ATG22_VANPO
ID ATG22_VANPO Reviewed; 520 AA.
AC A7TFA9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Autophagy-related protein 22;
GN Name=ATG22; ORFNames=Kpol_2000p102;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Vacuole and punctate structures.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG22 family. {ECO:0000305}.
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DR EMBL; DS480382; EDO19134.1; -; Genomic_DNA.
DR RefSeq; XP_001646992.1; XM_001646942.1.
DR AlphaFoldDB; A7TFA9; -.
DR STRING; 436907.A7TFA9; -.
DR EnsemblFungi; EDO19134; EDO19134; Kpol_2000p102.
DR GeneID; 5547464; -.
DR KEGG; vpo:Kpol_2000p102; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_0_1; -.
DR InParanoid; A7TFA9; -.
DR OMA; MYPLGAV; -.
DR OrthoDB; 1460747at2759; -.
DR PhylomeDB; A7TFA9; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd17483; MFS_Atg22_like; 1.
DR Gene3D; 1.20.1250.20; -; 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..520
FT /note="Autophagy-related protein 22"
FT /id="PRO_0000318035"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 58470 MW; FA03727FFB26E7FD CRC64;
MRYGTLGEEI NTTEVTDEFE TLQTIKRTKQ NIVGWYFYSF SSEPFVVSAI ATYIPLLLEQ
FARHNGVTLE DHSVHCTADH DKCVLGLFSN RIYIDTSSFA LYTFSVSVFF QTLVVITVSG
VVDIWNTVTF KRNVLLLFGI IGALSTILIS RIYNTQYYML AFLCILSNSC YGVVNVVGNS
LLPLFVSEYL QHNSSSLDER DNVDILTTLI SGRGASIGYS SALVVQIISI FLIKKSKSSE
NIQVATLFVG IWWLIWQLPM SWLLQDSPIS ADVTPEDMDN LSIHKPKKWI FKFSNLKHGW
SSLFQALKHA KLLKDVVIFL VGWFIVSDSV TTINSTAILF AKTELKMSTL SLIVLSILTM
INAILGAFTI PQFISRKFQL PGEKLLIYII LWASFIPFYG ILGFVFKNIG LKHKFEMFIT
AIWYGISLGG LSAVSRSVFS LIIPRGQEST FFSIFNVTDK GSSILGPLLI GLITDYTHDI
RYSFFLLFAL LILAIPIFHL LDVERGKKEA SSLQKIPIAD