TPH2_HUMAN
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 03-AUG-2022, entry version 166.
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 AlphaFoldDB; Q8IWU9; -.
DR SMR; Q8IWU9; -.
DR BioGRID; 125720; 5.
DR IntAct; Q8IWU9; 3.
DR MINT; Q8IWU9; -.
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; 570 antibodies from 37 providers.
DR DNASU; 121278; -.
DR Ensembl; ENST00000333850.4; ENSP00000329093.3; ENSG00000139287.13. [Q8IWU9-1]
DR GeneID; 121278; -.
DR KEGG; hsa:121278; -.
DR MANE-Select; ENST00000333850.4; ENSP00000329093.3; NM_173353.4; NP_775489.2.
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; MASGHVM; -.
DR OrthoDB; 614557at2759; -.
DR PhylomeDB; Q8IWU9; -.
DR TreeFam; TF313327; -.
DR BioCyc; MetaCyc:HS06603-MON; -.
DR BRENDA; 1.14.16.4; 2681.
DR PathwayCommons; Q8IWU9; -.
DR Reactome; R-HSA-209931; Serotonin and melatonin biosynthesis.
DR SABIO-RK; Q8IWU9; -.
DR SignaLink; Q8IWU9; -.
DR SIGNOR; Q8IWU9; -.
DR UniPathway; UPA00846; UER00799.
DR BioGRID-ORCS; 121278; 14 hits in 1061 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 71 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; IPR045865; ACT-like_dom_sf.
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; SSF55021; SSF55021; 1.
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 BINDING 318
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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
