VID22_YEAST
ID VID22_YEAST Reviewed; 901 AA.
AC Q05934; D6VZ10;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Vacuolar import and degradation protein 22;
GN Name=VID22; OrderedLocusNames=YLR373C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11641409; DOI=10.1074/jbc.m109222200;
RA Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L.;
RT "Cyclophilin A mediates Vid22p function in the import of fructose-1,6-
RT bisphosphatase into Vid vesicles.";
RL J. Biol. Chem. 276:48017-48026(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11861771; DOI=10.1242/jcs.115.3.655;
RA Brown C.R., McCann J.A., Hung G.G.-C., Elco C.P., Chiang H.-L.;
RT "Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-
RT bisphosphatase degradation pathway.";
RL J. Cell Sci. 115:655-666(2002).
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).
CC -!- FUNCTION: Has a role in the negative regulation of gluconeogenesis.
CC Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate
CC vacuole import and degradation (Vid) vesicles. This is an indirect role
CC and requires cyclophilin A. {ECO:0000269|PubMed:11641409,
CC ECO:0000269|PubMed:11861771}.
CC -!- INTERACTION:
CC Q05934; Q02457: TBF1; NbExp=2; IntAct=EBI-30350, EBI-19005;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC Nucleus.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11861771}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VID22 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U19103; AAB67577.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09676.1; -; Genomic_DNA.
DR PIR; S51391; S51391.
DR RefSeq; NP_013477.1; NM_001182262.1.
DR AlphaFoldDB; Q05934; -.
DR BioGRID; 31633; 416.
DR DIP; DIP-4650N; -.
DR IntAct; Q05934; 4.
DR MINT; Q05934; -.
DR STRING; 4932.YLR373C; -.
DR iPTMnet; Q05934; -.
DR MaxQB; Q05934; -.
DR PaxDb; Q05934; -.
DR PRIDE; Q05934; -.
DR EnsemblFungi; YLR373C_mRNA; YLR373C; YLR373C.
DR GeneID; 851088; -.
DR KEGG; sce:YLR373C; -.
DR SGD; S000004365; VID22.
DR VEuPathDB; FungiDB:YLR373C; -.
DR eggNOG; ENOG502RKC9; Eukaryota.
DR GeneTree; ENSGT00940000176412; -.
DR HOGENOM; CLU_008135_0_0_1; -.
DR InParanoid; Q05934; -.
DR OMA; MNLLAMF; -.
DR BioCyc; YEAST:G3O-32442-MON; -.
DR PRO; PR:Q05934; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05934; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Metal-binding; Nucleus;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..901
FT /note="Vacuolar import and degradation protein 22"
FT /id="PRO_0000270928"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 66..122
FT /note="BED-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 901 AA; 102500 MW; D1AEFAFAE8802FC7 CRC64;
MRAMDTQVQS AERGLVLPPM NSTVSSATAA TTATNTDTDT DGDRDEERES LAEDGSEWVP
AYMLTRDRSR YLGHFLGVDK MLEAVKCKYC GVIIRRQGNS ISMAEASQTH LWSTHKIDPN
ANYYSGWTGV EAGSTFMVRP PLKNHQGGSA TTNSIANLLE IDEDFLKRTR EKEMALPLVQ
SLAIIIASEN LPLSFVDNTA VRLLINQNAN SLSFIDHDLI LNAIRSIAYN LDRIIQRTAL
RNNSDLSLII DKNYLLMDPT DRSNQLSNRL KNQLFEMQKI NFFSLSHSVW NNTISILSIQ
YYDDFHSQVK TLPLIIQNLH EYNNDPKLSI PAQLLKISQE LPGLQNTVIS ITLPRSQIVD
LLNVMDSQPF FPNTYTNAKN YYHNCIISII NSAILPLFGT PKSADITHPR QSSFSKEPLT
LLDSLIDLSN IDISNSIFSR INSFLDDLQS NSWQLDKFRS LCEKFGFEFV CSKFDLSRYS
TATVSLQTFL NLRPIIEEYQ SSIQIEKFNE IDFQIIDYLL ITLNSINRIL KFFTSSKSLN
FTYVLFAIMS IEKHLLSTLG SLQFQRLIAP FETFLSKIQE FKTILFSDDM NLLAMFLCPA
ILFEREVLEY SFHTISLSEI VDKLSTSIFS LLKRFLNLHT IGNVNNSHNT SNHSNMNIHT
DNQTNNINNR SGNNSDNNDN EHDNDNDNHS NSNTPASRID IDPTGGENSV LPEQQPQNSN
NNLSFGSLSD THHLSDSTIS KEIDSIFLQI IQEDLYDYLS TVNSIVPISY RSYCEQSNFI
RDSGRFKKRI ITEDSIIGEL EQPMNFIEEL LDIHVPVCNA FWSQYLDNDA GPIIRILFKI
MQCQSSSSIR GEYSFLNDFI PRVHPDLTQE IIKIKLFNDQ FVASKVDYDL DTLQTASQYL
P
