TDIF1_HUMAN
ID TDIF1_HUMAN Reviewed; 329 AA.
AC Q9H147; B2RA18; Q96DE3; Q9BQP2; Q9H148;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Deoxynucleotidyltransferase terminal-interacting protein 1;
DE AltName: Full=Terminal deoxynucleotidyltransferase-interacting factor 1;
DE Short=TdIF1 {ECO:0000303|PubMed:11473582, ECO:0000303|PubMed:23874396};
DE Short=TdT-interacting factor 1 {ECO:0000303|PubMed:11473582};
GN Name=DNTTIP1; Synonyms=C20orf167, TDIF1;
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], FUNCTION, INTERACTION WITH DNTT, SUBUNIT,
RP SUBCELLULAR LOCATION, DNA-BINDING, AND DOMAIN.
RC TISSUE=Thymus;
RX PubMed=11473582; DOI=10.1046/j.1365-2443.2001.00449.x;
RA Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T.,
RA Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.;
RT "Terminal deoxynucleotidyltransferase directly interacts with a novel
RT nuclear protein that is homologous to p65.";
RL Genes Cells 6:641-652(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, 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 [7]
RP INTERACTION WITH TRERF1 AND DNTT, AND SUBCELLULAR LOCATION.
RX PubMed=16371131; DOI=10.1111/j.1365-2443.2005.00916.x;
RA Fujisaki S., Sato A., Toyomoto T., Hayano T., Sugai M., Kubota T.,
RA Koiwai O.;
RT "Direct binding of TReP-132 with TdT results in reduction of TdT
RT activity.";
RL Genes Cells 11:47-57(2006).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX, AND INTERACTION WITH ZNF541;
RP TRERF1; HDAC1; HDAC2 AND MIDEAS.
RX PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT dependent recruitment of a conserved histone deacetylase complex.";
RL PLoS Genet. 7:E1002065-E1002065(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=23874396; DOI=10.1371/journal.pone.0066710;
RA Kubota T., Koiwai O., Hori K., Watanabe N., Koiwai K.;
RT "TdIF1 recognizes a specific DNA sequence through its Helix-Turn-Helix and
RT AT-hook motifs to regulate gene transcription.";
RL PLoS ONE 8:E66710-E66710(2013).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-156, STRUCTURE BY NMR OF
RP 197-316, SUBUNIT, INTERACTION WITH MIDEAS AND HDAC1, IDENTIFICATION BY MASS
RP SPECTROMETRY, DOMAIN, DNA-BINDING, AND FUNCTION.
RX PubMed=25653165; DOI=10.1093/nar/gkv068;
RA Itoh T., Fairall L., Muskett F.W., Milano C.P., Watson P.J., Arnaudo N.,
RA Saleh A., Millard C.J., El-Mezgueldi M., Martino F., Schwabe J.W.;
RT "Structural and functional characterization of a cell cycle associated
RT HDAC1/2 complex reveals the structural basis for complex assembly and
RT nucleosome targeting.";
RL Nucleic Acids Res. 43:2033-2044(2015).
CC -!- FUNCTION: Increases DNTT terminal deoxynucleotidyltransferase activity
CC (in vitro) (PubMed:11473582). Also acts as a transcriptional regulator,
CC binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract.
CC Associates with RAB20 promoter and positively regulates its
CC transcription. Binds DNA and nucleosomes; may recruit HDAC1 complexes
CC to nucleosomes or naked DNA. {ECO:0000269|PubMed:11473582,
CC ECO:0000269|PubMed:23874396, ECO:0000305|PubMed:25653165}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:11473582, PubMed:25653165). A
CC minor proportion may form homotrimers (PubMed:11473582). Interacts with
CC ZNF541 (PubMed:21573134). Interacts with the terminal
CC deoxynucleotidyltransferase DNTT (PubMed:11473582, PubMed:16371131).
CC Interacts with TRERF1 (PubMed:16371131, PubMed:21573134). Identified in
CC a histone deacetylase complex that contains DNTTIP1, HDAC1 and MIDEAS;
CC this complex assembles into a tetramer that contains four copies of
CC each protein chain (PubMed:25653165). Component of a histone
CC deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2
CC (PubMed:21573134). {ECO:0000269|PubMed:11473582,
CC ECO:0000269|PubMed:16371131, ECO:0000269|PubMed:21573134,
CC ECO:0000269|PubMed:25653165}.
CC -!- INTERACTION:
CC Q9H147; P01023: A2M; NbExp=3; IntAct=EBI-2795449, EBI-640741;
CC Q9H147; Q92688: ANP32B; NbExp=3; IntAct=EBI-2795449, EBI-762428;
CC Q9H147; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2795449, EBI-10976677;
CC Q9H147; P50570-2: DNM2; NbExp=3; IntAct=EBI-2795449, EBI-10968534;
CC Q9H147; Q96JC9: EAF1; NbExp=3; IntAct=EBI-2795449, EBI-769261;
CC Q9H147; P22607: FGFR3; NbExp=3; IntAct=EBI-2795449, EBI-348399;
CC Q9H147; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-2795449, EBI-2549423;
CC Q9H147; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-2795449, EBI-10172004;
CC Q9H147; P42858: HTT; NbExp=15; IntAct=EBI-2795449, EBI-466029;
CC Q9H147; P43360: MAGEA6; NbExp=3; IntAct=EBI-2795449, EBI-1045155;
CC Q9H147; P55081: MFAP1; NbExp=3; IntAct=EBI-2795449, EBI-1048159;
CC Q9H147; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2795449, EBI-79165;
CC Q9H147; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2795449, EBI-5235340;
CC Q9H147; O14656-2: TOR1A; NbExp=3; IntAct=EBI-2795449, EBI-25847109;
CC Q9H147; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2795449, EBI-12806590;
CC Q9H147; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2795449, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11473582,
CC ECO:0000269|PubMed:16371131}.
CC -!- DOMAIN: The N-terminal domain mediates dimerization.
CC {ECO:0000269|PubMed:25653165}.
CC -!- DOMAIN: The C-terminal domain mediates interaction with DNA and
CC nucleosomes (PubMed:11473582, PubMed:25653165). It contains a HTH motif
CC that mediates recognition of the consensus sequence (PubMed:23874396).
CC {ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:23874396,
CC ECO:0000269|PubMed:25653165}.
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DR EMBL; AB035676; BAB62888.1; -; mRNA.
DR EMBL; AK314003; BAG36715.1; -; mRNA.
DR EMBL; AL050348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75812.1; -; Genomic_DNA.
DR EMBL; BC024290; AAH24290.1; -; mRNA.
DR EMBL; BC009535; AAH09535.1; -; mRNA.
DR CCDS; CCDS13369.1; -.
DR RefSeq; NP_443183.1; NM_052951.2.
DR PDB; 2MWI; NMR; -; A=197-316.
DR PDB; 4D6K; X-ray; 2.10 A; A/B/C/D/E/F=56-147.
DR PDB; 6Z2J; EM; 4.00 A; A/B=1-130.
DR PDB; 6Z2K; EM; 4.50 A; A/B/G/H=1-130.
DR PDBsum; 2MWI; -.
DR PDBsum; 4D6K; -.
DR PDBsum; 6Z2J; -.
DR PDBsum; 6Z2K; -.
DR AlphaFoldDB; Q9H147; -.
DR BMRB; Q9H147; -.
DR SMR; Q9H147; -.
DR BioGRID; 125472; 77.
DR CORUM; Q9H147; -.
DR IntAct; Q9H147; 65.
DR MINT; Q9H147; -.
DR STRING; 9606.ENSP00000361705; -.
DR iPTMnet; Q9H147; -.
DR PhosphoSitePlus; Q9H147; -.
DR BioMuta; DNTTIP1; -.
DR DMDM; 26400504; -.
DR EPD; Q9H147; -.
DR jPOST; Q9H147; -.
DR MassIVE; Q9H147; -.
DR MaxQB; Q9H147; -.
DR PaxDb; Q9H147; -.
DR PeptideAtlas; Q9H147; -.
DR PRIDE; Q9H147; -.
DR ProteomicsDB; 80354; -.
DR Antibodypedia; 12850; 264 antibodies from 23 providers.
DR DNASU; 116092; -.
DR Ensembl; ENST00000372622.8; ENSP00000361705.3; ENSG00000101457.13.
DR GeneID; 116092; -.
DR KEGG; hsa:116092; -.
DR MANE-Select; ENST00000372622.8; ENSP00000361705.3; NM_052951.3; NP_443183.1.
DR UCSC; uc002xpk.3; human.
DR CTD; 116092; -.
DR DisGeNET; 116092; -.
DR GeneCards; DNTTIP1; -.
DR HGNC; HGNC:16160; DNTTIP1.
DR HPA; ENSG00000101457; Low tissue specificity.
DR MIM; 611388; gene.
DR neXtProt; NX_Q9H147; -.
DR OpenTargets; ENSG00000101457; -.
DR PharmGKB; PA25709; -.
DR VEuPathDB; HostDB:ENSG00000101457; -.
DR eggNOG; KOG4801; Eukaryota.
DR GeneTree; ENSGT00510000047836; -.
DR InParanoid; Q9H147; -.
DR OMA; TENDHRA; -.
DR OrthoDB; 622558at2759; -.
DR PhylomeDB; Q9H147; -.
DR TreeFam; TF329275; -.
DR PathwayCommons; Q9H147; -.
DR SignaLink; Q9H147; -.
DR BioGRID-ORCS; 116092; 48 hits in 1097 CRISPR screens.
DR ChiTaRS; DNTTIP1; human.
DR GenomeRNAi; 116092; -.
DR Pharos; Q9H147; Tbio.
DR PRO; PR:Q9H147; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H147; protein.
DR Bgee; ENSG00000101457; Expressed in monocyte and 181 other tissues.
DR ExpressionAtlas; Q9H147; baseline and differential.
DR Genevisible; Q9H147; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR InterPro; IPR041384; DNTTIP1_dimer.
DR InterPro; IPR026064; TdIF1.
DR PANTHER; PTHR23399; PTHR23399; 1.
DR Pfam; PF18192; DNTTIP1_dimer; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..329
FT /note="Deoxynucleotidyltransferase terminal-interacting
FT protein 1"
FT /id="PRO_0000072473"
FT DNA_BIND 159..173
FT /note="A.T hook"
FT /evidence="ECO:0000305|PubMed:23874396"
FT DNA_BIND 216..237
FT /note="H-T-H motif"
FT /evidence="ECO:0000305|PubMed:23874396"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..147
FT /note="Important for dimerization"
FT /evidence="ECO:0000269|PubMed:25653165"
FT REGION 147..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..316
FT /note="Important for DNA and nucleosome binding"
FT /evidence="ECO:0000269|PubMed:25653165"
FT MOTIF 164..170
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 147..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 183
FT /note="A -> T (in dbSNP:rs408911)"
FT /id="VAR_014956"
FT HELIX 65..87
FT /evidence="ECO:0007829|PDB:4D6K"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4D6K"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:4D6K"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4D6K"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2MWI"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2MWI"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2MWI"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:2MWI"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:2MWI"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2MWI"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2MWI"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2MWI"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2MWI"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:2MWI"
FT TURN 281..285
FT /evidence="ECO:0007829|PDB:2MWI"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2MWI"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:2MWI"
SQ SEQUENCE 329 AA; 37013 MW; FB78297069CD960E CRC64;
MGATGDAEQP RGPSGAERGG LELGDAGAAG QLVLTNPWNI MIKHRQVQRR GRRSQMTTSF
TDPAISMDLL RAVLQPSINE EIQTVFNKYM KFFQKAALNV RDNVGEEVDA EQLIQEACRS
CLEQAKLLFS DGEKVIPRLT HELPGIKRGR QAEEECAHRG SPLPKKRKGR PPGHILSSDR
AAAGMVWKPK SCEPIRREGP KWDPARLNES TTFVLGSRAN KALGMGGTRG RIYIKHPHLF
KYAADPQDKH WLAEQHHMRA TGGKMAYLLI EEDIRDLAAS DDYRGCLDLK LEELKSFVLP
SWMVEKMRKY METLRTENEH RAVEAPPQT
