NUDT9_HUMAN
ID NUDT9_HUMAN Reviewed; 350 AA.
AC Q9BW91; Q8NBN1; Q8NCB9; Q8NG25;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=ADP-ribose pyrophosphatase, mitochondrial;
DE EC=3.6.1.13 {ECO:0000269|PubMed:11385575};
DE AltName: Full=ADP-ribose diphosphatase;
DE AltName: Full=ADP-ribose phosphohydrolase;
DE AltName: Full=Adenosine diphosphoribose pyrophosphatase;
DE Short=ADPR-PPase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 9;
DE Short=Nudix motif 9;
DE Flags: Precursor;
GN Name=NUDT9; Synonyms=NUDT10; ORFNames=PSEC0099, UNQ3012/PRO9771;
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), CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Spleen;
RX PubMed=11385575; DOI=10.1038/35079100;
RA Perraud A.-L., Fleig A., Dunn C.A., Bagley L.A., Launay P., Schmitz C.,
RA Stokes A.J., Zhu Q., Bessman M.J., Penner R., Kinet J.-P.,
RA Scharenberg A.M.;
RT "ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by
RT Nudix motif homology.";
RL Nature 411:595-599(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), COFACTOR, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC TISSUE=Fetal brain;
RX PubMed=11825615; DOI=10.1016/s0167-4838(01)00296-5;
RA Lin S., Gasmi L., Xie Y., Ying K., Gu S., Wang Z., Jin H., Chao Y., Wu C.,
RA Zhou Z., Tang R., Mao Y., McLennan A.G.;
RT "Cloning, expression and characterisation of a human Nudix hydrolase
RT specific for adenosine 5'-diphosphoribose (ADP-ribose).";
RL Biochim. Biophys. Acta 1594:127-135(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=12427752; DOI=10.1074/jbc.m205601200;
RA Perraud A.-L., Shen B., Dunn C.A., Rippe K., Smith M.K., Bessman M.J.,
RA Stoddard B.L., Scharenberg A.M.;
RT "NUDT9, a member of the Nudix hydrolase family, is an evolutionarily
RT conserved mitochondrial ADP-ribose pyrophosphatase.";
RL J. Biol. Chem. 278:1794-1801(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Lin S., Ying K.;
RT "NUDT10, a new member of human nudix hydrolase family.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 INTERACTION WITH GLOD4.
RX PubMed=12897971;
RA Zhang H.-T., Yan Z.-Q., Hu X.-B., Yang S.-L., Gong Y.;
RT "Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9 detected via
RT yeast two-hybrid method.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:747-751(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP 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-121, 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 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 59-350.
RX PubMed=12948489; DOI=10.1016/s0022-2836(03)00954-9;
RA Shen B.W., Perraud A.-L., Scharenberg A., Stoddard B.L.;
RT "The crystal structure and mutational analysis of human NUDT9.";
RL J. Mol. Biol. 332:385-398(2003).
CC -!- FUNCTION: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.
CC {ECO:0000269|PubMed:11385575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13; Evidence={ECO:0000269|PubMed:11385575};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for ADP-ribose {ECO:0000269|PubMed:11385575};
CC Vmax=11.8 umol/min/mg enzyme toward ADP-ribose
CC {ECO:0000269|PubMed:11385575};
CC -!- SUBUNIT: Monomer. Interacts with GLOD4. {ECO:0000269|PubMed:12427752,
CC ECO:0000269|PubMed:12897971}.
CC -!- INTERACTION:
CC Q9BW91; Q96AL5: PBX3; NbExp=3; IntAct=EBI-2682941, EBI-741171;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NUDT9a;
CC IsoId=Q9BW91-1; Sequence=Displayed;
CC Name=2; Synonyms=NUDT9b;
CC IsoId=Q9BW91-2; Sequence=VSP_010552;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed but isoform 1 is the most
CC predominant isoform. {ECO:0000269|PubMed:12427752}.
CC -!- INDUCTION: [Isoform 1]: Inhibited by fluoride and N-acetyl-p-
CC benzoquinoneimine. {ECO:0000269|PubMed:11825615}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC {ECO:0000305}.
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DR EMBL; AY026252; AAK07671.1; -; mRNA.
DR EMBL; AY359123; AAQ89480.1; -; mRNA.
DR EMBL; AF273028; AAM46068.1; -; mRNA.
DR EMBL; AK074845; BAC11239.1; -; mRNA.
DR EMBL; AK075408; BAC11601.1; -; mRNA.
DR EMBL; BC000542; AAH00542.1; -; mRNA.
DR CCDS; CCDS3620.1; -. [Q9BW91-1]
DR CCDS; CCDS3621.1; -. [Q9BW91-2]
DR RefSeq; NP_001234940.1; NM_001248011.1.
DR RefSeq; NP_076952.1; NM_024047.4. [Q9BW91-1]
DR RefSeq; NP_932155.1; NM_198038.2. [Q9BW91-2]
DR RefSeq; XP_011530334.1; XM_011532032.2. [Q9BW91-2]
DR PDB; 1Q33; X-ray; 1.81 A; A=59-350.
DR PDB; 1QVJ; X-ray; 1.91 A; A=59-350.
DR PDBsum; 1Q33; -.
DR PDBsum; 1QVJ; -.
DR AlphaFoldDB; Q9BW91; -.
DR SMR; Q9BW91; -.
DR BioGRID; 119744; 34.
DR IntAct; Q9BW91; 9.
DR STRING; 9606.ENSP00000303575; -.
DR BindingDB; Q9BW91; -.
DR ChEMBL; CHEMBL4105984; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB04352; beta-D-Ribose-5-phosphate.
DR iPTMnet; Q9BW91; -.
DR PhosphoSitePlus; Q9BW91; -.
DR BioMuta; NUDT9; -.
DR DMDM; 20455184; -.
DR EPD; Q9BW91; -.
DR jPOST; Q9BW91; -.
DR MassIVE; Q9BW91; -.
DR MaxQB; Q9BW91; -.
DR PaxDb; Q9BW91; -.
DR PeptideAtlas; Q9BW91; -.
DR PRIDE; Q9BW91; -.
DR ProteomicsDB; 79264; -. [Q9BW91-1]
DR ProteomicsDB; 79265; -. [Q9BW91-2]
DR Antibodypedia; 14458; 268 antibodies from 26 providers.
DR DNASU; 53343; -.
DR Ensembl; ENST00000302174.9; ENSP00000303575.4; ENSG00000170502.13. [Q9BW91-1]
DR Ensembl; ENST00000473942.5; ENSP00000421811.1; ENSG00000170502.13. [Q9BW91-2]
DR GeneID; 53343; -.
DR KEGG; hsa:53343; -.
DR MANE-Select; ENST00000302174.9; ENSP00000303575.4; NM_024047.5; NP_076952.1.
DR UCSC; uc003hqq.4; human. [Q9BW91-1]
DR CTD; 53343; -.
DR DisGeNET; 53343; -.
DR GeneCards; NUDT9; -.
DR HGNC; HGNC:8056; NUDT9.
DR HPA; ENSG00000170502; Low tissue specificity.
DR MIM; 606022; gene.
DR neXtProt; NX_Q9BW91; -.
DR OpenTargets; ENSG00000170502; -.
DR PharmGKB; PA31842; -.
DR VEuPathDB; HostDB:ENSG00000170502; -.
DR eggNOG; KOG4195; Eukaryota.
DR GeneTree; ENSGT00390000017405; -.
DR HOGENOM; CLU_067226_0_0_1; -.
DR InParanoid; Q9BW91; -.
DR OMA; PQWNQLD; -.
DR PhylomeDB; Q9BW91; -.
DR TreeFam; TF106351; -.
DR PathwayCommons; Q9BW91; -.
DR Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins. [Q9BW91-1]
DR SignaLink; Q9BW91; -.
DR BioGRID-ORCS; 53343; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; NUDT9; human.
DR EvolutionaryTrace; Q9BW91; -.
DR GeneWiki; NUDT9; -.
DR GenomeRNAi; 53343; -.
DR Pharos; Q9BW91; Tbio.
DR PRO; PR:Q9BW91; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BW91; protein.
DR Bgee; ENSG00000170502; Expressed in islet of Langerhans and 201 other tissues.
DR ExpressionAtlas; Q9BW91; baseline and differential.
DR Genevisible; Q9BW91; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; EXP:Reactome.
DR GO; GO:0019144; F:ADP-sugar diphosphatase activity; NAS:UniProtKB.
DR GO; GO:0046032; P:ADP catabolic process; IEA:Ensembl.
DR GO; GO:0046709; P:IDP catabolic process; IEA:Ensembl.
DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039989; NUDT9.
DR PANTHER; PTHR13030; PTHR13030; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..350
FT /note="ADP-ribose pyrophosphatase, mitochondrial"
FT /id="PRO_0000019950"
FT DOMAIN 178..334
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 53..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..237
FT /note="Nudix box"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11825615,
FT ECO:0000303|PubMed:12427752, ECO:0000303|PubMed:14702039"
FT /id="VSP_010552"
FT CONFLICT 118
FT /note="S -> G (in Ref. 4; AAM46068)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="E -> V (in Ref. 7; BAC11601)"
FT /evidence="ECO:0000305"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 163..178
FT /evidence="ECO:0007829|PDB:1Q33"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1Q33"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:1Q33"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 276..292
FT /evidence="ECO:0007829|PDB:1Q33"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:1Q33"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:1Q33"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1Q33"
SQ SEQUENCE 350 AA; 39125 MW; 2EA5B24B88FB3420 CRC64;
MAGRLLGKAL AAVSLSLALA SVTIRSSRCR GIQAFRNSFS SSWFHLNTNV MSGSNGSKEN
SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYKPVEYT AVSVLAGPRW ADPQISESNF
SPKFNEKDGH VERKSKNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR
DSSGNKIMHP VSGKHILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ
KTSAEKREIE EKLHKLFSQD HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGEIMDNLML
EAGDDAGKVK WVDINDKLKL YASHSQFIKL VAEKRDAHWS EDSEADCHAL
