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P25568 (ATG22_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy-related protein 22
Gene names
Name:ATG22
Synonyms:AUT4
Ordered Locus Names:YCL038C
ORF Names:YCL38C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vacuolar effluxer which mediate the efflux of leucine and other amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation. Ref.3 Ref.4 Ref.6

Subcellular location

Vacuole membrane; Multi-pass membrane protein. Note: Vacuole and punctate structures. Ref.6

Sequence similarities

Belongs to the ATG22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Autophagy-related protein 22
PRO_0000207629

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11921Helical; Potential
Topological domain120 – 13011Vacuolar Potential
Transmembrane131 – 15121Helical; Potential
Topological domain152 – 1532Cytoplasmic Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 21036Vacuolar Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 24110Cytoplasmic Potential
Transmembrane242 – 26221Helical; Potential
Topological domain263 – 31856Vacuolar Potential
Transmembrane319 – 33921Helical; Potential
Topological domain340 – 35213Cytoplasmic Potential
Transmembrane353 – 37321Helical; Potential
Topological domain374 – 38815Vacuolar Potential
Transmembrane389 – 40921Helical; Potential
Topological domain410 – 4178Cytoplasmic Potential
Transmembrane418 – 43821Helical; Potential
Topological domain439 – 48547Vacuolar Potential
Transmembrane486 – 50621Helical; Potential
Topological domain507 – 52822Cytoplasmic Potential

Amino acid modifications

Modified residue2781Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P25568 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: FC26CAFD581A66DB

FASTA52858,844
        10         20         30         40         50         60 
MSYGTINDMN ESVTNYRIKK AQNNIKGWYA YSFSSEPFVV SAVSTYIPLL LQQFASINGV 

        70         80         90        100        110        120 
KVHDHSIPCL SETGSDSDKC VLGLFNNRIF VDTSSFALYV FSLSVLFQTI IVISVSGIVD 

       130        140        150        160        170        180 
LWGSVKFKGR ILVWFGIVGA LSTVAISKLN DTQIYSLAGL YIVANGCFGV INVVGNSLLP 

       190        200        210        220        230        240 
IFVKDSLKCQ SQGAYEPDKV DSLTTVISGR GASLGYSSAL IVQIVSMFLV ASKKGSKQDV 

       250        260        270        280        290        300 
QVAVLFVGIW WFVWQLPMIW LIDDVTIPIR VDDSTLASAR SPYPGEQDAL GQLNWKNYLS 

       310        320        330        340        350        360 
YGWVSLFESF KHARLLKDVM IFLIAWFIIS DSITTINSTA VLFSKAELHM STLNLIMISV 

       370        380        390        400        410        420 
LTVVNAMLGA FMIPQFLATK FRWTSSQTLM YIIIWASFIP FYGILGFFFN AFGLKHKFEM 

       430        440        450        460        470        480 
FLLAIWYGLS LGGLSAVSRS VFSLIVPPGK ESTFFSMFSI TDKGSSILGP FLVGLLTDKT 

       490        500        510        520 
HNIRYSFYFF FLLLMLSLPV LNCLDVKRGR REAEELSQVL PESERRLD 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway."
Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.
J. Biol. Chem. 271:17621-17624(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The breakdown of autophagic vesicles inside the vacuole depends on Aut4p."
Suriapranata I., Epple U.D., Bernreuther D., Bredschneider M., Sovarasteanu K., Thumm M.
J. Cell Sci. 113:4025-4033(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"A unified nomenclature for yeast autophagy-related genes."
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.
Dev. Cell 5:539-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[6]"Atg22 recycles amino acids to link the degradative and recycling functions of autophagy."
Yang Z., Huang J., Geng J., Nair U., Klionsky D.J.
Mol. Biol. Cell 17:5094-5104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAA42378.1.
BK006937 Genomic DNA. Translation: DAA07446.1.
PIRS19366.
RefSeqNP_009892.1. NM_001178683.1.

3D structure databases

ProteinModelPortalP25568.
SMRP25568. Positions 420-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30945. 16 interactions.
DIPDIP-4976N.
IntActP25568. 3 interactions.
MINTMINT-478200.
STRING4932.YCL038C.

Protein family/group databases

TCDB2.A.1.24.1. the major facilitator superfamily (mfs).
9.A.15.1.1. the autophagy-related phagophore-formation transporter (apt) family.

Proteomic databases

PaxDbP25568.
PeptideAtlasP25568.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL038C; YCL038C; YCL038C.
GeneID850319.
KEGGsce:YCL038C.

Organism-specific databases

CYGDYCL038c.
SGDS000000543. ATG22.

Phylogenomic databases

eggNOGCOG2270.
HOGENOMHOG000034115.
KOK06902.
OMAIRPAFWF.
OrthoDBEOG71GB3P.

Enzyme and pathway databases

BioCycYEAST:G3O-29297-MONOMER.

Gene expression databases

GenevestigatorP25568.

Family and domain databases

InterProIPR024671. Atg22-like.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF11700. ATG22. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
ProtoNetSearch...

Other

NextBio965727.

Entry information

Entry nameATG22_YEAST
AccessionPrimary (citable) accession number: P25568
Secondary accession number(s): D6VQX7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: March 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families