FNIP2_HUMAN
ID FNIP2_HUMAN Reviewed; 1114 AA.
AC Q9P278; Q05DC3; Q96I31; Q9H994;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Folliculin-interacting protein 2 {ECO:0000303|PubMed:18663353};
DE AltName: Full=FNIP1-like protein {ECO:0000303|PubMed:18663353};
DE AltName: Full=O6-methylguanine-induced apoptosis 1 protein {ECO:0000303|PubMed:19137017};
GN Name=FNIP2 {ECO:0000303|PubMed:18663353, ECO:0000312|HGNC:HGNC:29280};
GN Synonyms=FNIPL {ECO:0000303|PubMed:18663353},
GN KIAA1450 {ECO:0000303|PubMed:10819331},
GN MAPO1 {ECO:0000303|PubMed:19137017};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-650 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 787-983 (ISOFORM 1).
RC TISSUE=Lymph, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 663-1114 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH FLCN; PRKAA1; PRKAB1 AND PRKAG1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022;
RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A.,
RA Linehan W.M., Schmidt L.S.;
RT "Identification and characterization of a novel folliculin-interacting
RT protein FNIP2.";
RL Gene 415:60-67(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FLCN AND PRKAA1, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=18663353; DOI=10.1038/onc.2008.261;
RA Takagi Y., Kobayashi T., Shiono M., Wang L., Piao X., Sun G., Zhang D.,
RA Abe M., Hagiwara Y., Takahashi K., Hino O.;
RT "Interaction of folliculin (Birt-Hogg-Dube gene product) with a novel
RT Fnip1-like (FnipL/Fnip2) protein.";
RL Oncogene 27:5339-5347(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19137017; DOI=10.1038/onc.2008.462;
RA Komori K., Takagi Y., Sanada M., Lim T.H., Nakatsu Y., Tsuzuki T.,
RA Sekiguchi M., Hidaka M.;
RT "A novel protein, MAPO1, that functions in apoptosis triggered by O6-
RT methylguanine mispair in DNA.";
RL Oncogene 28:1142-1150(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723 AND SER-726, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION.
RX PubMed=25126726; DOI=10.4161/auto.29640;
RA Dunlop E.A., Seifan S., Claessens T., Behrends C., Kamps M.A., Rozycka E.,
RA Kemp A.J., Nookala R.K., Blenis J., Coull B.J., Murray J.T.,
RA van Steensel M.A., Wilkinson S., Tee A.R.;
RT "FLCN, a novel autophagy component, interacts with GABARAP and is regulated
RT by ULK1 phosphorylation.";
RL Autophagy 10:1749-1760(2014).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH HSP70; HSP90AA1; FLCN; STIP1; PTGES3;
RP CDC37; BRAF; GCR AND CDK4, AND TISSUE SPECIFICITY.
RX PubMed=27353360; DOI=10.1038/ncomms12037;
RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [11] {ECO:0007744|PDB:6ULG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) IN COMPLEX WITH FLCN
RP RRAGA; RRAGC; LAMTOR1; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5, AND
RP IDENTIFICATION IN THE LFC COMPLEX.
RX PubMed=31704029; DOI=10.1016/j.cell.2019.10.036;
RA Shen K., Rogala K.B., Chou H.T., Huang R.K., Yu Z., Sabatini D.M.;
RT "Cryo-EM structure of the human FLCN-FNIP2-Rag-Ragulator complex.";
RL Cell 179:1319-1329(2019).
RN [12] {ECO:0007744|PDB:6NZD}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH FLCN;
RP RRAGA; RRAGC; LAMTOR1; LAMTOR2; LAMTOR3; LAMTOR4 AND LAMTOR5,
RP IDENTIFICATION IN THE LFC COMPLEX, AND FUNCTION.
RX PubMed=31672913; DOI=10.1126/science.aax0364;
RA Lawrence R.E., Fromm S.A., Fu Y., Yokom A.L., Kim D.J., Thelen A.M.,
RA Young L.N., Lim C.Y., Samelson A.J., Hurley J.H., Zoncu R.;
RT "Structural mechanism of a Rag GTPase activation checkpoint by the
RT lysosomal folliculin complex.";
RL Science 366:971-977(2019).
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 (PubMed:18663353, PubMed:31672913). In low-amino acid
CC conditions, component of the lysosomal folliculin complex (LFC) on the
CC membrane of lysosomes, which inhibits the GTPase-activating activity of
CC FLCN, thereby inactivating mTORC1 and promoting nuclear translocation
CC of TFEB and TFE3 (PubMed:31672913). Upon amino acid restimulation,
CC disassembly of the LFC complex liberates the GTPase-activating activity
CC of FLCN, leading to activation of mTORC1 and subsequent cytoplasmic
CC retention of TFEB and TFE3 (PubMed:31672913). Together with FLCN,
CC regulates autophagy: following phosphorylation by ULK1, interacts with
CC GABARAP and promotes autophagy (PubMed:25126726). In addition to its
CC role in mTORC1 signaling, also acts as a co-chaperone of
CC HSP90AA1/Hsp90: inhibits the ATPase activity of HSP90AA1/Hsp90, leading
CC to activate both kinase and non-kinase client proteins of
CC HSP90AA1/Hsp90 (PubMed:18403135). Acts as a scaffold to load client
CC protein FLCN onto HSP90AA1/Hsp90 (PubMed:18403135). Competes with the
CC activating co-chaperone AHSA1 for binding to HSP90AA1, thereby
CC providing a reciprocal regulatory mechanism for chaperoning of client
CC proteins (PubMed:18403135). May play a role in the signal transduction
CC pathway of apoptosis induced by O6-methylguanine-mispaired lesions (By
CC similarity). {ECO:0000250|UniProtKB:Q80TD3,
CC ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353,
CC ECO:0000269|PubMed:25126726, ECO:0000269|PubMed:31672913}.
CC -!- SUBUNIT: Homodimer and homomultimer (PubMed:18403135, PubMed:27353360).
CC Heterodimer and heteromultimer with FNIP1 (PubMed:18403135,
CC PubMed:27353360). Interacts (via C-terminus) with FLCN (via C-terminus)
CC (PubMed:18403135, PubMed:18663353, PubMed:27353360). Phosphorylated
CC FLCN is preferentially bound (PubMed:18663353). Component of the
CC lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2),
CC RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD GTP-bound,
CC and Ragulator (PubMed:31704029, PubMed:31672913). Interacts with
CC PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase
CC (PubMed:18403135, PubMed:27353360). Interacts with HSP70, HSP90AA1,
CC STIP1, PTGES3, CDC37, BRAF, GCR and CDK4 (PubMed:27353360).
CC {ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353,
CC ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:31672913,
CC ECO:0000269|PubMed:31704029}.
CC -!- INTERACTION:
CC Q9P278; Q8NFG4: FLCN; NbExp=7; IntAct=EBI-7597109, EBI-2970160;
CC Q9P278; Q8TF40: FNIP1; NbExp=7; IntAct=EBI-7597109, EBI-2946919;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000305|PubMed:31672913}.
CC Cytoplasm {ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353,
CC ECO:0000269|PubMed:19137017}. Note=Colocalizes with FLCN in the
CC cytoplasm. {ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P278-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P278-2; Sequence=VSP_031656;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in muscle,
CC nasal mucosa, salivary gland, uvula, fat, liver, heart, placenta and
CC pancreas (PubMed:18403135, PubMed:18663353, PubMed:27353360).
CC Moderately expressed in the lung, small intestine, kidney and brain.
CC Lower levels detected in renal cell carcinoma than in normal kidney
CC tissue (PubMed:18403135). Higher levels detected in oncocytoma tumors
CC than in normal kidney. Higher levels detected in renal cell carcinoma
CC tumors than in normal kidney tissue (PubMed:27353360).
CC {ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353,
CC ECO:0000269|PubMed:27353360}.
CC -!- PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:18663353}.
CC -!- SIMILARITY: Belongs to the FNIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH16638.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA95974.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB040883; BAA95974.1; ALT_INIT; mRNA.
DR EMBL; BC007861; AAH07861.1; ALT_INIT; mRNA.
DR EMBL; BC016638; AAH16638.1; ALT_SEQ; mRNA.
DR EMBL; AK022968; BAB14338.1; ALT_INIT; mRNA.
DR CCDS; CCDS47155.1; -. [Q9P278-1]
DR RefSeq; NP_001310845.1; NM_001323916.1. [Q9P278-2]
DR RefSeq; NP_001332972.1; NM_001346043.1.
DR RefSeq; NP_065891.1; NM_020840.2. [Q9P278-1]
DR PDB; 6NZD; EM; 3.60 A; I=1-1114.
DR PDB; 6ULG; EM; 3.31 A; N=1-1114.
DR PDB; 7LSW; X-ray; 3.05 A; A/B/C/D/E/F=552-576.
DR PDB; 7LT6; X-ray; 1.80 A; A/B/C=558-576.
DR PDBsum; 6NZD; -.
DR PDBsum; 6ULG; -.
DR PDBsum; 7LSW; -.
DR PDBsum; 7LT6; -.
DR AlphaFoldDB; Q9P278; -.
DR SMR; Q9P278; -.
DR BioGRID; 121650; 17.
DR CORUM; Q9P278; -.
DR IntAct; Q9P278; 7.
DR MINT; Q9P278; -.
DR STRING; 9606.ENSP00000264433; -.
DR iPTMnet; Q9P278; -.
DR PhosphoSitePlus; Q9P278; -.
DR BioMuta; FNIP2; -.
DR DMDM; 189035874; -.
DR EPD; Q9P278; -.
DR jPOST; Q9P278; -.
DR MassIVE; Q9P278; -.
DR MaxQB; Q9P278; -.
DR PaxDb; Q9P278; -.
DR PeptideAtlas; Q9P278; -.
DR PRIDE; Q9P278; -.
DR ProteomicsDB; 83745; -. [Q9P278-1]
DR ProteomicsDB; 83746; -. [Q9P278-2]
DR Antibodypedia; 28193; 161 antibodies from 26 providers.
DR DNASU; 57600; -.
DR Ensembl; ENST00000264433.11; ENSP00000264433.6; ENSG00000052795.13. [Q9P278-1]
DR GeneID; 57600; -.
DR KEGG; hsa:57600; -.
DR MANE-Select; ENST00000264433.11; ENSP00000264433.6; NM_020840.3; NP_065891.1.
DR UCSC; uc003iqe.5; human. [Q9P278-1]
DR CTD; 57600; -.
DR DisGeNET; 57600; -.
DR GeneCards; FNIP2; -.
DR HGNC; HGNC:29280; FNIP2.
DR HPA; ENSG00000052795; Low tissue specificity.
DR MIM; 612768; gene.
DR neXtProt; NX_Q9P278; -.
DR OpenTargets; ENSG00000052795; -.
DR PharmGKB; PA162388758; -.
DR VEuPathDB; HostDB:ENSG00000052795; -.
DR eggNOG; KOG3693; Eukaryota.
DR GeneTree; ENSGT00390000009391; -.
DR HOGENOM; CLU_003447_0_0_1; -.
DR InParanoid; Q9P278; -.
DR OMA; SRCSFKP; -.
DR OrthoDB; 303571at2759; -.
DR PhylomeDB; Q9P278; -.
DR TreeFam; TF324090; -.
DR PathwayCommons; Q9P278; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q9P278; -.
DR SIGNOR; Q9P278; -.
DR BioGRID-ORCS; 57600; 6 hits in 1078 CRISPR screens.
DR ChiTaRS; FNIP2; human.
DR GenomeRNAi; 57600; -.
DR Pharos; Q9P278; Tbio.
DR PRO; PR:Q9P278; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9P278; protein.
DR Bgee; ENSG00000052795; Expressed in kidney epithelium and 195 other tissues.
DR ExpressionAtlas; Q9P278; baseline and differential.
DR Genevisible; Q9P278; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA damage; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1114
FT /note="Folliculin-interacting protein 2"
FT /id="PRO_0000320553"
FT DOMAIN 42..460
FT /note="uDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT DOMAIN 468..1040
FT /note="cDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT DOMAIN 1050..1105
FT /note="dDENN FNIP1/2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01180"
FT REGION 12..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..911
FT /note="Interaction with PRKAA1"
FT /evidence="ECO:0000269|PubMed:18663353"
FT REGION 585..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..35
FT /note="MAPTLLQKLFNKRGSSGSSAAASAQGRAPKEGPAF -> MCGGTANTTNQPE
FT SWQDSARCVSDAVPGAGRIYRALLCTKIKKHTGVDRSTDHTELDN (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031656"
FT VARIANT 298
FT /note="T -> S (in dbSNP:rs2276938)"
FT /id="VAR_045612"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6ULG"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:6ULG"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 337..359
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 365..390
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 399..405
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 485..491
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:7LSW"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:7LT6"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:7LT6"
FT HELIX 975..986
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 989..992
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 999..1002
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 1007..1010
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 1012..1014
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 1029..1043
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 1050..1071
FT /evidence="ECO:0007829|PDB:6ULG"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6ULG"
FT HELIX 1097..1102
FT /evidence="ECO:0007829|PDB:6ULG"
SQ SEQUENCE 1114 AA; 122115 MW; 8951340C11EE0D5B CRC64;
MAPTLLQKLF NKRGSSGSSA AASAQGRAPK EGPAFSWSCS EFDLNEIRLI VYQDCDRRGR
QVLFDSKAVQ KIEEVTAQKT EDVPIKISAK CCQGSSSVSS SSSSSISSHS SSGGSSHHAK
EQLPKYQYTR PASDVNMLGE MMFGSVAMSY KGSTLKIHYI RSPPQLMISK VFSARMGSFC
GSTNNLQDSF EYINQDPNLG KLNTNQNSLG PCRTGSNLAH STPVDMPSRG QNEDRDSGIA
RSASLSSLLI TPFPSPSSST SSSSSYQRRW LRSQTTSLEN GIIPRRSTDE TFSLAEETCS
SNPAMVRRKK IAISIIFSLC EKEEAQRNFQ DFFFSHFPLF ESHMNRLKSA IEKAMISCRK
IAESSLRVQF YVSRLMEALG EFRGTIWNLY SVPRIAEPVW LTMMSGTLEK NQLCQRFLKE
FTLLIEQINK NQFFAALLTA VLTYHLAWVP TVMPVDHPPI KAFSEKRTSQ SVNMLAKTHP
YNPLWAQLGD LYGAIGSPVR LTRTVVVGKQ KDLVQRILYV LTYFLRCSEL QENQLTWSGN
HGEGDQVLNG SKIITALEKG EVEESEYVVI TVRNEPALVP PILPPTAAER HNPWPTGFPE
CPEGTDSRDL GLKPDKEANR RPEQGSEACS AGCLGPASDA SWKPQNAFCG DEKNKEAPQD
GSSRLPSCEV LGAGMKMDQQ AVCELLKVEM PTRLPDRSVA WPCPDRHLRE KPSLEKVTFQ
IGSFASPESD FESRMKKMEE RVKACGPSLE ASEAADVAQD PQVSRSPFKP GFQENVCCPQ
NRLSEGDEGE SDKGFAEDRG SRNDMAADIA GQLSHAADLG TASHGAGGTG GRRLEATRGL
YVKAAEGPVL EPVAPRCVQR GPGLVAGANI PCGDDNKKAN FRTEGDIPRN ESSDSALGDS
DDEACASAML DLGHGGDRTG GSLEVELPLP RSQSISTQNV RNFGRSLLAG YCPTYMPDLV
LHGTGSDEKL KQCLVADLVH TVHHPVLDEP IAEAVCIIAD TDKWSVQVAT SQRKVTDNMK
LGQDVLVSSQ VSSLLQSILQ LYKLHLPADF CIMHLEDRLQ EMYLKSKMLS EYLRGHTRVH
VKELGVVLGI ESNDLPLLTA IASTHSPYVA QILL
