSSFPQE PFSIKHNSNS VATISRPDKS TNNFTISIPE KSSEDITTTF 130 140 150 160 170 180 NFLAQLTSDA KSKVTEPKSI VYSFYSENTM FNDVIDYVAK NTSAITTDGG IYKTNNTAWF 190 200 210 220 230 240 TVDLPMRTFR NPVYLTSQTS SSSDYVFDTS LTKFEVVTAV DSFNEPINAI PYTTVHDYST 250 260 270 280 290 300 EDEIRCLFNS TISGGLYFRV TYFTKKLSTS SISNTVELTY PDEGTSVRLL GKRDTSTTLA 310 320 330 340 350 360 SELYSESAAN IDSTTSDDTT SSDAAITPTY SNSTLSSYTS QSSAIPEVAV TASLSSGILS 370 380 390 400 410 420 STVDGASTSA DASMSAVSTV SSSSEQASSS SISLSAPSSS NSTFTTPSSS LSATETYSII 430 440 450 460 470 480 SSASISVTQA SYIDNSTTTA VTQSTSTIAV SSAEKLSSTL SYTSNVTISV SSATQHTTTP 490 500 510 520 530 540 SYVSNSTTLS SSSVLESVIS SPYLANTTVS GASSASQSTN PPYVSNSTTS SATQLATIAP 550 560 570 580 590 600 FAINITGTSI SSSITNTSSV SSTTSSLSSG PFVSNTAVAS GSYILTTTTE SAQLTEIGSL 610 620 630 640 650 660 IPISTITTST TTSGTDKTGS NKVASSTEIA QSIVNNSSLS VSTINTNAAT AAANARNATF 670 680 690 700 710 720 THATHSGSLQ PSYHSSSLLS STIDTKVTTA TTSTSRDGSS SLAFTTGLNQ SVVTGTDKSD 730 740 750 760 770 780 TYSVISSTES AQVTEYDSLL PISTLKPTVV TGTSRNSTFS MVSSTKLTEA TATDKGDAYS 790 800 810 820 830 840 VISSTQSAQV TEYGSMLPIS TLETPTVIMS TDESGYFTLT TCTESGQATE YGSLIPISTL 850 860 870 880 890 900 DGSVIYTFTG ESVVVGYSTT VGAAQYAQHT SLVPVSTIKG SKTSLSTEES VVAGYSTTVG 910 920 930 940 950 960 AAQYAQHTSL VPVSTIKGSK TSLSTEESVV AGYSTTVDSA QYAEHTNLVA IDTLKTSTFQ 970 980 990 1000 1010 1020 KATATEVCVT CTALSSPHSA TLDAGTTISL PTSSSTSLST IITWYSSSTI KPPSISTYSG 1030 1040 AAGQLTIRIG SLLLGLISFL L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"EGT2 gene transcription is induced predominantly by Swi5 in early G1." Kovacech B., Nasmyth K., Schuster T. Mol. Cell. Biol. 16:3264-3274(1996) [PubMed: 8668141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION.
[2]	"Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames." Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C. Yeast 11:567-572(1995) [PubMed: 7645347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1676.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae." Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K. Mol. Gen. Genet. 258:53-59(1998) [PubMed: 9613572] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"GPI7 involved in glycosylphosphatidylinositol biosynthesis is essential for yeast cell separation." Fujita M., Yoko-o T., Okamoto M., Jigami Y. J. Biol. Chem. 279:51869-51879(2004) [PubMed: 15452134] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Intragenic tandem repeats generate functional variability." Verstrepen K.J., Jansen A., Lewitter F., Fink G.R. Nat. Genet. 37:986-990(2005) [PubMed: 16086015] [Abstract] Cited for: REPEATS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z46259 Genomic DNA. Translation: CAA86371.1. Z71603 Genomic DNA. Translation: CAA96259.1.
PIR	S55862.
RefSeq	NP_014072.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4267N.
IntAct	P42835. 2 interactions.
STRING	P42835.
Genome annotation databases
Ensembl	YNL327W; YNL327W; YNL327W; Saccharomyces cerevisiae. [Genome view]
GeneID	855389.
KEGG	sce:YNL327W.
NMPDR	fig|4932.3.peg.5134.
Organism-specific databases
CYGD	YNL327w.
SGD	S000005271. EGT2.
Phylogenomic databases
HOGENOM	P42835.
OrthoDB	EOG9W0ZXF
Gene expression databases
ArrayExpress	P42835.
Genevestigator	P42835.
GermOnline	YNL327W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	979196.

Entry information

Entry name

EGT2_YEAST

Accession

Primary (citable) accession number: P42835

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)