ID   NGRN_HUMAN              Reviewed;         291 AA.
AC   Q9NPE2; B2R6M8; Q4V9L7; Q9HBL4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Neugrin;
DE   AltName: Full=Mesenchymal stem cell protein DSC92;
DE   AltName: Full=Neurite outgrowth-associated protein;
DE   AltName: Full=Spinal cord-derived protein FI58G;
DE   Flags: Precursor;
GN   Name=NGRN {ECO:0000303|PubMed:27667664, ECO:0000312|HGNC:HGNC:18077};
GN   Synonyms=FI58G; ORFNames=HT020;
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] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11118320; DOI=10.1006/bbrc.2000.3971;
RA   Ishigaki S., Niwa J., Yoshihara T., Mitsuma N., Doyu M., Sobue G.;
RT   "Two novel genes, human neugrin and mouse m-neugrin, are upregulated with
RT   neuronal differentiation in neuroblastoma cells.";
RL   Biochem. Biophys. Res. Commun. 279:526-533(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Mesenchymal stem cell;
RA   van den Bos C., Mbalaviele G., Thiede M.;
RT   "cDNA DSC92 expressed by osteogenic human mesenchymal stem cells.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG   The European IMAGE consortium;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Chondrosarcoma, Lung, Muscle, Placenta, and Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-291 (ISOFORM 2).
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 73-291 (ISOFORM 1).
RA   Hu X., Xu Y., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Neuroblastoma;
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RX   PubMed=27667664; DOI=10.1016/j.cmet.2016.08.017;
RA   Arroyo J.D., Jourdain A.A., Calvo S.E., Ballarano C.A., Doench J.G.,
RA   Root D.E., Mootha V.K.;
RT   "A Genome-wide CRISPR Death Screen Identifies Genes Essential for Oxidative
RT   Phosphorylation.";
RL   Cell Metab. 24:875-885(2016).
CC   -!- FUNCTION: Plays an essential role in mitochondrial ribosome biogenesis.
CC       As a component of a functional protein-RNA module, consisting of RCC1L,
CC       NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal
CC       RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for
CC       intra-mitochondrial translation of core subunits of the oxidative
CC       phosphorylation system. {ECO:0000269|PubMed:27667664}.
CC   -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L,
CC       NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. Interacts with
CC       16S mt-rRNA; this interaction is direct. {ECO:0000269|PubMed:27667664}.
CC   -!- INTERACTION:
CC       Q9NPE2; Q6ZYL4: GTF2H5; NbExp=3; IntAct=EBI-2683432, EBI-6380438;
CC       Q9NPE2; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-2683432, EBI-2510804;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118320}. Secreted
CC       {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:27667664}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NPE2-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NPE2-3; Sequence=VSP_039710, VSP_039711;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in heart, brain and
CC       skeletal muscle. In brain, mainly expressed in neurons rather than
CC       glial cells. {ECO:0000269|PubMed:11118320}.
CC   -!- INDUCTION: Highly up-regulated in neuroblastostoma cells by retinoic
CC       acid treatment inducing neurite outgrowth.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neugrin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF65447.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAG09725.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAG09725.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH01682.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAH07222.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAH09389.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAH17192.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=BAB21533.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=BAB21533.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAG35525.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=BAG35525.1; Type=Miscellaneous discrepancy; Note=N-terminus does not match isoform 2.; Evidence={ECO:0000305};
CC       Sequence=CAB96088.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=CAD39160.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; AB029315; BAB21533.1; ALT_SEQ; mRNA.
DR   EMBL; AF242770; AAF65447.1; ALT_SEQ; mRNA.
DR   EMBL; AL360142; CAB96088.1; ALT_SEQ; mRNA.
DR   EMBL; AL834503; CAD39160.1; ALT_SEQ; mRNA.
DR   EMBL; AC091167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001682; AAH01682.1; ALT_SEQ; mRNA.
DR   EMBL; BC007222; AAH07222.1; ALT_SEQ; mRNA.
DR   EMBL; BC009389; AAH09389.1; ALT_SEQ; mRNA.
DR   EMBL; BC017192; AAH17192.1; ALT_SEQ; mRNA.
DR   EMBL; BC096824; AAH96824.1; -; mRNA.
DR   EMBL; BG719592; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF225423; AAG09725.1; ALT_SEQ; mRNA.
DR   EMBL; AY049780; AAL15437.1; -; mRNA.
DR   EMBL; AK312641; BAG35525.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS32329.1; -. [Q9NPE2-2]
DR   PIR; JC7563; JC7563.
DR   RefSeq; NP_001028260.2; NM_001033088.1. [Q9NPE2-2]
DR   AlphaFoldDB; Q9NPE2; -.
DR   SMR; Q9NPE2; -.
DR   BioGRID; 119482; 245.
DR   IntAct; Q9NPE2; 36.
DR   MINT; Q9NPE2; -.
DR   STRING; 9606.ENSP00000368389; -.
DR   GlyCosmos; Q9NPE2; 3 sites, No reported glycans.
DR   GlyGen; Q9NPE2; 3 sites.
DR   iPTMnet; Q9NPE2; -.
DR   PhosphoSitePlus; Q9NPE2; -.
DR   BioMuta; NGRN; -.
DR   DMDM; 306526226; -.
DR   EPD; Q9NPE2; -.
DR   jPOST; Q9NPE2; -.
DR   MassIVE; Q9NPE2; -.
DR   MaxQB; Q9NPE2; -.
DR   PaxDb; 9606-ENSP00000368389; -.
DR   PeptideAtlas; Q9NPE2; -.
DR   ProteomicsDB; 81977; -. [Q9NPE2-2]
DR   ProteomicsDB; 81978; -. [Q9NPE2-3]
DR   Pumba; Q9NPE2; -.
DR   Antibodypedia; 28784; 152 antibodies from 25 providers.
DR   DNASU; 51335; -.
DR   Ensembl; ENST00000379095.5; ENSP00000368389.4; ENSG00000182768.9. [Q9NPE2-2]
DR   GeneID; 51335; -.
DR   KEGG; hsa:51335; -.
DR   MANE-Select; ENST00000379095.5; ENSP00000368389.4; NM_001033088.3; NP_001028260.2.
DR   UCSC; uc002bpf.2; human. [Q9NPE2-2]
DR   AGR; HGNC:18077; -.
DR   CTD; 51335; -.
DR   DisGeNET; 51335; -.
DR   GeneCards; NGRN; -.
DR   HGNC; HGNC:18077; NGRN.
DR   HPA; ENSG00000182768; Tissue enhanced (skeletal).
DR   MIM; 616718; gene.
DR   neXtProt; NX_Q9NPE2; -.
DR   OpenTargets; ENSG00000182768; -.
DR   PharmGKB; PA142671265; -.
DR   VEuPathDB; HostDB:ENSG00000182768; -.
DR   eggNOG; ENOG502S5A6; Eukaryota.
DR   GeneTree; ENSGT00390000014472; -.
DR   HOGENOM; CLU_076903_1_0_1; -.
DR   InParanoid; Q9NPE2; -.
DR   OMA; AMDQIRY; -.
DR   OrthoDB; 2971965at2759; -.
DR   PhylomeDB; Q9NPE2; -.
DR   TreeFam; TF324463; -.
DR   PathwayCommons; Q9NPE2; -.
DR   SignaLink; Q9NPE2; -.
DR   BioGRID-ORCS; 51335; 113 hits in 1154 CRISPR screens.
DR   ChiTaRS; NGRN; human.
DR   GenomeRNAi; 51335; -.
DR   Pharos; Q9NPE2; Tbio.
DR   PRO; PR:Q9NPE2; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NPE2; Protein.
DR   Bgee; ENSG00000182768; Expressed in dorsolateral prefrontal cortex and 101 other cell types or tissues.
DR   ExpressionAtlas; Q9NPE2; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR   GO; GO:0061668; P:mitochondrial ribosome assembly; IMP:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; NAS:UniProtKB.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR   InterPro; IPR010487; NGRN/Rrg9.
DR   PANTHER; PTHR13475; NEUGRIN; 1.
DR   PANTHER; PTHR13475:SF4; NEUGRIN; 1.
DR   Pfam; PF06413; Neugrin; 1.
DR   Genevisible; Q9NPE2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Differentiation; Glycoprotein;
KW   Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..291
FT                   /note="Neugrin"
FT                   /id="PRO_0000294483"
FT   REGION          26..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         55..64
FT                   /note="STLKRQKQAI -> RYRLLPGPSA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10931946,
FT                   ECO:0000303|PubMed:11118320, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_039710"
FT   VAR_SEQ         65..291
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10931946,
FT                   ECO:0000303|PubMed:11118320, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2,
FT                   ECO:0000303|Ref.3"
FT                   /id="VSP_039711"
FT   VARIANT         174
FT                   /note="L -> F (in dbSNP:rs11073922)"
FT                   /id="VAR_053905"
FT   VARIANT         267
FT                   /note="D -> G (in dbSNP:rs16944113)"
FT                   /id="VAR_053906"
FT   CONFLICT        28
FT                   /note="A -> C (in Ref. 2; BG719592)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="P -> R (in Ref. 7; AAG09725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  32408 MW;  F0480D6D94BE2ACE CRC64;
     MAVTLSLLLG GRVCAAVTRC GFATRGVAGP GPIGREPDPD SDWEPEEREL QEVESTLKRQ
     KQAIRFQKIR RQMEAPGAPP RTLTWEAMEQ IRYLHEEFPE SWSVPRLAEG FDVSTDVIRR
     VLKSKFLPTL EQKLKQDQKV LKKAGLAHSL QHLRGSGNTS KLLPAGHSVS GSLLMPGHEA
     SSKDPNHSTA LKVIESDTHR TNTPRRRKGR NKEIQDLEES FVPVAAPLGH PRELQKYSSD
     SESPRGTGSG ALPSGQKLEE LKAEEPDNFS SKVVQRGREF FDSNGNFLYR I
//