ID   NUFP2_MOUSE             Reviewed;         692 AA.
AC   Q5F2E7; Q3TCE2; Q3V195; Q80TF1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=FMR1-interacting protein NUFIP2 {ECO:0000305|PubMed:12837692};
DE   AltName: Full=82 kDa FMRP-interacting protein;
DE            Short=82-FIP;
DE   AltName: Full=FMRP-interacting protein 2;
GN   Name=Nufip2; Synonyms=Kiaa1321;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Dendritic cell, Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH FMR1.
RX   PubMed=12837692; DOI=10.1093/hmg/ddg181;
RA   Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F.,
RA   Pastore A., Khandjian E.W., Mandel J.-L.;
RT   "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting
RT   protein, shows a cell cycle-dependent intracellular localization.";
RL   Hum. Mol. Genet. 12:1689-1698(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-215 AND SER-649, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-213; SER-215;
RP   SER-570; SER-626; SER-649 AND SER-652, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Binds RNA. {ECO:0000250|UniProtKB:Q7Z417}.
CC   -!- SUBUNIT: Interacts with FMR1 (via N-terminus) (PubMed:12837692).
CC       Interacts with DDX6 (By similarity). {ECO:0000250|UniProtKB:Q7Z417,
CC       ECO:0000269|PubMed:12837692}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837692}. Cytoplasm
CC       {ECO:0000269|PubMed:12837692}. Cytoplasm, Stress granule
CC       {ECO:0000250|UniProtKB:Q7Z417}. Note=Localized in both nucleus and
CC       cytoplasm in most neurons. In the cortex, distributed in a diffuse way
CC       in the nucleus and in the cytoplasm. Localized in the cytoplasm in
CC       neurons of the dentate gyrus in the olfactive bulb, in the ependymal
CC       epithelium and in the granular layer of the cerebellum. In Purkinje
CC       cells, distributed in both cell compartments and in nuclear dots
CC       adjacent to the nucleolus (PubMed:12837692).
CC       {ECO:0000250|UniProtKB:Q7Z417, ECO:0000269|PubMed:12837692}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5F2E7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5F2E7-2; Sequence=VSP_019729;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK122494; BAC65776.1; ALT_INIT; mRNA.
DR   EMBL; AK132603; BAE21256.1; -; mRNA.
DR   EMBL; AK152336; BAE31134.1; -; mRNA.
DR   EMBL; AK160601; BAE35905.1; -; mRNA.
DR   EMBL; AK170764; BAE42015.1; -; mRNA.
DR   EMBL; AL591136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS25083.1; -. [Q5F2E7-1]
DR   RefSeq; NP_001019376.1; NM_001024205.2. [Q5F2E7-1]
DR   RefSeq; XP_006534125.1; XM_006534062.3. [Q5F2E7-1]
DR   AlphaFoldDB; Q5F2E7; -.
DR   BioGRID; 212929; 35.
DR   IntAct; Q5F2E7; 4.
DR   MINT; Q5F2E7; -.
DR   STRING; 10090.ENSMUSP00000098365; -.
DR   GlyGen; Q5F2E7; 12 sites, 1 O-linked glycan (12 sites).
DR   iPTMnet; Q5F2E7; -.
DR   PhosphoSitePlus; Q5F2E7; -.
DR   EPD; Q5F2E7; -.
DR   jPOST; Q5F2E7; -.
DR   MaxQB; Q5F2E7; -.
DR   PaxDb; 10090-ENSMUSP00000098365; -.
DR   PeptideAtlas; Q5F2E7; -.
DR   ProteomicsDB; 287855; -. [Q5F2E7-1]
DR   ProteomicsDB; 287856; -. [Q5F2E7-2]
DR   Pumba; Q5F2E7; -.
DR   Antibodypedia; 2837; 119 antibodies from 23 providers.
DR   DNASU; 68564; -.
DR   Ensembl; ENSMUST00000100802.11; ENSMUSP00000098365.5; ENSMUSG00000037857.17. [Q5F2E7-1]
DR   Ensembl; ENSMUST00000181023.2; ENSMUSP00000137922.2; ENSMUSG00000037857.17. [Q5F2E7-2]
DR   GeneID; 68564; -.
DR   KEGG; mmu:68564; -.
DR   UCSC; uc007khd.2; mouse. [Q5F2E7-1]
DR   AGR; MGI:1915814; -.
DR   CTD; 57532; -.
DR   MGI; MGI:1915814; Nufip2.
DR   VEuPathDB; HostDB:ENSMUSG00000037857; -.
DR   eggNOG; ENOG502QPMD; Eukaryota.
DR   GeneTree; ENSGT00440000038328; -.
DR   HOGENOM; CLU_020745_0_0_1; -.
DR   InParanoid; Q5F2E7; -.
DR   OMA; NEQKGNR; -.
DR   OrthoDB; 5307266at2759; -.
DR   PhylomeDB; Q5F2E7; -.
DR   TreeFam; TF332832; -.
DR   BioGRID-ORCS; 68564; 7 hits in 77 CRISPR screens.
DR   ChiTaRS; Nufip2; mouse.
DR   PRO; PR:Q5F2E7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5F2E7; Protein.
DR   Bgee; ENSMUSG00000037857; Expressed in manus and 221 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC.
DR   GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR   GO; GO:0005840; C:ribosome; ISS:HGNC.
DR   GO; GO:0003723; F:RNA binding; ISS:HGNC.
DR   InterPro; IPR032747; NUFIP2.
DR   PANTHER; PTHR28333; NUCLEAR FRAGILE X MENTAL RETARDATION-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR28333:SF2; NUCLEAR FRAGILE X MENTAL RETARDATION-INTERACTING PROTEIN 2; 1.
DR   Pfam; PF15293; NUFIP2; 1.
DR   Genevisible; Q5F2E7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..692
FT                   /note="FMR1-interacting protein NUFIP2"
FT                   /id="PRO_0000245522"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..56
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         88
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         219
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         221
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         291
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         569
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         630
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        79
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        110
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        137
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        158
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        262
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        281
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   CROSSLNK        307
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z417"
FT   VAR_SEQ         676..692
FT                   /note="DPKRIITYNEAMDSPDQ -> VFCLCVYMYTYVHHVMSLHGRERTLDPLELA
FT                   LHWS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_019729"
FT   CONFLICT        52
FT                   /note="Missing (in Ref. 2; BAE42015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="Q -> R (in Ref. 2; BAE42015)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  75657 MW;  3E295AC111814564 CRC64;
     MEEKPGQPQP QHHHSHHHPH HHPQQQQQQQ SHHHHHYYFY NHSHNHHHHH HHQQPHQYLQ
     HGAEGSPKAQ PKPLKHEQKH TLQQHQETPK KKTGYGEING NAGEREISLK SLSSDEATNP
     ISRVLNGNQQ VVETSLKQTV KTSTFGKAGI KTKNFIQKNS MDKKNGKSYE NKSGETQAVD
     KTDTIAIPNG VITSSSGYIT NGYMSKGADN DGSGSESGYT TPKKRKARRN SAKGCENLNL
     VQDKIMQETS VPALKQGLET LKPDYSEQKG MRVDGSKPIW KYETGPGGTS RGKPAMGDVL
     RKSSDIKPGL SSKKFDDRPK GKHASAAASK EDSWTLFKPP PVFPVDNSSA KIVPKISYAS
     KVKENLNKTV QNSSVSPSSS SSSSSTGETQ TQSSSRLSQV PMSALKSVTS ASFSNGPVLA
     GTDGSVYPSG GQPLLTTAAN TLTPISTGTD SVLQDMSLAS AAVEQIKSSL FIYPSNMQTV
     LLSAQVDLPS QTDQQNLGDI FQNQWGLSFI NEPSAGPETV IGKSSDHKVM EVTFQGEYPA
     TLVSQGAEII PSGTEHPVFP KAYELEKRTS PQVLGHILKP GTTESGALSL DPSHIGDLQK
     ADTSSQGALV FLSKDYEIEN QNPLASPTNT LLGSAKEQRY QRGLERNDSW GSFDLRAAIV
     YHTKEMESIW NLQKQDPKRI ITYNEAMDSP DQ
//