INO1_HUMAN
ID INO1_HUMAN Reviewed; 558 AA.
AC Q9NPH2; B3KRT1; G5E9U0; Q6NXT5; Q7Z525; Q9BT65; Q9H2Y2; Q9NSU0; Q9NVW7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Inositol-3-phosphate synthase 1;
DE Short=IPS 1;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase;
DE Short=MI-1-P synthase;
DE Short=MIP synthase;
DE Short=hIPS;
DE AltName: Full=Myo-inositol 1-phosphate synthase A1;
DE Short=hINO1;
GN Name=ISYNA1; Synonyms=INO1;
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 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Hepatoma;
RX PubMed=12941308; DOI=10.1016/s0003-9861(03)00388-6;
RA Guan G., Dai P., Shechter I.;
RT "cDNA cloning and gene expression analysis of human myo-inositol 1-
RT phosphate synthase.";
RL Arch. Biochem. Biophys. 417:251-259(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=17121280; DOI=10.1007/0-387-27600-9_12;
RA Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F.,
RA Parthasarathy R.N.;
RT "Mammalian inositol 3-phosphate synthase: its role in the biosynthesis of
RT brain inositol and its clinical use as a psychoactive agent.";
RL Subcell. Biochem. 39:293-314(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou Y., Yu L., Zhao E.P., Hua Y.M., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to S.polyrrhiza D-myo-inositol-3-
RT phosphate synthase mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryo, and Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, 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 [9]
RP INDUCTION.
RX PubMed=15464731; DOI=10.1016/j.abb.2004.08.002;
RA Seelan R.S., Parthasarathy L.K., Parthasarathy R.N.;
RT "E2F1 regulation of the human myo-inositol 1-phosphate synthase (ISYNA1)
RT gene promoter.";
RL Arch. Biochem. Biophys. 431:95-106(2004).
RN [10]
RP FUNCTION, ENZYME ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15024000; DOI=10.1074/jbc.m312078200;
RA Ju S., Shaltiel G., Shamir A., Agam G., Greenberg M.L.;
RT "Human 1-D-myo-inositol-3-phosphate synthase is functional in yeast.";
RL J. Biol. Chem. 279:21759-21765(2004).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=17988368; DOI=10.1111/j.1399-5618.2007.00440.x;
RA Shamir A., Shaltiel G., Mark S., Bersudsky Y., Belmaker R.H., Agam G.;
RT "Human MIP synthase splice variants in bipolar disorder.";
RL Bipolar Disord. 9:766-771(2007).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=17901568;
RA Galit S., Shirley M., Ora K., Belmaker R.H., Galila A.;
RT "Effects of valproate derivatives on human brain myo-inositol-1-phosphate
RT (MIP) synthase activity and amphetamine-induced rearing.";
RL Pharmacol. Rep. 59:402-407(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-
CC phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC synthesis of all inositol-containing compounds.
CC {ECO:0000269|PubMed:15024000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate;
CC Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548;
CC EC=5.5.1.4; Evidence={ECO:0000269|PubMed:15024000};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:15024000};
CC -!- ACTIVITY REGULATION: Inhibited by mood-stabilizing drugs such as
CC valproate (VPA) and lithium. {ECO:0000269|PubMed:17901568,
CC ECO:0000269|PubMed:17988368}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 mM for 6-phosphate {ECO:0000269|PubMed:15024000};
CC KM=8 uM for NAD {ECO:0000269|PubMed:15024000};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15024000};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 1/2.
CC -!- INTERACTION:
CC Q9NPH2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-720563, EBI-3867333;
CC Q9NPH2; Q9NUX5: POT1; NbExp=2; IntAct=EBI-720563, EBI-752420;
CC Q9NPH2; Q9BUZ4: TRAF4; NbExp=6; IntAct=EBI-720563, EBI-3650647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NPH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPH2-2; Sequence=VSP_032324;
CC Name=3;
CC IsoId=Q9NPH2-3; Sequence=VSP_046065;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, ovary, heart, placenta
CC and pancreas. Weakly expressed in blood leukocyte, thymus, skeletal
CC muscle and colon. {ECO:0000269|PubMed:12941308}.
CC -!- INDUCTION: By glucose and lovastain. Up-regulation is prevented by
CC mevalonic acid, farnesol, and geranylgeraniol. Up-regulated by E2F1.
CC {ECO:0000269|PubMed:12941308, ECO:0000269|PubMed:15464731}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97151.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF207640; AAG35698.1; -; mRNA.
DR EMBL; AF220530; AAF26444.1; -; mRNA.
DR EMBL; AF220259; AAF26739.1; -; Genomic_DNA.
DR EMBL; AF220250; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220251; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220252; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220253; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220254; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220255; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220256; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220257; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF220258; AAF26739.1; JOINED; Genomic_DNA.
DR EMBL; AF086921; AAP97151.1; ALT_FRAME; mRNA.
DR EMBL; AK001325; BAA91626.1; -; mRNA.
DR EMBL; AK021526; BAB13837.1; -; mRNA.
DR EMBL; AK092179; BAG52493.1; -; mRNA.
DR EMBL; AL137749; CAB70904.1; -; mRNA.
DR EMBL; AC008397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84703.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84705.1; -; Genomic_DNA.
DR EMBL; BC004320; AAH04320.1; -; mRNA.
DR EMBL; BC018952; AAH18952.1; -; mRNA.
DR EMBL; BC066902; AAH66902.1; -; mRNA.
DR CCDS; CCDS12379.1; -. [Q9NPH2-1]
DR CCDS; CCDS54234.1; -. [Q9NPH2-3]
DR CCDS; CCDS62603.1; -. [Q9NPH2-2]
DR PIR; T46317; T46317.
DR RefSeq; NP_001164409.1; NM_001170938.1. [Q9NPH2-3]
DR RefSeq; NP_001240318.1; NM_001253389.1. [Q9NPH2-2]
DR RefSeq; NP_057452.1; NM_016368.4. [Q9NPH2-1]
DR AlphaFoldDB; Q9NPH2; -.
DR SMR; Q9NPH2; -.
DR BioGRID; 119562; 50.
DR IntAct; Q9NPH2; 25.
DR MINT; Q9NPH2; -.
DR STRING; 9606.ENSP00000337746; -.
DR DrugBank; DB01840; 2-Deoxy-D-Glucitol 6-(E)-Vinylhomophosphonate.
DR DrugBank; DB04516; 2-Deoxy-Glucitol-6-Phosphate.
DR DrugBank; DB09462; Glycerin.
DR GlyGen; Q9NPH2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPH2; -.
DR PhosphoSitePlus; Q9NPH2; -.
DR BioMuta; ISYNA1; -.
DR DMDM; 74734304; -.
DR REPRODUCTION-2DPAGE; IPI00549569; -.
DR CPTAC; CPTAC-227; -.
DR CPTAC; CPTAC-228; -.
DR EPD; Q9NPH2; -.
DR jPOST; Q9NPH2; -.
DR MassIVE; Q9NPH2; -.
DR MaxQB; Q9NPH2; -.
DR PaxDb; Q9NPH2; -.
DR PeptideAtlas; Q9NPH2; -.
DR PRIDE; Q9NPH2; -.
DR ProteomicsDB; 34039; -.
DR ProteomicsDB; 81997; -. [Q9NPH2-1]
DR ProteomicsDB; 81998; -. [Q9NPH2-2]
DR Antibodypedia; 28044; 94 antibodies from 23 providers.
DR DNASU; 51477; -.
DR Ensembl; ENST00000338128.13; ENSP00000337746.7; ENSG00000105655.19. [Q9NPH2-1]
DR Ensembl; ENST00000457269.8; ENSP00000415458.3; ENSG00000105655.19. [Q9NPH2-3]
DR Ensembl; ENST00000578963.5; ENSP00000475677.1; ENSG00000105655.19. [Q9NPH2-2]
DR GeneID; 51477; -.
DR KEGG; hsa:51477; -.
DR MANE-Select; ENST00000338128.13; ENSP00000337746.7; NM_016368.5; NP_057452.1.
DR UCSC; uc002nja.3; human. [Q9NPH2-1]
DR CTD; 51477; -.
DR DisGeNET; 51477; -.
DR GeneCards; ISYNA1; -.
DR HGNC; HGNC:29821; ISYNA1.
DR HPA; ENSG00000105655; Tissue enhanced (choroid plexus, testis).
DR MIM; 611670; gene.
DR neXtProt; NX_Q9NPH2; -.
DR OpenTargets; ENSG00000105655; -.
DR PharmGKB; PA164721116; -.
DR VEuPathDB; HostDB:ENSG00000105655; -.
DR eggNOG; KOG0693; Eukaryota.
DR GeneTree; ENSGT00390000018395; -.
DR HOGENOM; CLU_021486_2_1_1; -.
DR InParanoid; Q9NPH2; -.
DR OMA; EHDLFIQ; -.
DR OrthoDB; 451916at2759; -.
DR PhylomeDB; Q9NPH2; -.
DR TreeFam; TF300382; -.
DR BRENDA; 5.5.1.4; 2681.
DR PathwayCommons; Q9NPH2; -.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SignaLink; Q9NPH2; -.
DR SIGNOR; Q9NPH2; -.
DR UniPathway; UPA00823; UER00787.
DR BioGRID-ORCS; 51477; 53 hits in 1082 CRISPR screens.
DR ChiTaRS; ISYNA1; human.
DR GenomeRNAi; 51477; -.
DR Pharos; Q9NPH2; Tbio.
DR PRO; PR:Q9NPH2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NPH2; protein.
DR Bgee; ENSG00000105655; Expressed in right testis and 180 other tissues.
DR ExpressionAtlas; Q9NPH2; baseline and differential.
DR Genevisible; Q9NPH2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IMP:CACAO.
DR GO; GO:0006021; P:inositol biosynthetic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11510; PTHR11510; 1.
DR Pfam; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Inositol biosynthesis; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; NAD; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1..558
FT /note="Inositol-3-phosphate synthase 1"
FT /id="PRO_0000324628"
FT REGION 537..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032324"
FT VAR_SEQ 40..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046065"
FT CONFLICT 17
FT /note="G -> S (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="E -> K (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> T (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> Q (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Missing (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="K -> N (in Ref. 1; AAG35698)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> N (in Ref. 3; AAP97151)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="P -> Q (in Ref. 8; AAH66902)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="S -> G (in Ref. 8; AAH66902)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="H -> R (in Ref. 4; BAG52493)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="P -> R (in Ref. 8; AAH66902)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="S -> C (in Ref. 4; BAA91626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61068 MW; 3A1009D941A5F87D CRC64;
MEAAAQFFVE SPDVVYGPEA IEAQYEYRTT RVSREGGVLK VHPTSTRFTF RTARQVPRLG
VMLVGWGGNN GSTLTAAVLA NRLRLSWPTR SGRKEANYYG SLTQAGTVSL GLDAEGQEVF
VPFSAVLPMV APNDLVFDGW DISSLNLAEA MRRAKVLDWG LQEQLWPHME ALRPRPSVYI
PEFIAANQSA RADNLIPGSR AQQLEQIRRD IRDFRSSAGL DKVIVLWTAN TERFCEVIPG
LNDTAENLLR TIELGLEVSP STLFAVASIL EGCAFLNGSP QNTLVPGALE LAWQHRVFVG
GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG ENLSAPLQFR SKEVSKSNVV
DDMVQSNPVL YTPGEEPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
LLAAPIMLDL ALLTELCQRV SFCTDMDPEP QTFHPVLSLL SFLFKAPLVP PGSPVVNALF
RQRSCIENIL RACVGLPPQN HMLLEHKMER PGPSLKRVGP VAATYPMLNK KGPVPAATNG
CTGDANGHLQ EEPPMPTT
