P53076 (VID30_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar import and degradation protein 30

Alternative name(s):
Glucose-induced degradation protein 1

Gene names

Name:	VID30
Synonyms:	GID1
Ordered Locus Names:	YGL227W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	958 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in the negative regulation of gluconeogenesis. Required for both proteasome-dependent and vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Ref.3
Subcellular location	Nucleus. Cytoplasm Ref.4.
Miscellaneous	Present with 1500 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Contains 1 B30.2/SPRY domain. Contains 1 CTLH domain. Contains 1 LisH domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of gluconeogenesis Inferred from mutant phenotype Ref.3. Source: SGD proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.3. Source: SGD regulation of nitrogen utilization Inferred from mutant phenotype. Source: SGD vacuolar protein catabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	GID complex Inferred from direct assay. Source: SGD nucleus Inferred from direct assay Ref.4. Source: SGD vacuole Inferred from mutant phenotype. Source: GOC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 958	958	Vacuolar import and degradation protein 30		PRO_0000065829
Regions
	Domain	390 – 592	203	B30.2/SPRY
	Domain	710 – 742	33	LisH
	Domain	769 – 826	58	CTLH
	Compositional bias	165 – 185	21	Poly-Asp
	Compositional bias	450 – 453	4	Poly-Ser
Amino acid modifications
	Modified residue	147	1	Phosphoserine Ref.6 Ref.7
	Modified residue	246	1	Phosphoserine Ref.7
	Modified residue	248	1	Phosphoserine Ref.6 Ref.7
	Modified residue	277	1	Phosphoserine Ref.7
	Modified residue	453	1	Phosphoserine Ref.7
	Modified residue	469	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P53076 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 335ADD152949F8C8	FASTA	958	108,179
	10 20 30 40 50 60 MSEYMDDVDR EFINCLFPSY LLQQPVAYDL WILYLQHRKL FHKLKNTNLI NADENPTGVG 70 80 90 100 110 120 MGRTKLTALT RKEIWSKLMN LGVLGTISFE AVNDDYLIQV YKYFYPDVND FTLRFGVKDS 130 140 150 160 170 180 NKNSVRVMKA SSDMRKNAQE LLEPVLSERE MALNSNTSLE NDRNDDDDDD DDDDDDDDDD 190 200 210 220 230 240 DDDDDESDLE SLEGEVDTDT DDNNEGDGSD NHEEGGEEGS RGADADVSSA QQRAERVADP 250 260 270 280 290 300 WIYQRSRSAI NIETESRNLW DTSDKNSGLQ YYPPDQSPSS SFSSPRVSSG NDKNDNEATN 310 320 330 340 350 360 VLSNSGSKKK NSMIPDIYKI LGYFLPSRWQ AQPNNSLQLS QDGITHLQPN PDYHSYMTYE 370 380 390 400 410 420 RSSASSASTR NRLRTSFENS GKVDFAVTWA NKSLPDNKLT IFYYEIKVLS VTSTESAENS 430 440 450 460 470 480 NIVIGYKLVE NELMEATTKK SVSRSSVAGS SSSLGGSNNM SSNRVPSTSF TMEGTQRRDY 490 500 510 520 530 540 IYEGGVSAMS LNVDGSINKC QKYGFDLNVF GYCGFDGLIT NSTEQSKEYA KPFGRDDVIG 550 560 570 580 590 600 CGINFIDGSI FFTKNGIHLG NAFTDLNDLE FVPYVALRPG NSIKTNFGLN EDFVFDIIGY 610 620 630 640 650 660 QDKWKSLAYE HICRGRQMDV SIEEFDSDES EEDETENGPE ENKSTNVNED LMDIDQEDGA 670 680 690 700 710 720 AGNKDTKKLN DEKDNNLKFL LGEDNRFIDG KLVRPDVNNI NNLSVDDGSL PNTLNVMIND 730 740 750 760 770 780 YLIHEGLVDV AKGFLKDLQK DAVNVNGQHS ESKDVIRHNE RQIMKEERMV KIRQELRYLI 790 800 810 820 830 840 NKGQISKCIN YIDNEIPDLL KNNLELVFEL KLANYLVMIK KSSSKDDDEI ENLILKGQEL 850 860 870 880 890 900 SNEFIYDTKI PQSLRDRFSG QLSNVSALLA YSNPLVEAPK EISGYLSDEY LQERLFQVSN 910 920 930 940 950 NTILTFLHKD SECALENVIS NTRAMLSTLL EYNAFGSTNS SDPRYYKAIN FDEDVLNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways." Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D., Thumm M., Wolf D.H. Mol. Biol. Cell 14:1652-1663(2003) [PubMed: 12686616] [Abstract] Cited for: FUNCTION.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-248, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-246; SER-248; SER-277; SER-453 AND SER-469, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z72749 Genomic DNA. Translation: CAA96943.1. BK006941 Genomic DNA. Translation: DAA07891.1.
PIR	S64249.
RefSeq	NP_011287.1. NM_001181093.1.
3D structure databases
ProteinModelPortal	P53076.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6352N.
IntAct	P53076. 16 interactions.
MINT	MINT-692085.
STRING	P53076.
Proteomic databases
PeptideAtlas	P53076.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL227W; YGL227W; YGL227W.
GeneID	852624.
KEGG	sce:YGL227W.
NMPDR	fig|4932.3.peg.2390.
Organism-specific databases
CYGD	YGL227w.
SGD	S000003196. VID30.
Phylogenomic databases
eggNOG	fuNOG04513.
GeneTree	EFGT00050000002406.
HOGENOM	HBG204393.
OMA	INDYLIH.
OrthoDB	EOG4J6W02.
Gene expression databases
ArrayExpress	P53076.
Genevestigator	P53076.
GermOnline	YGL227W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001870. B30.2/SPRY. IPR008985. ConA-like_lec_gl. IPR006595. CTLH_C. IPR006594. LisH_dimerisation. IPR013144. Ran-bd_prot-like_CRA_domain. IPR018355. SPla/RYanodine_receptor_subgr. IPR003877. SPRY_rcpt. [Graphical view]
Pfam	PF00622. SPRY. 1 hit. [Graphical view]
SMART	SM00757. CRA. 1 hit. SM00668. CTLH. 1 hit. SM00667. LisH. 1 hit. SM00449. SPRY. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50188. B302_SPRY. 1 hit. PS50897. CTLH. 1 hit. PS50896. LISH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971844.

Entry information

Entry name

VID30_YEAST

Accession

Primary (citable) accession number: P53076
Secondary accession number(s): D6VVA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program