PDE12_HUMAN
ID PDE12_HUMAN Reviewed; 609 AA.
AC Q6L8Q7; B4DTU8; Q8IYU3; Q8NDU2; Q8TE78;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=2',5'-phosphodiesterase 12;
DE Short=2'-PDE;
DE Short=2-PDE;
DE EC=3.1.4.- {ECO:0000269|PubMed:26055709};
DE AltName: Full=Mitochondrial deadenylase;
DE EC=3.1.13.4 {ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976};
DE Flags: Precursor;
GN Name=PDE12;
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), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15231837; DOI=10.1074/jbc.m400089200;
RA Kubota K., Nakahara K., Ohtsuka T., Yoshida S., Kawaguchi J., Fujita Y.,
RA Ozeki Y., Hara A., Yoshimura C., Furukawa H., Haruyama H., Ichikawa K.,
RA Yamashita M., Matsuoka T., Iijima Y.;
RT "Identification of 2'-phosphodiesterase, which plays a role in the 2-5A
RT system regulated by interferon.";
RL J. Biol. Chem. 279:37832-37841(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-23.
RC TISSUE=Placenta;
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], AND VARIANT TRP-23.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-609 (ISOFORM 1).
RC TISSUE=Lymph node;
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21245038; DOI=10.1093/nar/gkq1282;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Durand F., Faou P.,
RA Vestergaard A.L., Talbo G.H., Hoogenraad N., Brodersen D.E., Justesen J.,
RA Martensen P.M.;
RT "Human 2'-phosphodiesterase localizes to the mitochondrial matrix with a
RT putative function in mitochondrial RNA turnover.";
RL Nucleic Acids Res. 39:3754-3770(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21666256; DOI=10.1093/nar/gkr470;
RA Rorbach J., Nicholls T.J., Minczuk M.;
RT "PDE12 removes mitochondrial RNA poly(A) tails and controls translation in
RT human mitochondria.";
RL Nucleic Acids Res. 39:7750-7763(2011).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22285541; DOI=10.1016/j.biochi.2012.01.012;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Vestergaard A.L., Justesen J.,
RA Martensen P.M.;
RT "Characterization of human phosphodiesterase 12 and identification of a
RT novel 2'-5' oligoadenylate nuclease - The ectonucleotide
RT pyrophosphatase/phosphodiesterase 1.";
RL Biochimie 94:1098-1107(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=30389976; DOI=10.1038/s41598-018-34615-0;
RA Estrella M.A., Du J., Korennykh A.;
RT "Crystal Structure of Human Nocturnin Catalytic Domain.";
RL Sci. Rep. 8:16294-16294(2018).
RN [15] {ECO:0007744|PDB:4Z0V, ECO:0007744|PDB:4Z2B}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 155-609 IN COMPLEX WITH
RP MAGNESIUM, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26055709; DOI=10.1074/jbc.m115.653113;
RA Wood E.R., Bledsoe R., Chai J., Daka P., Deng H., Ding Y.,
RA Harris-Gurley S., Kryn L.H., Nartey E., Nichols J., Nolte R.T., Prabhu N.,
RA Rise C., Sheahan T., Shotwell J.B., Smith D., Tai V., Taylor J.D.,
RA Tomberlin G., Wang L., Wisely B., You S., Xia B., Dickson H.;
RT "The Role of Phosphodiesterase 12 (PDE12) as a Negative Regulator of the
RT Innate Immune Response and the Discovery of Antiviral Inhibitors.";
RL J. Biol. Chem. 290:19681-19696(2015).
RN [16] {ECO:0007744|PDB:4ZKF}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 154-609 IN COMPLEX WITH
RP MAGNESIUM.
RA Kim S.Y., Kohno T., Mori T., Kitano K., Hakoshima T.;
RT "Crystal structure of human phosphodiesterase.";
RL Submitted (APR-2015) to the PDB data bank.
CC -!- FUNCTION: Enzyme that cleaves 2',5'-phosphodiester bond linking
CC adenosines of the 5'-triphosphorylated oligoadenylates,
CC triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A
CC system. Degrades triphosphorylated 2-5A to produce AMP and ATP
CC (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of
CC oligoadenylates (PubMed:21666256, PubMed:30389976, PubMed:26055709).
CC Plays a role as a negative regulator of the 2-5A system that is one of
CC the major pathways for antiviral and antitumor functions induced by
CC interferons (IFNs). Suppression of this enzyme increases cellular 2-5A
CC levels and decreases viral replication in cultured small-airway
CC epithelial cells and Hela cells (PubMed:26055709).
CC {ECO:0000269|PubMed:15231837, ECO:0000269|PubMed:21245038,
CC ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541,
CC ECO:0000269|PubMed:26055709, ECO:0000269|PubMed:30389976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256,
CC ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709,
CC ECO:0000269|PubMed:30389976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22285541, ECO:0000269|PubMed:26055709,
CC ECO:0000269|Ref.16};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for 2'-5' oligoadenylate exonuclease activity.
CC {ECO:0000269|PubMed:22285541};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256,
CC ECO:0000269|PubMed:22285541}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6L8Q7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6L8Q7-2; Sequence=VSP_032202, VSP_032203;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15231837}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; AB115695; BAD20938.1; -; mRNA.
DR EMBL; AK074423; BAB85079.1; -; mRNA.
DR EMBL; AK300374; BAG62110.1; -; mRNA.
DR EMBL; CH471055; EAW65342.1; -; Genomic_DNA.
DR EMBL; AL831824; CAD38538.1; -; mRNA.
DR CCDS; CCDS33772.1; -. [Q6L8Q7-1]
DR RefSeq; NP_808881.3; NM_177966.6. [Q6L8Q7-1]
DR PDB; 4Z0V; X-ray; 1.78 A; A=155-609.
DR PDB; 4Z2B; X-ray; 1.80 A; A=155-609.
DR PDB; 4ZKF; X-ray; 1.82 A; A=154-609.
DR PDBsum; 4Z0V; -.
DR PDBsum; 4Z2B; -.
DR PDBsum; 4ZKF; -.
DR AlphaFoldDB; Q6L8Q7; -.
DR SMR; Q6L8Q7; -.
DR BioGRID; 128397; 108.
DR IntAct; Q6L8Q7; 23.
DR MINT; Q6L8Q7; -.
DR STRING; 9606.ENSP00000309142; -.
DR BindingDB; Q6L8Q7; -.
DR ChEMBL; CHEMBL4523342; -.
DR iPTMnet; Q6L8Q7; -.
DR PhosphoSitePlus; Q6L8Q7; -.
DR BioMuta; PDE12; -.
DR DMDM; 172046137; -.
DR EPD; Q6L8Q7; -.
DR jPOST; Q6L8Q7; -.
DR MassIVE; Q6L8Q7; -.
DR MaxQB; Q6L8Q7; -.
DR PaxDb; Q6L8Q7; -.
DR PeptideAtlas; Q6L8Q7; -.
DR PRIDE; Q6L8Q7; -.
DR ProteomicsDB; 66555; -. [Q6L8Q7-1]
DR ProteomicsDB; 66556; -. [Q6L8Q7-2]
DR Antibodypedia; 46309; 125 antibodies from 22 providers.
DR DNASU; 201626; -.
DR Ensembl; ENST00000311180.9; ENSP00000309142.7; ENSG00000174840.9. [Q6L8Q7-1]
DR GeneID; 201626; -.
DR KEGG; hsa:201626; -.
DR MANE-Select; ENST00000311180.9; ENSP00000309142.7; NM_177966.7; NP_808881.3.
DR UCSC; uc003diw.5; human. [Q6L8Q7-1]
DR CTD; 201626; -.
DR DisGeNET; 201626; -.
DR GeneCards; PDE12; -.
DR HGNC; HGNC:25386; PDE12.
DR HPA; ENSG00000174840; Low tissue specificity.
DR MIM; 616519; gene.
DR neXtProt; NX_Q6L8Q7; -.
DR OpenTargets; ENSG00000174840; -.
DR PharmGKB; PA162399016; -.
DR VEuPathDB; HostDB:ENSG00000174840; -.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000157205; -.
DR HOGENOM; CLU_016428_7_2_1; -.
DR OMA; LFRWFRE; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; Q6L8Q7; -.
DR TreeFam; TF323175; -.
DR PathwayCommons; Q6L8Q7; -.
DR Reactome; R-HSA-8983711; OAS antiviral response.
DR SignaLink; Q6L8Q7; -.
DR BioGRID-ORCS; 201626; 152 hits in 1082 CRISPR screens.
DR ChiTaRS; PDE12; human.
DR GenomeRNAi; 201626; -.
DR Pharos; Q6L8Q7; Tchem.
DR PRO; PR:Q6L8Q7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6L8Q7; protein.
DR Bgee; ENSG00000174840; Expressed in mucosa of sigmoid colon and 196 other tissues.
DR ExpressionAtlas; Q6L8Q7; baseline and differential.
DR Genevisible; Q6L8Q7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IMP:UniProtKB.
DR GO; GO:0004527; F:exonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034611; F:oligoribonucleotidase activity; TAS:Reactome.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0071359; P:cellular response to dsRNA; IDA:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IMP:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; TAS:Reactome.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IMP:UniProtKB.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IMP:UniProtKB.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IMP:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Mitochondrion; mRNA processing; Nuclease; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..609
FT /note="2',5'-phosphodiesterase 12"
FT /id="PRO_0000324312"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26055709, ECO:0000269|Ref.16,
FT ECO:0007744|PDB:4Z0V, ECO:0007744|PDB:4ZKF"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:4ZKF"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.16, ECO:0007744|PDB:4ZKF"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 527..535
FT /note="EERCNMSLT -> GGFGGNFLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032202"
FT VAR_SEQ 536..609
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032203"
FT VARIANT 23
FT /note="R -> W (in dbSNP:rs2241988)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT /id="VAR_039698"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4Z2B"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4Z2B"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 370..387
FT /evidence="ECO:0007829|PDB:4Z0V"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 412..417
FT /evidence="ECO:0007829|PDB:4Z0V"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 434..444
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 464..483
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 504..511
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:4Z0V"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:4Z0V"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 588..592
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:4Z0V"
FT STRAND 602..608
FT /evidence="ECO:0007829|PDB:4Z0V"
SQ SEQUENCE 609 AA; 67352 MW; 1D1F3AB4795B52A4 CRC64;
MWRLPGARAA LRVIRTAVEK LSRAEAGSQT AAGAMERAVV RCVPSEPKLS LSFALADGSH
KNMQRDQSEP LGRVLSRIAT NALKGHAKAA AAKKSRKSRP NASGGAACSG PGPEPAVFCE
PVVKLYYREE AVAEDVLNVD AWQDGAVLQI GDVKYKVERN PPAFTELQLP RYIMAGFPVC
PKLSLEFGDP ASSLFRWYKE AKPGAAEPEV GVPSSLSPSS PSSSWTETDV EERVYTPSNA
DIGLRLKLHC TPGDGQRFGH SRELESVCVV EAGPGTCTFD HRHLYTKKVT EDALIRTVSY
NILADTYAQT EFSRTVLYPY CAPYALELDY RQNLIQKELT GYNADVICLQ EVDRAVFSDS
LVPALEAFGL EGVFRIKQHE GLATFYRKSK FSLLSQHDIS FYEALESDPL HKELLEKLVL
YPSAQEKVLQ RSSVLQVSVL QSTKDSSKRI CVANTHLYWH PKGGYIRLIQ MAVALAHIRH
VSCDLYPGIP VIFCGDFNST PSTGMYHFVI NGSIPEDHED WASNGEEERC NMSLTHFFKL
KSACGEPAYT NYVGGFHGCL DYIFIDLNAL EVEQVIPLPS HEEVTTHQAL PSVSHPSDHI
ALVCDLKWK
