FNIP1_CHICK
ID FNIP1_CHICK Reviewed; 1157 AA.
AC Q5W4S4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Folliculin-interacting protein 1 {ECO:0000250|UniProtKB:Q8TF40};
GN Name=FNIP1 {ECO:0000250|UniProtKB:Q8TF40};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15626157; DOI=10.1089/jir.2004.24.600;
RA Avery S., Rothwell L., Degen W.D.J., Schijns V.E.J.C., Young J.,
RA Kaufman J., Kaiser P.;
RT "Characterization of the first nonmammalian T2 cytokine gene cluster: the
RT cluster contains functional single-copy genes for IL-3, IL-4, IL-13, and
RT GM-CSF, a gene for IL-5 that appears to be a pseudogene, and a gene
RT encoding another cytokinelike transcript, KK34.";
RL J. Interferon Cytokine Res. 24:600-610(2004).
CC -!- FUNCTION: Binding partner of the GTPase-activating protein FLCN:
CC involved in the cellular response to amino acid availability by
CC regulating the mTORC1 signaling cascade controlling the MiT/TFE factors
CC TFEB and TFE3 (By similarity). In low-amino acid conditions, component
CC of the lysosomal folliculin complex (LFC) on the membrane of lysosomes,
CC which inhibits the GTPase-activating activity of FLCN, thereby
CC inactivating mTORC1 and promoting nuclear translocation of TFEB and
CC TFE3. Upon amino acid restimulation, disassembly of the LFC complex
CC liberates the GTPase-activating activity of FLCN, leading to activation
CC of mTORC1 and subsequent cytoplasmic retention of TFEB and TFE3 (By
CC similarity). Required to promote FLCN recruitment to lysosomes and
CC interaction with Rag GTPases. In addition to its role in mTORC1
CC signaling, also acts as a co-chaperone of HSP90AA1/Hsp90: inhibits the
CC ATPase activity of HSP90AA1/Hsp90, leading to activate both kinase and
CC non-kinase client proteins of HSP90AA1/Hsp90. Acts as a scaffold to
CC load client protein FLCN onto HSP90AA1/Hsp90 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TF40, ECO:0000250|UniProtKB:Q9P278}.
CC -!- SUBUNIT: Homodimer and homomultimer. Heterodimer and heteromultimer
CC with FNIP2 (By similarity). Component of the lysosomal folliculin
CC complex (LFC) (By similarity). {ECO:0000250|UniProtKB:Q8TF40,
CC ECO:0000250|UniProtKB:Q9P278}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8TF40}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8TF40}. Note=Localizes to
CC lysosome membrane in amino acid-depleted conditions and relocalizes to
CC the cytosol upon refeeding. Colocalizes with FLCN in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8TF40}.
CC -!- SIMILARITY: Belongs to the FNIP family. {ECO:0000305}.
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DR EMBL; AJ621744; CAF34415.1; -; Genomic_DNA.
DR RefSeq; NP_001034403.1; NM_001039314.1.
DR AlphaFoldDB; Q5W4S4; -.
DR SMR; Q5W4S4; -.
DR STRING; 9031.ENSGALP00000010596; -.
DR PaxDb; Q5W4S4; -.
DR GeneID; 427642; -.
DR KEGG; gga:427642; -.
DR CTD; 96459; -.
DR VEuPathDB; HostDB:geneid_427642; -.
DR eggNOG; KOG3693; Eukaryota.
DR HOGENOM; CLU_003447_0_0_1; -.
DR InParanoid; Q5W4S4; -.
DR OrthoDB; 303571at2759; -.
DR PhylomeDB; Q5W4S4; -.
DR PRO; PR:Q5W4S4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0042030; F:ATPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR InterPro; IPR037545; DENN_FNIP1/2.
DR InterPro; IPR028086; FNIP_C_dom.
DR InterPro; IPR026156; FNIP_fam.
DR InterPro; IPR028085; FNIP_mid_dom.
DR InterPro; IPR028084; FNIP_N_dom.
DR Pfam; PF14638; FNIP_C; 1.
DR Pfam; PF14637; FNIP_M; 1.
DR Pfam; PF14636; FNIP_N; 1.
DR PRINTS; PR02073; FOLLICULNIP1.
DR PROSITE; PS51836; DENN_FNIP12; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lysosome; Membrane; Reference proteome.
FT CHAIN 1..1157
FT /note="Folliculin-interacting protein 1"
FT /id="PRO_0000308486"
FT DOMAIN 37..467
FT /note="uDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT DOMAIN 475..1083
FT /note="cDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT DOMAIN 1093..1148
FT /note="dDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT REGION 92..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 128311 MW; 86F9156F5C1C921F CRC64;
MESPLFELNS ALSAASSKSE AMLCSISSKG SWPLPEFDPS QIRLIVYQDC ERRGRNVLFD
SSAKRKIEDV SVSKLCSDAQ VRVFGKCCQL KPGGDSSSSL DSSINSSSSF SDAKEQCPKY
QGSRCSSDAN MLGEMMFGSV AMSYKGSTLK IHQIRSPPQL MLSKVFTART GSSIYGSLNT
LQDSLEFINQ DSNTLKPDHS TIMNGLLGNI VHSNPMDMPG REQNEDRDSG IARSASLSSL
LITPFPSPGS SFNKSCASSY QRRWRRSQTT SLENGVFPRW SMDESFNLSD DSSGPSPGIV
RKKKIAIGVI FSLSRDEDEN NKFNEFFFSH FPLFESHMNK LKSAIEQLCL VLLICLMLVF
KAMKMSRRSA DASQRSLAYN RIVDALNEFR TTICNLYTMP RIGEPVWLTM MSGTPEKNQL
CHRFMKEFTF LMENAAKNQF LPALLTAVLT NHLAWVPTVM PNGQPPIRIF LEKHSSQSVD
MLAKTHPYNP LWAQLGDLYG AIGSPVRLAK TVVVGKRHDL VQRLLYFLTY FIRCSELQET
HLLENGEDEA IVMPGTVITT TLEKGEVEES EYVLVTMHKN RGNLLPKESE EMRTPNCSCK
NCKCPISLAQ NIEGVSQQER EDAQNTPKVE LETSSDESRT IVPDDGQEDA ADGHQPRTCQ
DTKVESVVCT GSSSPEKRVL AESGLEATAN MWRNEDVLEA GSQAISATRS PGIAVEKKPP
DKLFCDAFPC SAAEAQTKVT FLIGDSMSPD SDIELRSQAV VEQIARHHSP PTAEEGVSAD
QNCEAKQTVE DQNRDCGTAE PFPQVASEHQ SWNPNAYNAE GMSLFDDNFT DDGSVETRTM
DDLPGQAAAE LLTHNSNLEF SKKLCTKTSK PPSEFCKFMD SVRQETYKNC FAEQDQREKI
SIRVPHGDRE NAEKKVAPGI DWDIPRNESS DSALGDSESE DAGHELTRPS SNYYGGEQED
WAEEYEIPFP GSKLVEVNSV QPSIANFGRS LLGGYCSSYV PDFVLQGIGS DEKLRHCLVS
DLSHAVQHPV LDEPIAEAVC IIADTDKWTV QVASSQRRMI DNKLGKEVLV SSLVSNLLHS
TLQLYKHNLS PNFCVMHLED RLQELYFKSK MLSEYLKGQM RVHVKELGVV LGIESSDLPL
LAAVASTHSP YVAQILL
