NPRL2_HUMAN
ID NPRL2_HUMAN Reviewed; 380 AA.
AC Q8WTW4; A8K831; Q6FGS2; Q9Y249; Q9Y497;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=GATOR complex protein NPRL2 {ECO:0000305};
DE AltName: Full=Gene 21 protein {ECO:0000303|Ref.1};
DE Short=G21 protein {ECO:0000303|Ref.1};
DE AltName: Full=Nitrogen permease regulator 2-like protein {ECO:0000303|PubMed:11085536};
DE Short=NPR2-like protein {ECO:0000303|PubMed:11085536};
DE AltName: Full=Tumor suppressor candidate 4 {ECO:0000303|PubMed:18616680};
GN Name=NPRL2 {ECO:0000312|HGNC:HGNC:24969};
GN Synonyms=TUSC4 {ECO:0000303|PubMed:18616680};
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 [MRNA] (ISOFORMS 1 AND 2).
RA Kondo M., Sekido Y., Latif F., Cundiff S., Duh F.-M., Wei M.-H.,
RA Lerman M.I., Minna J.D.;
RT "Gene 21, a new candidate human tumor suppressor gene located in the 3p21.3
RT small cell lung cancer homozygous deletion region homologous to the yeast
RT nitrogen permease regulator NPR2.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Skin;
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 [7]
RP DISCUSSION OF SEQUENCE.
RX PubMed=11085536;
RG The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium;
RA Lerman M.I., Minna J.D.;
RT "The 630-kb lung cancer homozygous deletion region on human chromosome
RT 3p21.3: identification and evaluation of the resident candidate tumor
RT suppressor genes.";
RL Cancer Res. 60:6116-6133(2000).
RN [8]
RP DISCUSSION OF SEQUENCE.
RX PubMed=11980673;
RA Ji L., Nishizaki M., Gao B., Burbee D., Kondo M., Kamibayashi C., Xu K.,
RA Yen N., Atkinson E.N., Fang B., Lerman M.I., Roth J.A., Minna J.D.;
RT "Expression of several genes in the human chromosome 3p21.3 homozygous
RT deletion region by an adenovirus vector results in tumor suppressor
RT activities in vitro and in vivo.";
RL Cancer Res. 62:2715-2720(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH PDPK1.
RX PubMed=18616680; DOI=10.1111/j.1349-7006.2008.00874.x;
RA Kurata A., Katayama R., Watanabe T., Tsuruo T., Fujita N.;
RT "TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine
RT phosphorylation and its downstream signaling.";
RL Cancer Sci. 99:1827-1834(2008).
RN [10]
RP INTERACTION WITH NPRL3.
RX PubMed=19521502; DOI=10.1371/journal.pgen.1000515;
RA Neklesa T.K., Davis R.W.;
RT "A genome-wide screen for regulators of TORC1 in response to amino acid
RT starvation reveals a conserved Npr2/3 complex.";
RL PLoS Genet. 5:E1000515-E1000515(2009).
RN [11]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
RP PROTEINS.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A.,
RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=28199306; DOI=10.1038/nature21423;
RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K.,
RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M.,
RA Frankel W.N., Sabatini D.M.;
RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to
RT regulate mTORC1.";
RL Nature 543:438-442(2017).
RN [13]
RP INVOLVEMENT IN FFEVF2, VARIANTS FFEVF2 PRO-105; SER-110 AND HIS-214, AND
RP TISSUE SPECIFICITY.
RX PubMed=26505888; DOI=10.1002/ana.24547;
RG Epilepsy Electroclinical Study Group;
RA Ricos M.G., Hodgson B.L., Pippucci T., Saidin A., Ong Y.S., Heron S.E.,
RA Licchetta L., Bisulli F., Bayly M.A., Hughes J., Baldassari S., Palombo F.,
RA Santucci M., Meletti S., Berkovic S.F., Rubboli G., Thomas P.Q.,
RA Scheffer I.E., Tinuper P., Geoghegan J., Schreiber A.W., Dibbens L.M.;
RT "Mutations in the mammalian target of rapamycin pathway regulators NPRL2
RT and NPRL3 cause focal epilepsy.";
RL Ann. Neurol. 79:120-131(2016).
RN [14]
RP INVOLVEMENT IN FFEVF2, VARIANT FFEVF2 HIS-198, AND TISSUE SPECIFICITY.
RX PubMed=27173016; DOI=10.1111/epi.13391;
RA Weckhuysen S., Marsan E., Lambrecq V., Marchal C., Morin-Brureau M.,
RA An-Gourfinkel I., Baulac M., Fohlen M., Kallay Zetchi C., Seeck M.,
RA de la Grange P., Dermaut B., Meurs A., Thomas P., Chassoux F., Leguern E.,
RA Picard F., Baulac S.;
RT "Involvement of GATOR complex genes in familial focal epilepsies and focal
RT cortical dysplasia.";
RL Epilepsia 57:994-1003(2016).
CC -!- FUNCTION: As a component of the GATOR1 complex functions as an
CC inhibitor of the amino acid-sensing branch of the TORC1 pathway. The
CC GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB
CC within RRAGC-containing heterodimers, thereby deactivating RRAGs,
CC releasing mTORC1 from lysosomal surface and inhibiting mTORC1
CC signaling. The GATOR1 complex is negatively regulated by GATOR2 the
CC other GATOR subcomplex in this amino acid-sensing branch of the TORC1
CC pathway. {ECO:0000269|PubMed:23723238}.
CC -!- FUNCTION: Suppresses Src-dependent tyrosine phosphorylation and
CC activation of PDPK1 and its downstream signaling. Down-regulates PDPK1
CC kinase activity by interfering with tyrosine phosphorylation at 'Tyr-
CC 9', 'Tyr-373' and 'Tyr-376' residues. May act as a tumor suppressor.
CC Suppresses cell growth and enhances sensitivity to various anticancer
CC drugs. {ECO:0000269|PubMed:18616680}.
CC -!- SUBUNIT: Forms a heterodimer with NPRL3. Interacts with PDPK1. Within
CC the GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5,
CC NPRL2 and NPRL3. GATOR1 mediates the strong interaction of the GATOR
CC complex with RRAGA/RRAGC and RRAGB/RRAGC heterodimers.
CC {ECO:0000269|PubMed:18616680, ECO:0000269|PubMed:19521502,
CC ECO:0000269|PubMed:23723238}.
CC -!- INTERACTION:
CC Q8WTW4; Q12980: NPRL3; NbExp=6; IntAct=EBI-1043552, EBI-2650314;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:28199306}.
CC Note=Localization to lysosomes is amino acid-independent.
CC {ECO:0000269|PubMed:28199306}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WTW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WTW4-2; Sequence=VSP_010329, VSP_010330, VSP_010331;
CC -!- TISSUE SPECIFICITY: Most abundant in skeletal muscle, followed by
CC brain, liver and pancreas, with lower amounts in lung, kidney, placenta
CC and heart. Expressed in the frontal lobe cortex as well as in the
CC temporal, parietal, and occipital lobes (PubMed:27173016,
CC PubMed:26505888). Expressed in most lung cancer cell lines tested.
CC {ECO:0000269|PubMed:26505888, ECO:0000269|PubMed:27173016}.
CC -!- DISEASE: Note=Inactivating mutations and truncating deletions in the
CC genes encoding GATOR1 proteins, including NPRL2, are detected in
CC glioblastoma and ovarian tumors and are associated with loss of
CC heterozygosity events. Inactivation of GATOR1 proteins promotes
CC constitutive localization of mTORC1 to the lysosomal membrane and
CC blocks mTORC1 inactivation following amino acid withdrawal
CC (PubMed:23723238). {ECO:0000269|PubMed:23723238}.
CC -!- DISEASE: Epilepsy, familial focal, with variable foci 2 (FFEVF2)
CC [MIM:617116]: An autosomal dominant form of epilepsy characterized by
CC focal seizures arising from different cortical regions, including the
CC temporal, frontal, parietal, and occipital lobes. Seizure types
CC commonly include temporal lobe epilepsy, frontal lobe epilepsy, and
CC nocturnal frontal lobe epilepsy. Some patients may have intellectual
CC disability or autism spectrum disorders. Seizure onset usually occurs
CC in the first or second decades, although later onset has been reported,
CC and there is phenotypic variability within families. A subset of
CC patients have structural brain abnormalities. Penetrance of the
CC disorder is incomplete. {ECO:0000269|PubMed:26505888,
CC ECO:0000269|PubMed:27173016}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NPR2 family. {ECO:0000305}.
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DR EMBL; AF040707; AAC62535.1; -; mRNA.
DR EMBL; AF040708; AAC62536.1; -; mRNA.
DR EMBL; AK292196; BAF84885.1; -; mRNA.
DR EMBL; CR542035; CAG46832.1; -; mRNA.
DR EMBL; AC002481; AAB67310.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65106.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65107.1; -; Genomic_DNA.
DR EMBL; BC021984; AAH21984.1; -; mRNA.
DR EMBL; BC056861; AAH56861.1; -; mRNA.
DR CCDS; CCDS2826.1; -. [Q8WTW4-1]
DR RefSeq; NP_006536.3; NM_006545.4. [Q8WTW4-1]
DR PDB; 6CES; EM; 4.00 A; N=1-380.
DR PDB; 6CET; EM; 4.40 A; N=1-380.
DR PDB; 7T3A; EM; 4.00 A; B=1-380.
DR PDB; 7T3B; EM; 3.90 A; B=1-380.
DR PDB; 7T3C; EM; 4.00 A; B=1-380.
DR PDBsum; 6CES; -.
DR PDBsum; 6CET; -.
DR PDBsum; 7T3A; -.
DR PDBsum; 7T3B; -.
DR PDBsum; 7T3C; -.
DR AlphaFoldDB; Q8WTW4; -.
DR SMR; Q8WTW4; -.
DR BioGRID; 115885; 136.
DR ComplexPortal; CPX-6226; GATOR1 complex.
DR CORUM; Q8WTW4; -.
DR DIP; DIP-50746N; -.
DR IntAct; Q8WTW4; 15.
DR MINT; Q8WTW4; -.
DR STRING; 9606.ENSP00000232501; -.
DR iPTMnet; Q8WTW4; -.
DR PhosphoSitePlus; Q8WTW4; -.
DR BioMuta; NPRL2; -.
DR DMDM; 47117604; -.
DR EPD; Q8WTW4; -.
DR jPOST; Q8WTW4; -.
DR MassIVE; Q8WTW4; -.
DR MaxQB; Q8WTW4; -.
DR PaxDb; Q8WTW4; -.
DR PeptideAtlas; Q8WTW4; -.
DR PRIDE; Q8WTW4; -.
DR ProteomicsDB; 74610; -. [Q8WTW4-1]
DR ProteomicsDB; 74611; -. [Q8WTW4-2]
DR Antibodypedia; 30939; 296 antibodies from 34 providers.
DR DNASU; 10641; -.
DR Ensembl; ENST00000232501.8; ENSP00000232501.3; ENSG00000114388.14. [Q8WTW4-1]
DR GeneID; 10641; -.
DR KEGG; hsa:10641; -.
DR MANE-Select; ENST00000232501.8; ENSP00000232501.3; NM_006545.5; NP_006536.3.
DR UCSC; uc003daj.2; human. [Q8WTW4-1]
DR CTD; 10641; -.
DR DisGeNET; 10641; -.
DR GeneCards; NPRL2; -.
DR HGNC; HGNC:24969; NPRL2.
DR HPA; ENSG00000114388; Low tissue specificity.
DR MalaCards; NPRL2; -.
DR MIM; 607072; gene.
DR MIM; 617116; phenotype.
DR neXtProt; NX_Q8WTW4; -.
DR OpenTargets; ENSG00000114388; -.
DR Orphanet; 98820; Familial focal epilepsy with variable foci.
DR PharmGKB; PA165697981; -.
DR VEuPathDB; HostDB:ENSG00000114388; -.
DR eggNOG; KOG3789; Eukaryota.
DR GeneTree; ENSGT00390000001414; -.
DR HOGENOM; CLU_014995_0_0_1; -.
DR InParanoid; Q8WTW4; -.
DR OMA; YASMTHG; -.
DR OrthoDB; 500740at2759; -.
DR PhylomeDB; Q8WTW4; -.
DR TreeFam; TF106159; -.
DR PathwayCommons; Q8WTW4; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q8WTW4; -.
DR SIGNOR; Q8WTW4; -.
DR BioGRID-ORCS; 10641; 44 hits in 1076 CRISPR screens.
DR ChiTaRS; NPRL2; human.
DR GeneWiki; TUSC4; -.
DR GenomeRNAi; 10641; -.
DR Pharos; Q8WTW4; Tbio.
DR PRO; PR:Q8WTW4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WTW4; protein.
DR Bgee; ENSG00000114388; Expressed in granulocyte and 201 other tissues.
DR ExpressionAtlas; Q8WTW4; baseline and differential.
DR Genevisible; Q8WTW4; HS.
DR GO; GO:1990130; C:GATOR1 complex; IDA:SGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR InterPro; IPR009348; NPR2.
DR PANTHER; PTHR12991; PTHR12991; 2.
DR Pfam; PF06218; NPR2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Epilepsy;
KW GTPase activation; Lysosome; Membrane; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..380
FT /note="GATOR complex protein NPRL2"
FT /id="PRO_0000213319"
FT REGION 1..133
FT /note="Interaction with PDPK1"
FT /evidence="ECO:0000269|PubMed:18616680"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.3"
FT /id="VSP_010329"
FT VAR_SEQ 312..323
FT /note="KLIQFGLMKNLI -> SEENLLGHLGVT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.3"
FT /id="VSP_010330"
FT VAR_SEQ 324..380
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.3"
FT /id="VSP_010331"
FT VARIANT 105
FT /note="L -> P (in FFEVF2; dbSNP:rs886037965)"
FT /evidence="ECO:0000269|PubMed:26505888"
FT /id="VAR_077122"
FT VARIANT 110
FT /note="T -> S (in FFEVF2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26505888"
FT /id="VAR_077123"
FT VARIANT 198
FT /note="P -> H (in FFEVF2; unknown pathological
FT significance; dbSNP:rs745518585)"
FT /evidence="ECO:0000269|PubMed:27173016"
FT /id="VAR_077124"
FT VARIANT 214
FT /note="D -> H (in FFEVF2; unknown pathological
FT significance; dbSNP:rs149128231)"
FT /evidence="ECO:0000269|PubMed:26505888"
FT /id="VAR_077125"
FT CONFLICT 17
FT /note="P -> L (in Ref. 6; AAH21984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43658 MW; 5ECA201CE073F964 CRC64;
MGSGCRIECI FFSEFHPTLG PKITYQVPED FISRELFDTV QVYIITKPEL QNKLITVTAM
EKKLIGCPVC IEHKKYSRNA LLFNLGFVCD AQAKTCALEP IVKKLAGYLT TLELESSFVS
MEESKQKLVP IMTILLEELN ASGRCTLPID ESNTIHLKVI EQRPDPPVAQ EYDVPVFTKD
KEDFFNSQWD LTTQQILPYI DGFRHIQKIS AEADVELNLV RIAIQNLLYY GVVTLVSILQ
YSNVYCPTPK VQDLVDDKSL QEACLSYVTK QGHKRASLRD VFQLYCSLSP GTTVRDLIGR
HPQQLQHVDE RKLIQFGLMK NLIRRLQKYP VRVTREEQSH PARLYTGCHS YDEICCKTGM
SYHELDERLE NDPNIIICWK
