ID   A0A8C4MM62_EQUAS        Unreviewed;       578 AA.
AC   A0A8C4MM62;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   02-SEP-2026, entry version 15.
DE   RecName: Full=Folliculin {ECO:0000256|ARBA:ARBA00021824};
GN   Name=FLCN {ECO:0000313|Ensembl:ENSEASP00005025924.2};
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005025924.2, ECO:0000313|Proteomes:UP000694387};
RN   [1] {ECO:0000313|Ensembl:ENSEASP00005025924.2, ECO:0000313|Proteomes:UP000694387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33293529;
RA   Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA   Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA   C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA   J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA   Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA   Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA   S., Zhou, X. and Zhong, J.;
RT   "Donkey genomes provide new insights into domestication and selection for
RT   coat color.";
RL   Nat. Commun. 11:6014-6014(2020).
RN   [2] {ECO:0000313|Ensembl:ENSEASP00005025924.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBUNIT: Interacts (via C-terminus) with FNIP1 or FNIP2 (via C-
CC       terminus). Component of the lysosomal folliculin complex (LFC),
CC       composed of FLCN, FNIP1 (or FNIP2), RagA/RRAGA or RagB/RRAGB GDP-bound,
CC       RagC/RRAGC or RagD/RRAGD GTP-bound, and Ragulator. Interaction with
CC       FNIP1 or FNIP2 mediates indirect interaction with the PRKAA1, PRKAB1
CC       and PRKAG1 subunits of 5'-AMP-activated protein kinase (AMPK).
CC       Interacts with HSP90AA1 in the presence of FNIP1. Interacts with HSP70,
CC       STUB1, CDC37, AHSA1, CCT2, STIP1, PTGES3 and PPP5C. Interacts with
CC       GABARAP; interaction takes place in the presence of FNIP1 and/or FNIP2.
CC       Interacts with RILP; the interaction is direct and promotes association
CC       between RILP and RAB34. Interacts with KIF3A and KIF3B. Interacts with
CC       lactate dehydrogenase LDHA, but not LDHB; the interaction is direct,
CC       may preferentially bind LDHA dimers rather than tetramers, and
CC       regulates LDHA activity, acting as an uncompetitive inhibitor.
CC       {ECO:0000256|ARBA:ARBA00064705}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
CC       Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004656}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the folliculin family.
CC       {ECO:0000256|ARBA:ARBA00009987}.
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DR   RefSeq; XP_014711839.1; XM_014856353.3.
DR   RefSeq; XP_014711841.1; XM_014856355.3.
DR   RefSeq; XP_044600332.1; XM_044744397.2.
DR   RefSeq; XP_044600334.1; XM_044744399.2.
DR   RefSeq; XP_044600335.1; XM_044744400.2.
DR   RefSeq; XP_044600336.1; XM_044744401.2.
DR   RefSeq; XP_070338318.1; XM_070482217.1.
DR   RefSeq; XP_070338319.1; XM_070482218.1.
DR   RefSeq; XP_070338320.1; XM_070482219.1.
DR   RefSeq; XP_070338321.1; XM_070482220.1.
DR   AlphaFoldDB; A0A8C4MM62; -.
DR   Ensembl; ENSEAST00005028144.2; ENSEASP00005025924.2; ENSEASG00005017691.2.
DR   GeneID; 106840675; -.
DR   KEGG; eai:106840675; -.
DR   CTD; 201163; -.
DR   GeneTree; ENSGT00390000009864; -.
DR   Proteomes; UP000694387; Chromosome 13.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-ARBA.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:TreeGrafter.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:TreeGrafter.
DR   FunFam; 1.10.10.1730:FF:000001; Folliculin; 1.
DR   FunFam; 3.40.50.12430:FF:000001; Folliculin; 1.
DR   Gene3D; 3.40.50.12430; -; 1.
DR   Gene3D; 1.10.10.1730; Folliculin; 1.
DR   InterPro; IPR037521; FLCN/SMCR8_DENN.
DR   InterPro; IPR044886; FLCN_DENN_C_sf.
DR   InterPro; IPR021713; Folliculin.
DR   InterPro; IPR037520; Folliculin/SMCR8_longin.
DR   InterPro; IPR032035; Folliculin_DENN.
DR   PANTHER; PTHR31441:SF2; FOLLICULIN; 1.
DR   PANTHER; PTHR31441; FOLLICULIN FAMILY MEMBER; 1.
DR   Pfam; PF11704; Folliculin; 1.
DR   Pfam; PF16692; Folliculin_C; 1.
DR   PROSITE; PS51834; DENN_FLCN_SMCR8; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694387}.
FT   DOMAIN          86..557
FT                   /note="UDENN FLCN/SMCR8-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51834"
FT   REGION          31..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..306
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  64380 MW;  4FB80CBC2A2B8C45 CRC64;
     MNAIVALCHF CELHGPRTLF CTEVLHAPLP QGAGTGDSPG QGEQAEEEEG GIQMSSRIRA
     HSPAEGASTE SSSPGPKKSD MCEGCRSLAA GHPGYISHDK ETSIKYVSHQ HPNHPQLFSI
     VRQACVRSLS CEVCPGREGP IFFGDEQHGF VFSHTFFIKD SLARGFQRWY SIIAIMMDRI
     YLINSWPFLL GKIRGIIDEL QGKALKVFEA EQFGCPQRAQ RMNTAFTPFL HQRNGNAARS
     LTSLTSDDNL WACLHTSFAW LLKACGSRLT EKLLEGAPTE DTLVQMEKLA DLEEESESWD
     NSEAEEEKTP VLPEGAEGRE LTKRPTDSSL LSDCGNWQPR KLSVFRSLRH MRQVLGAPSF
     RMLAWHVLMG NQVIWKSRDA DLVQSAFEVL RTMLPVGCVR IIPYSGQYEE AYRCNFLGLS
     PQVQIPSHVL SSEFAVIVEV HTATRSSLHP VGCEDDQSLS KYEFVVTSGS PVAADRVGPT
     ILNKMEAALT NQNLSVDVVD QCLVCLKEEW MNKVKVLFKF TKVDSRPKED TQKLLSILGA
     SEEDNVKLLK FWMTGLSKTY KSHLMSTVRS PSASEPRN
//