ID   ATG22_SCHPO             Reviewed;         529 AA.
AC   Q09812;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Autophagy-related protein 22;
GN   Name=atg22; ORFNames=SPAC2G11.13;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=21307582; DOI=10.1271/bbb.100747;
RA   Sugimoto N., Iwaki T., Chardwiriyapreecha S., Shimazu M., Kawano M.,
RA   Sekito T., Takegawa K., Kakinuma Y.;
RT   "Atg22p, a vacuolar membrane protein involved in the amino acid
RT   compartmentalization of Schizosaccharomyces pombe.";
RL   Biosci. Biotechnol. Biochem. 75:385-387(2011).
CC   -!- FUNCTION: Vacuolar effluxer which mediate the efflux of amino acids
CC       resulting from autophagic degradation. The release of autophagic amino
CC       acids allows the maintenance of protein synthesis and viability during
CC       nitrogen starvation. {ECO:0000269|PubMed:21307582}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:21307582};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:21307582}.
CC   -!- SIMILARITY: Belongs to the ATG22 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA91178.1; -; Genomic_DNA.
DR   PIR; T38579; S62468.
DR   RefSeq; NP_593093.1; NM_001018491.2.
DR   AlphaFoldDB; Q09812; -.
DR   BioGRID; 278317; 7.
DR   STRING; 4896.SPAC2G11.13.1; -.
DR   TCDB; 2.A.1.24.2; the major facilitator superfamily (mfs).
DR   iPTMnet; Q09812; -.
DR   PaxDb; Q09812; -.
DR   EnsemblFungi; SPAC2G11.13.1; SPAC2G11.13.1:pep; SPAC2G11.13.
DR   GeneID; 2541826; -.
DR   KEGG; spo:SPAC2G11.13; -.
DR   PomBase; SPAC2G11.13; atg22.
DR   VEuPathDB; FungiDB:SPAC2G11.13; -.
DR   eggNOG; ENOG502QR9I; Eukaryota.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   InParanoid; Q09812; -.
DR   OMA; QPWEIFP; -.
DR   PhylomeDB; Q09812; -.
DR   PRO; PR:Q09812; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR   GO; GO:0071627; C:integral component of fungal-type vacuolar membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0034639; F:L-amino acid efflux transmembrane transporter activity; ISO:PomBase.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IMP:PomBase.
DR   GO; GO:0032974; P:amino acid transmembrane export from vacuole; ISO:PomBase.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IMP:PomBase.
DR   CDD; cd17483; MFS_Atg22_like; 1.
DR   InterPro; IPR044738; Atg22.
DR   InterPro; IPR024671; Atg22-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF11700; ATG22; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..529
FT                   /note="Autophagy-related protein 22"
FT                   /id="PRO_0000207627"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  58642 MW;  18E2B0F2AFF88D8F CRC64;
     MNSPIQLHKK FSTTVWHVLS WILYAVGAGP TAIISMGVYV PLIVMKNAHD HGFLRTDHTI
     PCSLYPEEPC SLNIVGPLWI DVSSIVFAAS AISTFLQMAM MVSLGVICDY GNNRRYILFS
     CVIIGSISGI ILSWSPSSFL LGKIVFLILV DLNFIISQSC YDSFLPIFLR FYPITRGPIT
     LESALQDETD DLDSYITNTT IDSSEEEPYL LEHSLILNES APPADVEDEH KAKIAARLSS
     VGFGSFFGAA ILFQIIFTPI LYKTNNNPII LPITVTVCSC WWLILSTPLC TIVTLPVENH
     SSDAILTLLY NSVKESYHSF KHAMSISSIR LFLFSRLFIN CGIQTSLSSA VIFGKARLNL
     SNFQLTLLGM GISSFALLGT VIIPYLTEYF QLNSLQVVMI ISILLPMAPL YGLLGYIPGF
     ENAGIRTSAD VFRATLFFGF FLGGAHSYCR SVYAQLVPSG KETRFFALYA LISQTGVLFS
     HISLTLISNY TSDLRAVYIF VIVVMTLPLS SLWIMYQHSK TPNLHRSSS