ID   LST4_KLULA              Reviewed;         714 AA.
AC   Q6CXP4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Protein LST4;
GN   Name=LST4; OrderedLocusNames=KLLA0A06622g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382121; CAH02883.1; -; Genomic_DNA.
DR   RefSeq; XP_451295.1; XM_451295.1.
DR   PDB; 4ZY8; X-ray; 2.14 A; A/B/C/D=58-226.
DR   PDBsum; 4ZY8; -.
DR   AlphaFoldDB; Q6CXP4; -.
DR   SMR; Q6CXP4; -.
DR   STRING; 28985.XP_451295.1; -.
DR   PRIDE; Q6CXP4; -.
DR   EnsemblFungi; CAH02883; CAH02883; KLLA0_A06622g.
DR   GeneID; 2896770; -.
DR   KEGG; kla:KLLA0_A06622g; -.
DR   eggNOG; ENOG502QPJF; Eukaryota.
DR   HOGENOM; CLU_010482_0_0_1; -.
DR   InParanoid; Q6CXP4; -.
DR   OMA; NMVVANK; -.
DR   Proteomes; UP000000598; Chromosome A.
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   1: Evidence at protein level;
KW   3D-structure; Amino-acid transport; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..714
FT                   /note="Protein LST4"
FT                   /id="PRO_0000324406"
FT   DOMAIN          61..236
FT                   /note="uDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          244..620
FT                   /note="cDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   DOMAIN          634..712
FT                   /note="dDENN FNIP1/2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT   REGION          423..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   STRAND          134..144
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   STRAND          150..158
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           162..167
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           169..189
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           205..216
FT                   /evidence="ECO:0007829|PDB:4ZY8"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:4ZY8"
SQ   SEQUENCE   714 AA;  80951 MW;  02B6D45F6C5210F9 CRC64;
     MLGRLLRTSS LSEFVPFGSS NVTVGEEVFQ NEPFYMTDDL KTLLYGTRDK ALFERIANDR
     LHNGGFRLII SQELGHVTSR NNYQVVLDHS SVNFHTGAHI PLNELKDYIF GSSIRTIDYS
     ASSDKIKVVK SANIVLFTRI FYLNEKSTLR IAISCCVTDD VLPVLTECWP HISSFLDQCE
     NTLLKYLAKN DTQFLPHDWK ARNCIEVAAV LQTFQRKIIP LLSGYSDTPR LFLYPMDSIP
     YIKTWVKYVT NWIELKDGPR VRFLPILLAK LRYDFASLLK ENSNTRIVIL TGNMNVANRL
     IFILTAFLGP HFRGTLHKSI NSQGCPSPAG RKMSNMSGAS DFPFELKPSN SSITETNKGW
     EIPRIKRDPT FSVTSVSSDE TGVQTFIQPS SLKSGASSVQ YLSSSLNSAY GSYGSWFKKV
     AQSPSSRSNE SSHEVPPILH RNSSSTSFHQ QAVLGNINGS QRVTPQPSPT IAEYEEYPWF
     SPSPIARDQP RPEKRIPTPI SSYTTEKERR THLQSEIYDV DMKRTVNRLI DEDSLNDAFA
     DLVIDPPSYD TTVSNEKHGE IVEVNMASPR KQRNNQNQEL LRRFTSYTPH YNQWFQLQAC
     QITTESENKV IHSMKRDLTY ADQDPCKKDK STSTLLISLR SREIKQVTIV RDTNNRFIQR
     TKKILQNGKV GPVSRAMLSG IETTDQHLKK LMECNNDNEA LVSLFNDIVT CAST