LOCUS       NP_776114               1165 aa            linear   ROD 28-APR-2025
DEFINITION  folliculin-interacting protein 1 [Mus musculus].
ACCESSION   NP_776114 XP_109657
VERSION     NP_776114.2
DBSOURCE    REFSEQ: accession NM_173753.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Mao,Y., Jin,Z., Yang,J., Xu,D., Zhao,L., Kiram,A., Yin,Y., Zhou,D.,
            Sun,Z., Xiao,L., Zhou,Z., Yang,L., Fu,T., Xu,Z., Jia,Y., Chen,X.,
            Niu,F.N., Li,X., Zhu,Z. and Gan,Z.
  TITLE     Muscle-bone cross-talk through the FNIP1-TFEB-IGF2 axis is
            associated with bone metabolism in human and mouse
  JOURNAL   Sci Transl Med 16 (750), eadk9811 (2024)
   PUBMED   38838134
  REMARK    GeneRIF: Muscle-bone cross-talk through the FNIP1-TFEB-IGF2 axis is
            associated with bone metabolism in human and mouse.
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Xiao,L., Yin,Y., Sun,Z., Liu,J., Jia,Y., Yang,L., Mao,Y., Peng,S.,
            Xie,Z., Fang,L., Li,J., Xie,X. and Gan,Z.
  TITLE     AMPK phosphorylation of FNIP1 (S220) controls mitochondrial
            function and muscle fuel utilization during exercise
  JOURNAL   Sci Adv 10 (6), eadj2752 (2024)
   PUBMED   38324677
  REMARK    GeneRIF: AMPK phosphorylation of FNIP1 (S220) controls
            mitochondrial function and muscle fuel utilization during exercise.
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Sun,Z., Yang,L., Kiram,A., Yang,J., Yang,Z., Xiao,L., Yin,Y.,
            Liu,J., Mao,Y., Zhou,D., Yu,H., Zhou,Z., Xu,D., Jia,Y., Ding,C.,
            Guo,Q., Wang,H., Li,Y., Wang,L., Fu,T., Hu,S. and Gan,Z.
  TITLE     FNIP1 abrogation promotes functional revascularization of ischemic
            skeletal muscle by driving macrophage recruitment
  JOURNAL   Nat Commun 14 (1), 7136 (2023)
   PUBMED   37932296
  REMARK    GeneRIF: FNIP1 abrogation promotes functional revascularization of
            ischemic skeletal muscle by driving macrophage recruitment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1165)
  AUTHORS   Shillingford,J.M. and Shayman,J.A.
  TITLE     Functional TFEB activation characterizes multiple models of renal
            cystic disease and loss of polycystin-1
  JOURNAL   Am J Physiol Renal Physiol 324 (4), F404-F422 (2023)
   PUBMED   36794754
REFERENCE   5  (residues 1 to 1165)
  AUTHORS   Yin,Y., Xu,D., Mao,Y., Xiao,L., Sun,Z., Liu,J., Zhou,D., Xu,Z.,
            Liu,L., Fu,T., Ding,C., Guo,Q., Sun,W., Zhou,Z., Yang,L., Jia,Y.,
            Chen,X. and Gan,Z.
  TITLE     FNIP1 regulates adipocyte browning and systemic glucose homeostasis
            in mice by shaping intracellular calcium dynamics
  JOURNAL   J Exp Med 219 (5) (2022)
   PUBMED   35412553
  REMARK    GeneRIF: FNIP1 regulates adipocyte browning and systemic glucose
            homeostasis in mice by shaping intracellular calcium dynamics.
REFERENCE   6  (residues 1 to 1165)
  AUTHORS   Petit,C.S., Roczniak-Ferguson,A. and Ferguson,S.M.
  TITLE     Recruitment of folliculin to lysosomes supports the amino
            acid-dependent activation of Rag GTPases
  JOURNAL   J Cell Biol 202 (7), 1107-1122 (2013)
   PUBMED   24081491
REFERENCE   7  (residues 1 to 1165)
  AUTHORS   Betschinger,J., Nichols,J., Dietmann,S., Corrin,P.D., Paddison,P.J.
            and Smith,A.
  TITLE     Exit from pluripotency is gated by intracellular redistribution of
            the bHLH transcription factor Tfe3
  JOURNAL   Cell 153 (2), 335-347 (2013)
   PUBMED   23582324
REFERENCE   8  (residues 1 to 1165)
  AUTHORS   Baba,M., Keller,J.R., Sun,H.W., Resch,W., Kuchen,S., Suh,H.C.,
            Hasumi,H., Hasumi,Y., Kieffer-Kwon,K.R., Gonzalez,C.G.,
            Hughes,R.M., Klein,M.E., Oh,H.F., Bible,P., Southon,E.,
            Tessarollo,L., Schmidt,L.S., Linehan,W.M. and Casellas,R.
  TITLE     The folliculin-FNIP1 pathway deleted in human Birt-Hogg-Dube
            syndrome is required for murine B-cell development
  JOURNAL   Blood 120 (6), 1254-1261 (2012)
   PUBMED   22709692
REFERENCE   9  (residues 1 to 1165)
  AUTHORS   Park,H., Staehling,K., Tsang,M., Appleby,M.W., Brunkow,M.E.,
            Margineantu,D., Hockenbery,D.M., Habib,T., Liggitt,H.D., Carlson,G.
            and Iritani,B.M.
  TITLE     Disruption of Fnip1 reveals a metabolic checkpoint controlling B
            lymphocyte development
  JOURNAL   Immunity 36 (5), 769-781 (2012)
   PUBMED   22608497
REFERENCE   10 (residues 1 to 1165)
  AUTHORS   Hasumi,H., Baba,M., Hong,S.B., Hasumi,Y., Huang,Y., Yao,M.,
            Valera,V.A., Linehan,W.M. and Schmidt,L.S.
  TITLE     Identification and characterization of a novel
            folliculin-interacting protein FNIP2
  JOURNAL   Gene 415 (1-2), 60-67 (2008)
   PUBMED   18403135
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY239060.1, BC079892.1 and AL596127.12.
            
            On or before Nov 26, 2004 this sequence version replaced
            XP_109657.3, NP_776114.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079892.1, AK122574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 32.13 cM"
     Protein         1..1165
                     /product="folliculin-interacting protein 1"
                     /calculated_mol_wt=129995
     Region          41..159
                     /region_name="FNIP_N"
                     /note="Folliculin-interacting protein N-terminus;
                     pfam14636"
                     /db_xref="CDD:464228"
     Region          92..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:37079666; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          316..548
                     /region_name="FNIP_M"
                     /note="Folliculin-interacting protein middle domain;
                     pfam14637"
                     /db_xref="CDD:434087"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          608..615
                     /region_name="Cys degron.
                     /evidence=ECO:0000269|PubMed:32941802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          611..612
                     /region_name="KY-finger.
                     /evidence=ECO:0000269|PubMed:34562363"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          779..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          912..970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          928..1165
                     /region_name="Interaction with HSP90AA1.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            937
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            937
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF40; propagated from
                     UniProtKB/Swiss-Prot (Q68FD7.1)"
     Region          975..1161
                     /region_name="FNIP_C"
                     /note="Folliculin-interacting protein C-terminus;
                     pfam14638"
                     /db_xref="CDD:464229"
     CDS             1..1165
                     /gene="Fnip1"
                     /gene_synonym="A730024A03Rik"
                     /coded_by="NM_173753.4:119..3616"
                     /db_xref="CCDS:CCDS24698.1"
                     /db_xref="GeneID:216742"
                     /db_xref="MGI:MGI:2444668"
ORIGIN      
        1 maptlfqklf skrsglgapg rdardpdcaf swplpefdps qirlivyqdc errgrnvlfd
       61 ssvkrknedt svsklcndaq vkvfgkccql kpggdssssl dssitlssdg kdqcpkyqgs
      121 rcssdanmlg emmfgsvams ykgstlkihq irsppqlmls kvftartgss icgslntlqd
      181 slefinqdsn tlkadsstvs ngllgnigls qfcsprrafs eqgplrlirs asffavhsnp
      241 mdmpgrelne drdsgiarsa slsslfitpf pspnssltrs cassyqrrwr rsqttsleng
      301 vfprwsvees fnlsdescgp npgivrkkki aigvifslsk dedennkfne fffshfplfe
      361 shmnklksai eqamkmsrrs adasqrslay nrildaltef rtticnlytm prigepvwlt
      421 mmsgtpeknq lchrfmkeft flmenasknq flpalitavl tnhlawvptv mpngqppiki
      481 flekhssqsv gmlakthpyn plwaqlgdly gaigspvrla rtvvvgkrqd lvqrllyflt
      541 yfircselqe thllengede aivmpgtvit ttlekgeiee seyvlitmhr nkssllfkes
      601 eetrtpncnc kycshpvlgq ntenvsqper edtqdnskel lgisdecqki sppdcqeena
      661 vdvqqyrdkl rtcldtklet vvctgsapad kcvlsetcle preeswqnke lldsdnhtgt
      721 amrptgivve kkppdknvps afscevtqtk vtfligdsms pdsdtelrsq avvdqinrhh
      781 seplkedrgv adkhqeskit kdqsedsdtq nivsgescel pcwshsdpes mslfdeyfnd
      841 dsietrtidd vpvktstdsk eyccmleypk rlytktnkqk selckcietv hqdscnacfp
      901 qqdqrnslsi lvphgdkess dkknavgtew diprnessds algdsesedt gpdirrqagg
      961 ycggdqedwt eedeipfpgs klievsavqp nianfgrsll ggycssyvpd fvlqgignde
     1021 rlrqclvsdl shavqhpvld epiaeavcii admdkwtvqv assqrrvtdn klgkevlvss
     1081 lvsnllhstl qlykhnlspn fcvmhledrl qelyfkskml seylrgqmrv hvkelgvvlg
     1141 iessdlplla avasthspyv aqill
//
