NOB1_HUMAN
ID NOB1_HUMAN Reviewed; 412 AA.
AC Q9ULX3; Q7L6B7; Q7M4M4; Q7Z4B5; Q9NWB0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=RNA-binding protein NOB1;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
DE AltName: Full=Phosphorylation regulatory protein HP-10;
DE AltName: Full=Protein ART-4;
GN Name=NOB1; Synonyms=ART4, NOB1P, PSMD8BP1; ORFNames=MSTP158;
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].
RA Kawano K.;
RT "Adenocarcinoma antigen recognized by T lymphocytes-4 (ART-4).";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=16172919; DOI=10.1007/s11033-005-3141-7;
RA Zhang Y., Ni J., Zhou G., Yuan J., Ren W., Shan Y., Tang W., Yu L.,
RA Zhao S.;
RT "Cloning, expression and characterization of the human NOB1 gene.";
RL Mol. Biol. Rep. 32:185-189(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Placenta;
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 [5]
RP PROTEIN SEQUENCE OF 2-25; 32-38; 46-54; 65-71; 162-178 AND 324-330,
RP CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-412.
RC TISSUE=Aorta;
RA Liu B., Qin B.M., Sheng H., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q.,
RA Song L., Liu B.H., Lu H., Hui R.T.;
RT "Homo sapiens normal aorta mRNA MST158, complete cds.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 14-412, TISSUE SPECIFICITY, AND
RP VARIANT GLN-231.
RC TISSUE=Placenta;
RX PubMed=1791827; DOI=10.1007/bf00225511;
RA Daniele A., Altruda F., Ferrone M., Silengo L., Chiarantini L., Bianchi M.,
RA Stocchi V., Magnani M.;
RT "Cloning and expression of a new human polypeptide which regulates protein
RT phosphorylation in Escherichia coli.";
RL Mol. Cell. Biochem. 107:87-94(1991).
RN [8]
RP INTERACTION WITH UPF2.
RX PubMed=15231747; DOI=10.1101/gr.2122004;
RA Lehner B., Sanderson C.M.;
RT "A protein interaction framework for human mRNA degradation.";
RL Genome Res. 14:1315-1323(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-352, AND
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-201, AND
RP IDENTIFICATION BY 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-201; SER-325 AND
RP SER-352, AND IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) IN COMPLEX WITH ZINC
RP IONS, AND SUBUNIT.
RX PubMed=29875412; DOI=10.1038/s41586-018-0193-0;
RA Ameismeier M., Cheng J., Berninghausen O., Beckmann R.;
RT "Visualizing late states of human 40S ribosomal subunit maturation.";
RL Nature 558:249-253(2018).
CC -!- FUNCTION: May play a role in mRNA degradation (Probable). Endonuclease
CC required for processing of 20S pre-rRNA precursor and biogenesis of 40S
CC ribosomal subunits (By similarity). {ECO:0000250|UniProtKB:Q9FLL1,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts with UPF2 (Probable). Component of the small
CC ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex)
CC (PubMed:15231747). {ECO:0000269|PubMed:15231747,
CC ECO:0000305|PubMed:15231747}.
CC -!- INTERACTION:
CC Q9ULX3; Q9NRX1: PNO1; NbExp=4; IntAct=EBI-373285, EBI-712787;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16172919}.
CC -!- TISSUE SPECIFICITY: Detected in liver, lung, placenta, endothelial
CC cells and spleen. {ECO:0000269|PubMed:16172919,
CC ECO:0000269|PubMed:1791827}.
CC -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13705.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91473.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB026125; BAA86961.1; -; mRNA.
DR EMBL; AY487344; AAR85357.1; -; mRNA.
DR EMBL; AK001028; BAA91473.1; ALT_FRAME; mRNA.
DR EMBL; BC000050; AAH00050.2; -; mRNA.
DR EMBL; BC064630; AAH64630.1; -; mRNA.
DR EMBL; AF190161; AAQ13705.1; ALT_FRAME; mRNA.
DR CCDS; CCDS10884.1; -.
DR PIR; A61382; A61382.
DR RefSeq; NP_054781.1; NM_014062.2.
DR PDB; 6G18; EM; 3.60 A; y=1-412.
DR PDB; 6G4S; EM; 4.00 A; y=1-412.
DR PDB; 6G51; EM; 4.10 A; y=1-412.
DR PDB; 6G53; EM; 4.50 A; y=1-412.
DR PDB; 6G5I; EM; 3.50 A; y=1-412.
DR PDB; 6ZUO; EM; 3.10 A; y=1-412.
DR PDB; 6ZXD; EM; 3.20 A; y=1-412.
DR PDB; 6ZXE; EM; 3.00 A; y=1-412.
DR PDB; 6ZXF; EM; 3.70 A; y=1-412.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR AlphaFoldDB; Q9ULX3; -.
DR SMR; Q9ULX3; -.
DR BioGRID; 118808; 80.
DR IntAct; Q9ULX3; 28.
DR MINT; Q9ULX3; -.
DR STRING; 9606.ENSP00000268802; -.
DR iPTMnet; Q9ULX3; -.
DR PhosphoSitePlus; Q9ULX3; -.
DR SwissPalm; Q9ULX3; -.
DR BioMuta; NOB1; -.
DR DMDM; 74753398; -.
DR EPD; Q9ULX3; -.
DR jPOST; Q9ULX3; -.
DR MassIVE; Q9ULX3; -.
DR MaxQB; Q9ULX3; -.
DR PaxDb; Q9ULX3; -.
DR PeptideAtlas; Q9ULX3; -.
DR PRIDE; Q9ULX3; -.
DR ProteomicsDB; 85145; -.
DR Antibodypedia; 29888; 264 antibodies from 24 providers.
DR DNASU; 28987; -.
DR Ensembl; ENST00000268802.10; ENSP00000268802.5; ENSG00000141101.13.
DR GeneID; 28987; -.
DR KEGG; hsa:28987; -.
DR MANE-Select; ENST00000268802.10; ENSP00000268802.5; NM_014062.3; NP_054781.1.
DR UCSC; uc002exs.5; human.
DR CTD; 28987; -.
DR DisGeNET; 28987; -.
DR GeneCards; NOB1; -.
DR HGNC; HGNC:29540; NOB1.
DR HPA; ENSG00000141101; Low tissue specificity.
DR MIM; 613586; gene.
DR neXtProt; NX_Q9ULX3; -.
DR OpenTargets; ENSG00000141101; -.
DR PharmGKB; PA143485585; -.
DR VEuPathDB; HostDB:ENSG00000141101; -.
DR eggNOG; KOG2463; Eukaryota.
DR GeneTree; ENSGT00390000015857; -.
DR HOGENOM; CLU_024666_0_0_1; -.
DR InParanoid; Q9ULX3; -.
DR OMA; GYELECE; -.
DR OrthoDB; 765237at2759; -.
DR PhylomeDB; Q9ULX3; -.
DR TreeFam; TF105838; -.
DR PathwayCommons; Q9ULX3; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9ULX3; -.
DR BioGRID-ORCS; 28987; 677 hits in 1084 CRISPR screens.
DR GeneWiki; NOB1; -.
DR GenomeRNAi; 28987; -.
DR Pharos; Q9ULX3; Tbio.
DR PRO; PR:Q9ULX3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9ULX3; protein.
DR Bgee; ENSG00000141101; Expressed in body of pancreas and 103 other tissues.
DR ExpressionAtlas; Q9ULX3; baseline and differential.
DR Genevisible; Q9ULX3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; TAS:Reactome.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR Gene3D; 6.20.210.10; -; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR017117; Nob1_euk.
DR InterPro; IPR036283; NOB1_Zf-like_sf.
DR InterPro; IPR014881; NOB1_Zn-bd.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR InterPro; IPR033461; WRNPLPNID.
DR PANTHER; PTHR12814; PTHR12814; 1.
DR Pfam; PF08772; NOB1_Zn_bind; 1.
DR Pfam; PF17146; PIN_6; 1.
DR Pfam; PF15017; WRNPLPNID; 1.
DR PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF144206; SSF144206; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..412
FT /note="RNA-binding protein NOB1"
FT /id="PRO_0000233265"
FT DOMAIN 5..108
FT /note="PINc"
FT /evidence="ECO:0000255"
FT ZN_FING 260..332
FT /note="NOB1"
FT /evidence="ECO:0000255"
FT REGION 180..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29875412,
FT ECO:0007744|PDB:6G18, ECO:0007744|PDB:6G5I"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29875412,
FT ECO:0007744|PDB:6G18, ECO:0007744|PDB:6G5I"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29875412,
FT ECO:0007744|PDB:6G18, ECO:0007744|PDB:6G5I"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:29875412,
FT ECO:0007744|PDB:6G18, ECO:0007744|PDB:6G5I"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 231
FT /note="R -> Q (in dbSNP:rs3811348)"
FT /evidence="ECO:0000269|PubMed:1791827"
FT /id="VAR_050287"
FT VARIANT 366
FT /note="Y -> F (in dbSNP:rs1075935)"
FT /id="VAR_050288"
FT CONFLICT 408
FT /note="F -> L (in Ref. 6; AAQ13705)"
FT /evidence="ECO:0000305"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6ZUO"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6ZUO"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6ZUO"
FT HELIX 81..97
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:6ZUO"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 211..216
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6ZXD"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6ZUO"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6ZUO"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6ZUO"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6ZXD"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:6ZXD"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6ZUO"
SQ SEQUENCE 412 AA; 46675 MW; 369680A6DCFC7CB0 CRC64;
MAPVEHVVAD AGAFLRHAAL QDIGKNIYTI REVVTEIRDK ATRRRLAVLP YELRFKEPLP
EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKQEPQKV KVSSSIQHPE
TPLHISGFHL PYKPKPPQET EKGHSACEPE NLEFSSFMFW RNPLPNIDHE LQELLIDRGE
DVPSEEEEEE ENGFEDRKDD SDDDGGGWIT PSNIKQIQQE LEQCDVPEDV RVGCLTTDFA
MQNVLLQMGL HVLAVNGMLI REARSYILRC HGCFKTTSDM SRVFCSHCGN KTLKKVSVTV
SDDGTLHMHF SRNPKVLNPR GLRYSLPTPK GGKYAINPHL TEDQRFPQLR LSQKARQKTN
VFAPDYIAGV SPFVENDISS RSATLQVRDS TLGAGRRRLN PNASRKKFVK KR
