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Database: UniProt
Entry: Q8IWU9
LinkDB: Q8IWU9
Original site: Q8IWU9 
ID   TPH2_HUMAN              Reviewed;         490 AA.
AC   Q8IWU9; A6NGA4; Q14CB0;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-SEP-2021, entry version 163.
DE   RecName: Full=Tryptophan 5-hydroxylase 2;
DE            EC=1.14.16.4;
DE   AltName: Full=Neuronal tryptophan hydroxylase;
DE   AltName: Full=Tryptophan 5-monooxygenase 2;
GN   Name=TPH2; Synonyms=NTPH;
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 A).
RX   PubMed=12511643; DOI=10.1126/science.1078197;
RA   Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M., Fink H.,
RA   Bader M.;
RT   "Synthesis of serotonin by a second tryptophan hydroxylase isoform.";
RL   Science 299:76-76(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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   [4]
RP   BIOPHYSICOCHEMICAL PROPERTIES, VARIANT SER-206, AND CHARACTERIZATION OF
RP   VARIANTS SER-206 AND HIS-441.
RX   PubMed=17905754; DOI=10.1093/hmg/ddm286;
RA   Cichon S., Winge I., Mattheisen M., Georgi A., Karpushova A.,
RA   Freudenberg J., Freudenberg-Hua Y., Babadjanova G., Van Den Bogaert A.,
RA   Abramova L.I., Kapiletti S., Knappskog P.M., McKinney J., Maier W.,
RA   Jamra R.A., Schulze T.G., Schumacher J., Propping P., Rietschel M.,
RA   Haavik J., Noethen M.M.;
RT   "Brain-specific tryptophan hydroxylase 2 (TPH2): a functional Pro206Ser
RT   substitution and variation in the 5'-region are associated with bipolar
RT   affective disorder.";
RL   Hum. Mol. Genet. 17:87-97(2008).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS A AND B), AND RNA EDITING OF POSITIONS 433;
RP   441 AND 468.
RC   TISSUE=Brain;
RX   PubMed=20126463; DOI=10.1371/journal.pone.0008956;
RA   Grohmann M., Hammer P., Walther M., Paulmann N., Buttner A.,
RA   Eisenmenger W., Baghai T.C., Schule C., Rupprecht R., Bader M., Bondy B.,
RA   Zill P., Priller J., Walther D.J.;
RT   "Alternative splicing and extensive RNA editing of human TPH2
RT   transcripts.";
RL   PLoS ONE 5:E8956-E8956(2010).
RN   [6]
RP   INVOLVEMENT IN MDD, VARIANT HIS-441, AND CHARACTERIZATION OF VARIANT
RP   HIS-441.
RX   PubMed=15629698; DOI=10.1016/j.neuron.2004.12.014;
RA   Zhang X., Gainetdinov R.R., Beaulieu J.-M., Sotnikova T.D., Burch L.H.,
RA   Williams R.B., Schwartz D.A., Krishnan K.R.R., Caron M.G.;
RT   "Loss-of-function mutation in tryptophan hydroxylase-2 identified in
RT   unipolar major depression.";
RL   Neuron 45:11-16(2005).
RN   [7]
RP   VARIANT ADHD7 TRP-303.
RX   PubMed=18347598; DOI=10.1038/sj.mp.4002152;
RA   McKinney J., Johansson S., Halmoy A., Dramsdahl M., Winge I.,
RA   Knappskog P.M., Haavik J.;
RT   "A loss-of-function mutation in tryptophan hydroxylase 2 segregating with
RT   attention-deficit/hyperactivity disorder.";
RL   Mol. Psychiatry 13:365-367(2008).
RN   [8]
RP   CHARACTERIZATION OF VARIANTS VAL-36; PRO-36; TYR-41; CYS-55; SER-206;
RP   TRP-303; VAL-328; HIS-441 AND GLU-479.
RX   PubMed=19319927; DOI=10.1002/humu.20956;
RA   McKinney J.A., Turel B., Winge I., Knappskog P.M., Haavik J.;
RT   "Functional properties of missense variants of human tryptophan hydroxylase
RT   2.";
RL   Hum. Mutat. 30:787-794(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2
CC         = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-
CC         hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266,
CC         ChEBI:CHEBI:59560; EC=1.14.16.4;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=41.3 uM for L-tryptophan {ECO:0000269|PubMed:17905754};
CC         Vmax=833 nmol/min/mg enzyme {ECO:0000269|PubMed:17905754};
CC   -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis;
CC       serotonin from L-tryptophan: step 1/2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q8IWU9-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q8IWU9-2; Sequence=VSP_040971;
CC   -!- TISSUE SPECIFICITY: Brain specific.
CC   -!- RNA EDITING: Modified_positions=433 {ECO:0000269|PubMed:20126463}, 441
CC       {ECO:0000269|PubMed:20126463}, 468 {ECO:0000269|PubMed:20126463};
CC       Note=Modulates the kinetic properties of both isoforms.;
CC   -!- DISEASE: Major depressive disorder (MDD) [MIM:608516]: A common
CC       psychiatric disorder. It is a complex trait characterized by one or
CC       more major depressive episodes without a history of manic, mixed, or
CC       hypomanic episodes. A major depressive episode is characterized by at
CC       least 2 weeks during which there is a new onset or clear worsening of
CC       either depressed mood or loss of interest or pleasure in nearly all
CC       activities. Four additional symptoms must also be present including
CC       changes in appetite, weight, sleep, and psychomotor activity; decreased
CC       energy; feelings of worthlessness or guilt; difficulty thinking,
CC       concentrating, or making decisions; or recurrent thoughts of death or
CC       suicidal ideation, plans, or attempts. The episode must be accompanied
CC       by distress or impairment in social, occupational, or other important
CC       areas of functioning. {ECO:0000269|PubMed:15629698}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Attention deficit-hyperactivity disorder 7 (ADHD7)
CC       [MIM:613003]: A neurobehavioral developmental disorder primarily
CC       characterized by the coexistence of attentional problems and
CC       hyperactivity, with each behavior occurring infrequently alone.
CC       {ECO:0000269|PubMed:18347598}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC       Naturally occurring variants of TPH2 with impaired enzyme activity
CC       could cause deficiency of serotonin production and result in an
CC       increased risk of developing behavioral disorders.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000305}.
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DR   EMBL; AY098914; AAM28946.1; -; mRNA.
DR   EMBL; AC090109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC114499; AAI14500.1; -; mRNA.
DR   CCDS; CCDS31859.1; -. [Q8IWU9-1]
DR   RefSeq; NP_775489.2; NM_173353.3. [Q8IWU9-1]
DR   PDB; 4V06; X-ray; 2.63 A; A/B=148-490.
DR   PDBsum; 4V06; -.
DR   SMR; Q8IWU9; -.
DR   BioGRID; 125720; 2.
DR   IntAct; Q8IWU9; 3.
DR   STRING; 9606.ENSP00000329093; -.
DR   BindingDB; Q8IWU9; -.
DR   ChEMBL; CHEMBL5433; -.
DR   DrugBank; DB12095; Telotristat ethyl.
DR   DrugBank; DB00150; Tryptophan.
DR   GuidetoPHARMACOLOGY; 1242; -.
DR   GlyGen; Q8IWU9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IWU9; -.
DR   PhosphoSitePlus; Q8IWU9; -.
DR   BioMuta; TPH2; -.
DR   DMDM; 30580625; -.
DR   jPOST; Q8IWU9; -.
DR   MassIVE; Q8IWU9; -.
DR   PaxDb; Q8IWU9; -.
DR   PeptideAtlas; Q8IWU9; -.
DR   PRIDE; Q8IWU9; -.
DR   ProteomicsDB; 70900; -. [Q8IWU9-1]
DR   ProteomicsDB; 70901; -. [Q8IWU9-2]
DR   Antibodypedia; 17122; 568 antibodies.
DR   DNASU; 121278; -.
DR   Ensembl; ENST00000333850; ENSP00000329093; ENSG00000139287. [Q8IWU9-1]
DR   GeneID; 121278; -.
DR   KEGG; hsa:121278; -.
DR   UCSC; uc009zrw.1; human. [Q8IWU9-1]
DR   CTD; 121278; -.
DR   DisGeNET; 121278; -.
DR   GeneCards; TPH2; -.
DR   HGNC; HGNC:20692; TPH2.
DR   HPA; ENSG00000139287; Tissue enriched (brain).
DR   MalaCards; TPH2; -.
DR   MIM; 607478; gene.
DR   MIM; 608516; phenotype.
DR   MIM; 613003; phenotype.
DR   neXtProt; NX_Q8IWU9; -.
DR   OpenTargets; ENSG00000139287; -.
DR   PharmGKB; PA128747823; -.
DR   VEuPathDB; HostDB:ENSG00000139287; -.
DR   eggNOG; KOG3820; Eukaryota.
DR   GeneTree; ENSGT00950000182885; -.
DR   HOGENOM; CLU_023198_0_0_1; -.
DR   InParanoid; Q8IWU9; -.
DR   OMA; TRPFSVH; -.
DR   OrthoDB; 614557at2759; -.
DR   PhylomeDB; Q8IWU9; -.
DR   TreeFam; TF313327; -.
DR   BioCyc; MetaCyc:HS06603-MONOMER; -.
DR   BRENDA; 1.14.16.4; 2681.
DR   PathwayCommons; Q8IWU9; -.
DR   Reactome; R-HSA-209931; Serotonin and melatonin biosynthesis.
DR   SABIO-RK; Q8IWU9; -.
DR   SIGNOR; Q8IWU9; -.
DR   UniPathway; UPA00846; UER00799.
DR   BioGRID-ORCS; 121278; 11 hits in 1004 CRISPR screens.
DR   ChiTaRS; TPH2; human.
DR   GeneWiki; TPH2; -.
DR   GenomeRNAi; 121278; -.
DR   Pharos; Q8IWU9; Tchem.
DR   PRO; PR:Q8IWU9; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q8IWU9; protein.
DR   Bgee; ENSG00000139287; Expressed in secondary oocyte and 50 other tissues.
DR   Genevisible; Q8IWU9; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0042427; P:serotonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03346; eu_TrpOH; 1.
DR   Gene3D; 1.10.800.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005963; Trp_5_mOase.
DR   InterPro; IPR041904; TrpOH_cat.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   PANTHER; PTHR11473; PTHR11473; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; SSF56534; 1.
DR   TIGRFAMs; TIGR01270; Trp_5_monoox; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease variant; Iron; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   RNA editing; Serotonin biosynthesis.
FT   CHAIN           1..490
FT                   /note="Tryptophan 5-hydroxylase 2"
FT                   /id="PRO_0000205574"
FT   DOMAIN          65..140
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          31..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           318
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           323
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           363
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGU9"
FT   VAR_SEQ         147
FT                   /note="E -> GKE (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040971"
FT   VARIANT         36
FT                   /note="L -> P (the property of the variant is
FT                   indistinguishable from the wild-type; dbSNP:rs199775778)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058938"
FT   VARIANT         36
FT                   /note="L -> V (the property of the variant is
FT                   indistinguishable from the wild-type; dbSNP:rs34115267)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058939"
FT   VARIANT         41
FT                   /note="S -> Y (the property of the variant is
FT                   indistinguishable from the wild-type; dbSNP:rs78162420)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058940"
FT   VARIANT         55
FT                   /note="R -> C (the property of the variant is
FT                   indistinguishable from the wild-type; dbSNP:rs75558144)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058941"
FT   VARIANT         206
FT                   /note="P -> S (may be associated with susceptibility to
FT                   bipolar affective disorder; decreases solubility; decreases
FT                   thermal stability; catalytic activity as the wild type;
FT                   moderate loss-of-function observed manifested via stability
FT                   and solubility effect; dbSNP:rs17110563)"
FT                   /evidence="ECO:0000269|PubMed:17905754,
FT                   ECO:0000269|PubMed:19319927"
FT                   /id="VAR_046136"
FT   VARIANT         303
FT                   /note="R -> W (in ADHD7; has severely reduced solubility;
FT                   is completely inactive; loss of function may lead to a
FT                   reduced serotonin synthesis; dbSNP:rs120074176)"
FT                   /evidence="ECO:0000269|PubMed:18347598,
FT                   ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058942"
FT   VARIANT         328
FT                   /note="A -> V (moderate loss-of-function observed
FT                   manifested via stability and solubility effect;
FT                   dbSNP:rs2887147)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058943"
FT   VARIANT         433
FT                   /note="R -> G (in RNA edited version)"
FT                   /id="VAR_065019"
FT   VARIANT         441
FT                   /note="R -> H (linked with susceptibility to major
FT                   depressive disorder; may be due to a rare RNA editing
FT                   event; 80% loss of function; decreases solubility;
FT                   decreases thermal stability; reduces catalytic activity;
FT                   dbSNP:rs120074175)"
FT                   /evidence="ECO:0000269|PubMed:15629698,
FT                   ECO:0000269|PubMed:17905754, ECO:0000269|PubMed:19319927"
FT                   /id="VAR_026749"
FT   VARIANT         468
FT                   /note="Q -> R (in RNA edited version; dbSNP:rs1317926854)"
FT                   /id="VAR_065020"
FT   VARIANT         479
FT                   /note="D -> E (moderate loss-of-function observed
FT                   manifested via stability and solubility effect;
FT                   dbSNP:rs7488262)"
FT                   /evidence="ECO:0000269|PubMed:19319927"
FT                   /id="VAR_058944"
FT   CONFLICT        53
FT                   /note="S -> N (in Ref. 3; AAI14500)"
FT                   /evidence="ECO:0000305"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   TURN            180..183
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           185..199
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           214..228
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           231..234
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           237..249
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           260..270
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          279..282
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          295..298
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           316..322
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           324..327
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           330..343
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           348..359
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   TURN            360..364
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          365..369
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           378..382
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           384..390
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          392..395
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           402..405
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          412..414
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          419..423
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           425..435
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   TURN            436..438
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   TURN            449..452
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   STRAND          453..457
FT                   /evidence="ECO:0007829|PDB:4V06"
FT   HELIX           460..488
FT                   /evidence="ECO:0007829|PDB:4V06"
SQ   SEQUENCE   490 AA;  56057 MW;  753645E6E0CE430B CRC64;
     MQPAMMMFSS KYWARRGFSL DSAVPEEHQL LGSSTLNKPN SGKNDDKGNK GSSKREAATE
     SGKTAVVFSL KNEVGGLVKA LRLFQEKRVN MVHIESRKSR RRSSEVEIFV DCECGKTEFN
     ELIQLLKFQT TIVTLNPPEN IWTEEEELED VPWFPRKISE LDKCSHRVLM YGSELDADHP
     GFKDNVYRQR RKYFVDVAMG YKYGQPIPRV EYTEEETKTW GVVFRELSKL YPTHACREYL
     KNFPLLTKYC GYREDNVPQL EDVSMFLKER SGFTVRPVAG YLSPRDFLAG LAYRVFHCTQ
     YIRHGSDPLY TPEPDTCHEL LGHVPLLADP KFAQFSQEIG LASLGASDED VQKLATCYFF
     TIEFGLCKQE GQLRAYGAGL LSSIGELKHA LSDKACVKAF DPKTTCLQEC LITTFQEAYF
     VSESFEEAKE KMRDFAKSIT RPFSVYFNPY TQSIEILKDT RSIENVVQDL RSDLNTVCDA
     LNKMNQYLGI
//
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