HDHD1_HUMAN
ID HDHD1_HUMAN Reviewed; 228 AA.
AC Q08623; B2R7X6; B4DV93; B7Z6Q3; E9PAV8; F5GWZ2; Q53F84; Q96EB8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Pseudouridine-5'-phosphatase {ECO:0000312|HGNC:HGNC:16818};
DE EC=3.1.3.96;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1;
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 1A;
DE AltName: Full=Protein GS1;
DE AltName: Full=Pseudouridine-5'-monophosphatase;
DE Short=5'-PsiMPase;
GN Name=PUDP {ECO:0000312|HGNC:HGNC:16818};
GN Synonyms=DXF68S1E, FAM16AX, GS1, HDHD1, HDHD1A;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP MET-88.
RC TISSUE=Fetal brain, Neuroepithelioma, and Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver cancer;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Embryonic stem cell, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-228 (ISOFORM 1), AND VARIANT MET-88.
RX PubMed=1284467; DOI=10.1093/hmg/1.1.47;
RA Yen P.H., Ellison J., Salido E.C., Mohandas T., Shapiro L.;
RT "Isolation of a new gene from the distal short arm of the human X
RT chromosome that escapes X-inactivation.";
RL Hum. Mol. Genet. 1:47-52(1992).
RN [7]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Erythrocyte;
RX PubMed=20722631; DOI=10.1042/bj20100174;
RA Preumont A., Rzem R., Vertommen D., Van Schaftingen E.;
RT "HDHD1, which is often deleted in X-linked ichthyosis, encodes a
RT pseudouridine-5'-phosphatase.";
RL Biochem. J. 431:237-244(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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "The crystal structure of human haloacid dehalogenase-like hydrolase domain
RT containing 1A (HDHD1A).";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Dephosphorylates pseudouridine 5'-phosphate, a potential
CC intermediate in rRNA degradation. Pseudouridine is then excreted intact
CC in urine. {ECO:0000269|PubMed:20722631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + psi-UMP = phosphate + pseudouridine;
CC Xref=Rhea:RHEA:10944, ChEBI:CHEBI:15377, ChEBI:CHEBI:17802,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58380; EC=3.1.3.96;
CC Evidence={ECO:0000269|PubMed:20722631};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20722631};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 uM for 5'-PsiMP {ECO:0000269|PubMed:20722631};
CC KM=1.5 mM for 3'-AMP {ECO:0000269|PubMed:20722631};
CC KM=5.9 mM for Fructose-6-P {ECO:0000269|PubMed:20722631};
CC KM=9.4 mM for 5'-UMP {ECO:0000269|PubMed:20722631};
CC -!- INTERACTION:
CC Q08623; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-12807240, EBI-8643161;
CC Q08623; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-12807240, EBI-748515;
CC Q08623; P43358: MAGEA4; NbExp=3; IntAct=EBI-12807240, EBI-743122;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q08623-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08623-2; Sequence=VSP_040029;
CC Name=3;
CC IsoId=Q08623-3; Sequence=VSP_042020;
CC Name=4;
CC IsoId=Q08623-4; Sequence=VSP_044804;
CC -!- INDUCTION: Inhibited by low concentrations of calcium.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58622.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12494.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD97125.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG35973.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK300985; BAG62605.1; -; mRNA.
DR EMBL; AK313155; BAG35973.1; ALT_INIT; mRNA.
DR EMBL; AK223405; BAD97125.1; ALT_INIT; mRNA.
DR EMBL; AK300740; BAH13339.1; -; mRNA.
DR EMBL; AC073583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98748.1; -; Genomic_DNA.
DR EMBL; BC012494; AAH12494.1; ALT_INIT; mRNA.
DR EMBL; DR156836; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M86934; AAA58622.1; ALT_INIT; mRNA.
DR CCDS; CCDS48075.1; -. [Q08623-1]
DR CCDS; CCDS48076.1; -. [Q08623-4]
DR CCDS; CCDS55366.1; -. [Q08623-3]
DR CCDS; CCDS55367.1; -. [Q08623-2]
DR RefSeq; NP_001129037.1; NM_001135565.1. [Q08623-4]
DR RefSeq; NP_001171606.1; NM_001178135.1. [Q08623-3]
DR RefSeq; NP_001171607.1; NM_001178136.1. [Q08623-2]
DR RefSeq; NP_036212.3; NM_012080.4. [Q08623-1]
DR PDB; 3L5K; X-ray; 2.00 A; A=1-228.
DR PDBsum; 3L5K; -.
DR AlphaFoldDB; Q08623; -.
DR SMR; Q08623; -.
DR BioGRID; 113859; 73.
DR IntAct; Q08623; 3.
DR STRING; 9606.ENSP00000396452; -.
DR DEPOD; PUDP; -.
DR iPTMnet; Q08623; -.
DR PhosphoSitePlus; Q08623; -.
DR BioMuta; PUDP; -.
DR DMDM; 269849688; -.
DR EPD; Q08623; -.
DR jPOST; Q08623; -.
DR MassIVE; Q08623; -.
DR MaxQB; Q08623; -.
DR PeptideAtlas; Q08623; -.
DR PRIDE; Q08623; -.
DR ProteomicsDB; 19089; -.
DR ProteomicsDB; 58634; -. [Q08623-1]
DR ProteomicsDB; 58635; -. [Q08623-2]
DR ProteomicsDB; 58636; -. [Q08623-3]
DR Antibodypedia; 23565; 165 antibodies from 14 providers.
DR DNASU; 8226; -.
DR Ensembl; ENST00000381077.10; ENSP00000370467.6; ENSG00000130021.15. [Q08623-1]
DR Ensembl; ENST00000412827.6; ENSP00000406260.2; ENSG00000130021.15. [Q08623-2]
DR Ensembl; ENST00000424830.6; ENSP00000396452.2; ENSG00000130021.15. [Q08623-4]
DR Ensembl; ENST00000486446.3; ENSP00000430995.2; ENSG00000130021.15. [Q08623-3]
DR GeneID; 8226; -.
DR KEGG; hsa:8226; -.
DR MANE-Select; ENST00000381077.10; ENSP00000370467.6; NM_012080.5; NP_036212.3.
DR UCSC; uc004crv.2; human. [Q08623-1]
DR CTD; 8226; -.
DR DisGeNET; 8226; -.
DR GeneCards; PUDP; -.
DR HGNC; HGNC:16818; PUDP.
DR HPA; ENSG00000130021; Low tissue specificity.
DR MIM; 306480; gene.
DR neXtProt; NX_Q08623; -.
DR OpenTargets; ENSG00000130021; -.
DR PharmGKB; PA165756731; -.
DR VEuPathDB; HostDB:ENSG00000130021; -.
DR eggNOG; KOG2914; Eukaryota.
DR GeneTree; ENSGT00390000014753; -.
DR HOGENOM; CLU_045011_13_0_1; -.
DR OMA; DSERVYT; -.
DR OrthoDB; 1510544at2759; -.
DR PhylomeDB; Q08623; -.
DR TreeFam; TF105946; -.
DR PathwayCommons; Q08623; -.
DR Reactome; R-HSA-73614; Pyrimidine salvage.
DR SignaLink; Q08623; -.
DR BioGRID-ORCS; 8226; 9 hits in 693 CRISPR screens.
DR ChiTaRS; PUDP; human.
DR EvolutionaryTrace; Q08623; -.
DR GeneWiki; HDHD1A; -.
DR GenomeRNAi; 8226; -.
DR Pharos; Q08623; Tbio.
DR PRO; PR:Q08623; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q08623; protein.
DR Bgee; ENSG00000130021; Expressed in skeletal muscle tissue of rectus abdominis and 200 other tissues.
DR ExpressionAtlas; Q08623; baseline and differential.
DR Genevisible; Q08623; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:1990738; F:pseudouridine 5'-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07529; HAD_AtGPP-like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR045228; Gpp1/Gpp2-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Reference proteome.
FT CHAIN 1..228
FT /note="Pseudouridine-5'-phosphatase"
FT /id="PRO_0000108068"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 16
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 20
FT /note="L -> LGYTGSIVAAASGESSRGLQSRWT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044804"
FT VAR_SEQ 51..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040029"
FT VAR_SEQ 171..228
FT /note="CLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELF
FT GLPSYE -> SSIHRPRLLTAQKCQGCRDPFSALLLLCNQLLLCSDDT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042020"
FT VARIANT 88
FT /note="T -> M (in dbSNP:rs1131197)"
FT /evidence="ECO:0000269|PubMed:1284467,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_061094"
FT VARIANT 165
FT /note="P -> A (in dbSNP:rs3747386)"
FT /id="VAR_060625"
FT CONFLICT 116
FT /note="G -> R (in Ref. 5; AAH12494)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> G (in Ref. 1; BAD97125)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> A (in Ref. 6; AAA58622)"
FT /evidence="ECO:0000305"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:3L5K"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:3L5K"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3L5K"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3L5K"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:3L5K"
FT CONFLICT Q08623-3:198
FT /note="C -> S (in Ref. 1; BAH13339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25249 MW; EF9B8CC51C122924 CRC64;
MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI
IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF
DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG
VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE
