ID   LST4_ASHGO              Reviewed;         691 AA.
AC   Q757Y7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Protein LST4;
GN   Name=LST4; OrderedLocusNames=AEL127C; ORFNames=AGOS_AEL127C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 530; 533 AND 536.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Involved in extracellular amino acid uptake. Required for the
CC       protein trafficking from the Golgi to the plasma membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LST4 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52558.2; -; Genomic_DNA.
DR   RefSeq; NP_984734.2; NM_210088.2.
DR   AlphaFoldDB; Q757Y7; -.
DR   SMR; Q757Y7; -.
DR   STRING; 33169.AAS52558; -.
DR   PRIDE; Q757Y7; -.
DR   EnsemblFungi; AAS52558; AAS52558; AGOS_AEL127C.
DR   GeneID; 4620921; -.
DR   KEGG; ago:AGOS_AEL127C; -.
DR   eggNOG; ENOG502QPJF; Eukaryota.
DR   HOGENOM; CLU_010482_0_0_1; -.
DR   InParanoid; Q757Y7; -.
DR   OMA; NMVVANK; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:1990877; C:FNIP-folliculin RagC/D GAP; IEA:EnsemblFungi.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR037545; DENN_FNIP1/2.
DR   InterPro; IPR041153; Longin_2.
DR   Pfam; PF18639; Longin_2; 1.
DR   PROSITE; PS51836; DENN_FNIP12; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..691
FT                   /note="Protein LST4"
FT                   /id="PRO_0000324404"
FT   DOMAIN          67..243
FT                   /note="uDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          251..601
FT                   /note="cDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          607..687
FT                   /note="dDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   REGION          17..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  77517 MW;  DF894FF546D13434 CRC64;
     MLGRLLRTNS FIDLLGSFPN GKDDGKGPQP HHEATPPPSS MHMPDELRTL LYGCRKVEGE
     GRGGEGRGSG TFRLVVAQEL GQMMSRDNYQ VVLDCGGTRA AVGSGGAEMP LSELKEYIFG
     SPVRLSDRCR SDKLKLSRGA RVIVVTRIFY TGYAGNARRL AVCCCIPEQF LTVVTECWSQ
     VSAWFDEVQD VLMPLLEAEP LLPKDLRVSA PAQVDVLLHK FYRHLILPLH GLLETHRLFL
     YPADSLDFVT AWFREVFNWL EVKDGHRLKF LPALLGKLRH DAAAELLHNR SSRIVVMSGN
     VTVANKLIFI LSAFLRPRYS GQVHYVDDGL AARNVELKEA PADPKYSSTI TSKGWEIPRK
     RSRSSVLSKS SDETSFAHVF LPSSLRSTNS LQYISSSLNS QYGSYGSWFK KTIPLGHSPR
     INESPDNTFM HHHTNSTSSL QQQQAGTCAS GNNASSVTTS TTPNTNRWSQ GSPSISEYEE
     YPWLGYGTAP SGAPSKSRIQ KVNMPRNSNR VHDKKLLHER FVSICGDVQE VDFHTSPATE
     SYGAILEVPI LEELSFPSQE LLPRYSSYLP TLDPAFQVQA CPITSNTERR LVDCMKQDLH
     NAEYSRTLLI SLRSREIKEI TITKDPSTKT IVQRTKKIFL NGKPGHVSQK LHEEIHFVDN
     HLTATWKKWE DPVESEDKTK LFITSFHELM K