IMDH1_HUMAN
ID IMDH1_HUMAN Reviewed; 514 AA.
AC P20839; A4D0Z6; A4D0Z7; A6NDW5; A6NNI6; B3KNP7; B3KVM8; B4DE09; C9JV30;
AC J3KNX8; Q8N194; Q96NU2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Inosine-5'-monophosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156};
DE Short=IMP dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156};
DE Short=IMPD 1 {ECO:0000255|HAMAP-Rule:MF_03156};
DE Short=IMPDH 1 {ECO:0000255|HAMAP-Rule:MF_03156};
DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156};
DE AltName: Full=IMPDH-I;
GN Name=IMPDH1 {ECO:0000255|HAMAP-Rule:MF_03156}; Synonyms=IMPD1;
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).
RC TISSUE=Spleen;
RX PubMed=1969416; DOI=10.1016/s0021-9258(19)34120-1;
RA Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.;
RT "Two distinct cDNAs for human IMP dehydrogenase.";
RL J. Biol. Chem. 265:5292-5295(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Brain;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 3).
RC TISSUE=Blood;
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 PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=7903306; DOI=10.1016/s0021-9258(19)74247-1;
RA Carr S.F., Papp E., Wu J.C., Natsumeda Y.;
RT "Characterization of human type I and type II IMP dehydrogenases.";
RL J. Biol. Chem. 268:27286-27290(1993).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J.,
RA Stuve L.L.;
RT "PCR isolation and cloning of novel splice variant mRNAs from known drug
RT target genes.";
RL Genomics 83:566-571(2004).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7763314; DOI=10.1016/0006-2952(95)00026-v;
RA Hager P.W., Collart F.R., Huberman E., Mitchell B.S.;
RT "Recombinant human inosine monophosphate dehydrogenase type I and type II
RT proteins. Purification and characterization of inhibitor binding.";
RL Biochem. Pharmacol. 49:1323-1329(1995).
RN [10]
RP SUBCELLULAR LOCATION, AND NUCLEIC ACID-BINDING.
RX PubMed=14766016; DOI=10.1042/bj20031585;
RA McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M.,
RA Hedstrom L.;
RT "Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in
RT vivo.";
RL Biochem. J. 379:243-251(2004).
RN [11]
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
RA Risal D., Strickler M.D., Goldstein B.M.;
RT "Crystal structure of the human type I inosine monophosphate dehydrogenase
RT and implications for isoform specificity.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [14]
RP VARIANT RP10 PRO-224.
RX PubMed=11875049; DOI=10.1093/hmg/11.5.547;
RA Kennan A., Aherne A., Palfi A., Humphries M., McKee A., Stitt A.,
RA Simpson D.A., Demtroder K., Orntoft T., Ayuso C., Kenna P.F., Farrar G.J.,
RA Humphries P.;
RT "Identification of an IMPDH1 mutation in autosomal dominant retinitis
RT pigmentosa (RP10) revealed following comparative microarray analysis of
RT transcripts derived from retinas of wild-type and Rho(-/-) mice.";
RL Hum. Mol. Genet. 11:547-557(2002).
RN [15]
RP VARIANTS RP10 ASN-226 AND ILE-268.
RX PubMed=11875050; DOI=10.1093/hmg/11.5.559;
RA Bowne S.J., Sullivan L.S., Blanton S.H., Cepko C.L., Blackshaw S.,
RA Birch D.G., Hughbanks-Wheaton D., Heckenlively J.R., Daiger S.P.;
RT "Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause
RT the RP10 form of autosomal dominant retinitis pigmentosa.";
RL Hum. Mol. Genet. 11:559-568(2002).
RN [16]
RP VARIANTS RP10 MET-116; ASN-226; ILE-268 AND PRO-372, VARIANTS LCA11 TRP-105
RP AND LYS-198, VARIANTS THR-285 AND ASP-324, CHARACTERIZATION OF VARIANTS
RP RP10 MET-116 AND PRO-372, CHARACTERIZATION OF VARIANTS LCA11 TRP-105 AND
RP LYS-198, AND CHARACTERIZATION OF VARIANT ASP-324.
RX PubMed=16384941; DOI=10.1167/iovs.05-0868;
RA Bowne S.J., Sullivan L.S., Mortimer S.E., Hedstrom L., Zhu J.,
RA Spellicy C.J., Gire A.I., Hughbanks-Wheaton D., Birch D.G., Lewis R.A.,
RA Heckenlively J.R., Daiger S.P.;
RT "Spectrum and frequency of mutations in IMPDH1 associated with autosomal
RT dominant retinitis pigmentosa and Leber congenital amaurosis.";
RL Invest. Ophthalmol. Vis. Sci. 47:34-42(2006).
CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to
CC xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC step in the de novo synthesis of guanine nucleotides, and therefore
CC plays an important role in the regulation of cell growth. Could also
CC have a single-stranded nucleic acid-binding activity and could play a
CC role in RNA and/or DNA metabolism. It may also have a role in the
CC development of malignancy and the growth progression of some tumors.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03156};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03156};
CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC inhibitor that prevents formation of the closed enzyme conformation by
CC binding to the same site as the amobile flap. In contrast, mizoribine
CC monophosphate (MZP) is a competitive inhibitor that induces the closed
CC conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC bacterial IMPDH. Subject to product inhibition by XMP and NADH. Also
CC inhibited by ADP. {ECO:0000255|HAMAP-Rule:MF_03156,
CC ECO:0000269|PubMed:7903306}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:7763314,
CC ECO:0000269|PubMed:7903306};
CC KM=46 uM for NAD(+) {ECO:0000269|PubMed:7763314,
CC ECO:0000269|PubMed:7903306};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03156,
CC ECO:0000269|PubMed:7903306, ECO:0000269|Ref.13}.
CC -!- INTERACTION:
CC P20839-3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12188657, EBI-742054;
CC P20839-3; P20839-3: IMPDH1; NbExp=5; IntAct=EBI-12188657, EBI-12188657;
CC P20839-3; P12268: IMPDH2; NbExp=3; IntAct=EBI-12188657, EBI-353389;
CC P20839-3; O75928-2: PIAS2; NbExp=3; IntAct=EBI-12188657, EBI-348567;
CC P20839-3; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-12188657, EBI-948156;
CC P20839-3; P78317: RNF4; NbExp=3; IntAct=EBI-12188657, EBI-2340927;
CC P20839-3; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-12188657, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156,
CC ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03156,
CC ECO:0000269|PubMed:14766016}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=P20839-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20839-2; Sequence=VSP_002674;
CC Name=3;
CC IsoId=P20839-3; Sequence=VSP_014363;
CC Name=4;
CC IsoId=P20839-4; Sequence=VSP_043485;
CC Name=5;
CC IsoId=P20839-5; Sequence=VSP_046969;
CC Name=6;
CC IsoId=P20839-6; Sequence=VSP_046970;
CC Name=7;
CC IsoId=P20839-7; Sequence=VSP_046968;
CC -!- TISSUE SPECIFICITY: IMP type I is the main species in normal leukocytes
CC and type II predominates over type I in the tumor.
CC -!- INDUCTION: Constitutively expressed.
CC -!- DISEASE: Retinitis pigmentosa 10 (RP10) [MIM:180105]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:11875049,
CC ECO:0000269|PubMed:11875050, ECO:0000269|PubMed:16384941}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Leber congenital amaurosis 11 (LCA11) [MIM:613837]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:16384941}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Because IMPDH activity is tightly linked with cell
CC proliferation, it has been recognized as a target for cancer and viral
CC chemotherapy and as a target for immunosuppressive drugs. The
CC activities of the antitumor drug tiazofurin, the antiviral drug
CC ribavirin, and the immunosuppressive drugs mizoribine and mycophenolic
CC acid (MPA) are attributed to the inhibition of IMPDH. In addition,
CC bacterial and parasitic IMPDH's differ significantly from mammalian
CC enzymes, which makes it a suitable target for anti-infective drugs.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
CC Rule:MF_03156}.
CC -!- SEQUENCE CAUTION: [Isoform 5]:
CC Sequence=BAG53840.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the IMPDH1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/impdhmut.htm";
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DR EMBL; J05272; AAA36114.1; -; mRNA.
DR EMBL; AK054640; BAB70780.1; -; mRNA.
DR EMBL; AK054667; BAG51409.1; -; mRNA.
DR EMBL; AK122994; BAG53840.1; ALT_FRAME; mRNA.
DR EMBL; AK293413; BAG56920.1; -; mRNA.
DR EMBL; AC010655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24310.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24311.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83652.1; -; Genomic_DNA.
DR EMBL; BC033622; AAH33622.2; -; mRNA.
DR EMBL; CD014008; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS34748.1; -. [P20839-3]
DR CCDS; CCDS34749.1; -. [P20839-6]
DR CCDS; CCDS43643.1; -. [P20839-5]
DR CCDS; CCDS47699.1; -. [P20839-7]
DR CCDS; CCDS47700.1; -. [P20839-2]
DR CCDS; CCDS55161.1; -. [P20839-4]
DR PIR; A35566; A35566.
DR RefSeq; NP_000874.2; NM_000883.3. [P20839-6]
DR RefSeq; NP_001096075.1; NM_001102605.1. [P20839-5]
DR RefSeq; NP_001136045.1; NM_001142573.1. [P20839-1]
DR RefSeq; NP_001136046.1; NM_001142574.1. [P20839-4]
DR RefSeq; NP_001136047.1; NM_001142575.1. [P20839-2]
DR RefSeq; NP_001136048.1; NM_001142576.1. [P20839-7]
DR RefSeq; NP_001291450.1; NM_001304521.1.
DR RefSeq; NP_899066.1; NM_183243.2. [P20839-3]
DR RefSeq; XP_016867661.1; XM_017012172.1.
DR PDB; 1JCN; X-ray; 2.50 A; A/B=1-514.
DR PDB; 7RER; EM; 2.60 A; A/B/C/D/E/F/G/H=1-514.
DR PDB; 7RES; EM; 3.05 A; A/B/C/D/E/F/G/H=1-514.
DR PDB; 7RFE; EM; 2.60 A; A/B/C/D/E/F/G/H=11-514.
DR PDB; 7RFF; EM; 2.70 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RFG; EM; 2.60 A; A/B/C/D/E/F/G/H=1-514.
DR PDB; 7RFH; EM; 3.70 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RFI; EM; 2.60 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RGD; EM; 3.00 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RGI; EM; 3.60 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RGL; EM; 2.40 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RGM; EM; 2.80 A; A/B/C/D/E/F/G/H=1-509.
DR PDB; 7RGQ; EM; 3.90 A; A/B/C/D/E/F/G/H=1-509.
DR PDBsum; 1JCN; -.
DR PDBsum; 7RER; -.
DR PDBsum; 7RES; -.
DR PDBsum; 7RFE; -.
DR PDBsum; 7RFF; -.
DR PDBsum; 7RFG; -.
DR PDBsum; 7RFH; -.
DR PDBsum; 7RFI; -.
DR PDBsum; 7RGD; -.
DR PDBsum; 7RGI; -.
DR PDBsum; 7RGL; -.
DR PDBsum; 7RGM; -.
DR PDBsum; 7RGQ; -.
DR AlphaFoldDB; P20839; -.
DR SMR; P20839; -.
DR BioGRID; 109827; 137.
DR DIP; DIP-60163N; -.
DR IntAct; P20839; 67.
DR MINT; P20839; -.
DR STRING; 9606.ENSP00000345096; -.
DR BindingDB; P20839; -.
DR ChEMBL; CHEMBL1822; -.
DR DrugBank; DB03948; 6-Chloropurine Riboside, 5'-Monophosphate.
DR DrugBank; DB00993; Azathioprine.
DR DrugBank; DB01033; Mercaptopurine.
DR DrugBank; DB00688; Mycophenolate mofetil.
DR DrugBank; DB01024; Mycophenolic acid.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00811; Ribavirin.
DR DrugBank; DB06408; Taribavirin.
DR DrugBank; DB06103; VX-148.
DR DrugCentral; P20839; -.
DR GuidetoPHARMACOLOGY; 2624; -.
DR GlyGen; P20839; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P20839; -.
DR PhosphoSitePlus; P20839; -.
DR BioMuta; IMPDH1; -.
DR DMDM; 25014074; -.
DR EPD; P20839; -.
DR jPOST; P20839; -.
DR MassIVE; P20839; -.
DR MaxQB; P20839; -.
DR PaxDb; P20839; -.
DR PeptideAtlas; P20839; -.
DR PRIDE; P20839; -.
DR ProteomicsDB; 11817; -.
DR ProteomicsDB; 53811; -. [P20839-1]
DR ProteomicsDB; 53812; -. [P20839-2]
DR ProteomicsDB; 53813; -. [P20839-3]
DR ProteomicsDB; 53814; -. [P20839-4]
DR Antibodypedia; 17770; 284 antibodies from 33 providers.
DR DNASU; 3614; -.
DR Ensembl; ENST00000338791.11; ENSP00000345096.6; ENSG00000106348.18. [P20839-6]
DR Ensembl; ENST00000348127.10; ENSP00000265385.8; ENSG00000106348.18. [P20839-3]
DR Ensembl; ENST00000354269.9; ENSP00000346219.5; ENSG00000106348.18. [P20839-5]
DR Ensembl; ENST00000419067.6; ENSP00000399400.2; ENSG00000106348.18. [P20839-7]
DR Ensembl; ENST00000480861.5; ENSP00000420185.1; ENSG00000106348.18. [P20839-4]
DR Ensembl; ENST00000496200.5; ENSP00000420803.1; ENSG00000106348.18. [P20839-2]
DR GeneID; 3614; -.
DR KEGG; hsa:3614; -.
DR MANE-Select; ENST00000338791.11; ENSP00000345096.6; NM_000883.4; NP_000874.2. [P20839-6]
DR UCSC; uc003vmt.3; human. [P20839-1]
DR CTD; 3614; -.
DR DisGeNET; 3614; -.
DR GeneCards; IMPDH1; -.
DR GeneReviews; IMPDH1; -.
DR HGNC; HGNC:6052; IMPDH1.
DR HPA; ENSG00000106348; Tissue enhanced (retina).
DR MalaCards; IMPDH1; -.
DR MIM; 146690; gene.
DR MIM; 180105; phenotype.
DR MIM; 613837; phenotype.
DR neXtProt; NX_P20839; -.
DR OpenTargets; ENSG00000106348; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA29862; -.
DR VEuPathDB; HostDB:ENSG00000106348; -.
DR eggNOG; KOG2550; Eukaryota.
DR GeneTree; ENSGT00940000154156; -.
DR HOGENOM; CLU_022552_2_1_1; -.
DR OMA; MGYCGAK; -.
DR OrthoDB; 618077at2759; -.
DR PhylomeDB; P20839; -.
DR TreeFam; TF300378; -.
DR BioCyc; MetaCyc:HS02896-MON; -.
DR BRENDA; 1.1.1.205; 2681.
DR PathwayCommons; P20839; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SABIO-RK; P20839; -.
DR SignaLink; P20839; -.
DR SIGNOR; P20839; -.
DR UniPathway; UPA00601; UER00295.
DR BioGRID-ORCS; 3614; 37 hits in 1080 CRISPR screens.
DR ChiTaRS; IMPDH1; human.
DR EvolutionaryTrace; P20839; -.
DR GeneWiki; IMPDH1; -.
DR GenomeRNAi; 3614; -.
DR Pharos; P20839; Tclin.
DR PRO; PR:P20839; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P20839; protein.
DR Bgee; ENSG00000106348; Expressed in granulocyte and 171 other tissues.
DR ExpressionAtlas; P20839; baseline and differential.
DR Genevisible; P20839; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01964; IMPDH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR11911; PTHR11911; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; CBS domain; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA-binding; GMP biosynthesis;
KW Leber congenital amaurosis; Metal-binding; Methylation; NAD; Nucleus;
KW Oxidoreductase; Phosphoprotein; Potassium; Purine biosynthesis;
KW Reference proteome; Repeat; Retinitis pigmentosa; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156,
FT ECO:0000269|PubMed:7903306"
FT CHAIN 2..514
FT /note="Inosine-5'-monophosphate dehydrogenase 1"
FT /id="PRO_0000093670"
FT DOMAIN 114..173
FT /note="CBS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT DOMAIN 179..237
FT /note="CBS 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT ACT_SITE 331
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 324..326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 326
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 328
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 329
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT BINDING 331
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 364..366
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT BINDING 387..388
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT BINDING 411..415
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 441
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 500
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 501
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT BINDING 502
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P50096"
FT MOD_RES 355
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P50096"
FT VAR_SEQ 1..33
FT /note="MADYLISGGTGYVPEDGLTAQQLFASADGLTYN -> MEGPLTPPPLQGGGA
FT AAVPEPGARQHPGHETAAQRYSARLLQAGYEPESPRLDLATHPTTPRSELSSVVLLAGV
FT GVQMDRLRRAS (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_046968"
FT VAR_SEQ 1
FT /note="M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEP
FT ESM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014363"
FT VAR_SEQ 1
FT /note="M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEP
FT ESCFLLELSSVVLLAGVGVQMDRLRRASM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046969"
FT VAR_SEQ 1
FT /note="M -> MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEP
FT ESPRLDLATHPTTPRSELSSVVLLAGVGVQMDRLRRASM (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_046970"
FT VAR_SEQ 84..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_002674"
FT VAR_SEQ 104..108
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043485"
FT VARIANT 105
FT /note="R -> W (in LCA11; does not alter the enzymatic
FT affinity of the corresponding enzyme; alters the affinity
FT and/or the specificity of single-stranded nucleic acid)"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065616"
FT VARIANT 116
FT /note="T -> M (in RP10; does not alter the enzymatic
FT affinity of the corresponding enzyme; alters the affinity
FT and/or the specificity of single-stranded nucleic acid)"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065617"
FT VARIANT 198
FT /note="N -> K (in LCA11; does not alter the enzymatic
FT affinity of the corresponding enzyme; alters the affinity
FT and/or the specificity of single-stranded nucleic acid)"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065618"
FT VARIANT 224
FT /note="R -> P (in RP10)"
FT /evidence="ECO:0000269|PubMed:11875049"
FT /id="VAR_017031"
FT VARIANT 226
FT /note="D -> N (in RP10)"
FT /evidence="ECO:0000269|PubMed:11875050,
FT ECO:0000269|PubMed:16384941"
FT /id="VAR_017032"
FT VARIANT 268
FT /note="V -> I (in RP10)"
FT /evidence="ECO:0000269|PubMed:11875050,
FT ECO:0000269|PubMed:16384941"
FT /id="VAR_017033"
FT VARIANT 285
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065619"
FT VARIANT 324
FT /note="G -> D (does not alter the enzymatic affinity of the
FT corresponding enzyme; does not affect the affinity for
FT single-stranded nucleic acid)"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065620"
FT VARIANT 372
FT /note="H -> P (in RP10; alters the affinity and/or the
FT specificity of single-stranded nucleic acid)"
FT /evidence="ECO:0000269|PubMed:16384941"
FT /id="VAR_065621"
FT CONFLICT 29
FT /note="G -> D (in Ref. 1; AAA36114)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="K -> N (in Ref. 1; AAA36114)"
FT /evidence="ECO:0000305"
FT CONFLICT 273..274
FT /note="LD -> FH (in Ref. 1; AAA36114)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="A -> P (in Ref. 1; AAA36114)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> P (in Ref. 1; AAA36114)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1JCN"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1JCN"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7RGL"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7RER"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:7RFE"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7RES"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:7RFE"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1JCN"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:7RFE"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1JCN"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:7RFG"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:7RFG"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:7RFG"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7RFE"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7RES"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:1JCN"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:1JCN"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:7RFG"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7RER"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:7RGL"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:7RGL"
FT TURN 388..392
FT /evidence="ECO:0007829|PDB:1JCN"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 453..471
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7RGL"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:7RGL"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:7RGL"
SQ SEQUENCE 514 AA; 55406 MW; ABAC654A9091BE62 CRC64;
MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT
LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV
LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT
PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS
QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI
GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP
IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM
EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR
SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY
