Entry sw:PPA5_HUMAN

ID   PPA5_HUMAN              Reviewed;         325 AA.
AC   P13686; A8K3V2; Q2TAB1; Q6IAS6; Q9UCJ5; Q9UCJ6; Q9UCJ7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 3.
DT   30-NOV-2016, entry version 169.
DE   RecName: Full=Tartrate-resistant acid phosphatase type 5;
DE            Short=TR-AP;
DE            EC=3.1.3.2;
DE   AltName: Full=Tartrate-resistant acid ATPase;
DE            Short=TrATPase;
DE   AltName: Full=Type 5 acid phosphatase;
DE   Flags: Precursor;
GN   Name=ACP5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=2909539;
RA   Ketcham C.M., Roberts R.M., Simmen R.C.M., Nick H.S.;
RT   "Molecular cloning of the type 5, iron-containing, tartrate-resistant
RT   acid phosphatase from human placenta.";
RL   J. Biol. Chem. 264:557-563(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=2338077; DOI=10.1111/j.1432-1033.1990.tb15488.x;
RA   Lord D.K., Cross N.C.P., Bevilacqua M.A., Roder S.H., Gorman P.A.,
RA   Groves A.V., Moss D.W., Sheer D., Cox T.M.;
RT   "Type 5 acid phosphatase. Sequence, expression and chromosomal
RT   localization of a differentiation-associated protein of the human
RT   macrophage.";
RL   Eur. J. Biochem. 189:287-293(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-148 AND
RP   MET-200.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Skin;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
RX   PubMed=8359686; DOI=10.1016/0378-1119(93)90420-8;
RA   Cassady A.I., King A.G., Cross N.C.P., Hume D.A.;
RT   "Isolation and characterization of the genes encoding mouse and human
RT   type-5 acid phosphatase.";
RL   Gene 130:201-207(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 22-64 AND 183-202.
RC   TISSUE=Osteoclastoma;
RX   PubMed=2775236; DOI=10.1042/bj2610601;
RA   Hayman A.R., Warburton M.J., Pringle J.A.S., Coles B., Chambers T.J.;
RT   "Purification and characterization of a tartrate-resistant acid
RT   phosphatase from human osteoclastomas.";
RL   Biochem. J. 261:601-609(1989).
RN   [8]
RP   PROTEIN SEQUENCE OF 22-55 AND 183-203, AND SUBUNIT.
RC   TISSUE=Spleen;
RX   PubMed=1477968; DOI=10.1016/0009-9120(92)90075-4;
RA   Janckila A.J., Latham M.D., Lam K.-W., Chow K.-C., Li C.-Y., Yam L.T.;
RT   "Heterogeneity of hairy cell tartrate-resistant acid phosphatase.";
RL   Clin. Biochem. 25:437-443(1992).
RN   [9]
RP   PROTEIN SEQUENCE OF 22-37.
RC   TISSUE=Osteoclastoma;
RX   PubMed=2610679; DOI=10.1016/0006-291X(89)92705-8;
RA   Stepan J.J., Lau K.H.W., Mohan S., Kraenzlin M., Baylink D.J.;
RT   "Purification and N-terminal sequence of two tartrate-resistant acid
RT   phosphatases type-5 from the hairy cell leukemia spleen.";
RL   Biochem. Biophys. Res. Commun. 165:1027-1034(1989).
RN   [10]
RP   PROTEIN SEQUENCE OF 22-31.
RC   TISSUE=Osteoclastoma;
RX   PubMed=2334436; DOI=10.1016/0006-291X(90)92391-C;
RA   Stepan J.J., Lau K.H.W., Mohan S., Singer F.R., Baylink D.J.;
RT   "Purification and N-terminal amino acid sequence of the tartrate-
RT   resistant acid phosphatase from human osteoclastoma: evidence for a
RT   single structure.";
RL   Biochem. Biophys. Res. Commun. 168:792-800(1990).
RN   [11]
RP   SUBUNIT.
RX   PubMed=1872798; DOI=10.1042/bj2770631;
RA   Hayman A.R., Dryden A.J., Chambers T.J., Warburton M.J.;
RT   "Tartrate-resistant acid phosphatase from human osteoclastomas is
RT   translated as a single polypeptide.";
RL   Biochem. J. 277:631-634(1991).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 22-325 IN COMPLEX WITH IRON
RP   IONS, AND GLYCOSYLATION AT ASN-116.
RX   PubMed=15993892; DOI=10.1016/j.jmb.2005.04.014;
RA   Straeter N., Jasper B., Scholte M., Krebs B., Duff A.P., Langley D.B.,
RA   Han R., Averill B.A., Freeman H.C., Guss J.M.;
RT   "Crystal structures of recombinant human purple acid phosphatase with
RT   and without an inhibitory conformation of the repression loop.";
RL   J. Mol. Biol. 351:233-246(2005).
RN   [13]
RP   VARIANTS SPENCDI ILE-89; ARG-215; ASN-241 AND LYS-264.
RX   PubMed=21217755; DOI=10.1038/ng.748;
RA   Briggs T.A., Rice G.I., Daly S., Urquhart J., Gornall H.,
RA   Bader-Meunier B., Baskar K., Baskar S., Baudouin V., Beresford M.W.,
RA   Black G.C., Dearman R.J., de Zegher F., Foster E.S., Frances C.,
RA   Hayman A.R., Hilton E., Job-Deslandre C., Kulkarni M.L., Le Merrer M.,
RA   Linglart A., Lovell S.C., Maurer K., Musset L., Navarro V., Picard C.,
RA   Puel A., Rieux-Laucat F., Roifman C.M., Scholl-Burgi S., Smith N.,
RA   Szynkiewicz M., Wiedeman A., Wouters C., Zeef L.A., Casanova J.L.,
RA   Elkon K.B., Janckila A., Lebon P., Crow Y.J.;
RT   "Tartrate-resistant acid phosphatase deficiency causes a bone
RT   dysplasia with autoimmunity and a type I interferon expression
RT   signature.";
RL   Nat. Genet. 43:127-131(2011).
RN   [14]
RP   VARIANTS SPENCDI MET-52; ARG-109; PRO-201; ARG-215; HIS-262; LYS-264
RP   AND TYR-278 DEL.
RX   PubMed=21217752; DOI=10.1038/ng.749;
RA   Lausch E., Janecke A., Bros M., Trojandt S., Alanay Y., De Laet C.,
RA   Hubner C.A., Meinecke P., Nishimura G., Matsuo M., Hirano Y.,
RA   Tenoutasse S., Kiss A., Rosa R.F., Unger S.L., Renella R., Bonafe L.,
RA   Spranger J., Unger S., Zabel B., Superti-Furga A.;
RT   "Genetic deficiency of tartrate-resistant acid phosphatase associated
RT   with skeletal dysplasia, cerebral calcifications and autoimmunity.";
RL   Nat. Genet. 43:132-137(2011).
CC   -!- FUNCTION: Involved in osteopontin/bone sialoprotein
CC       dephosphorylation. Its expression seems to increase in certain
CC       pathological states such as Gaucher and Hodgkin diseases, the
CC       hairy cell, the B-cell, and the T-cell leukemias.
CC   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 2 iron ions per subunit.;
CC   -!- SUBUNIT: Exists either as monomer or, after proteolytic
CC       processing, as a dimer of two chains linked by disulfide bond(s).
CC       {ECO:0000269|PubMed:1477968, ECO:0000269|PubMed:15993892,
CC       ECO:0000269|PubMed:1872798}.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- DISEASE: Spondyloenchondrodysplasia with immune dysregulation
CC       (SPENCDI) [MIM:607944]: A disease characterized by vertebral and
CC       metaphyseal dysplasia, spasticity with cerebral calcifications,
CC       and strong predisposition to autoimmune diseases. The skeletal
CC       dysplasia is characterized by radiolucent and irregular spondylar
CC       and metaphyseal lesions that represent islands of chondroid tissue
CC       within bone. {ECO:0000269|PubMed:21217752,
CC       ECO:0000269|PubMed:21217755}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry. ACP5
CC       inactivating mutations result in a functional excess of
CC       phosphorylated osteopontin causing deregulation of osteopontin
CC       signaling and consequential autoimmune disease.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC       Purple acid phosphatase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Tartrate-resistant acid
CC       phosphatase entry;
CC       URL="https://en.wikipedia.org/wiki/Tartrate-resistant_acid_phosphatase";
DR   EMBL; J04430; AAA76849.1; -; mRNA.
DR   EMBL; X14618; CAA32771.1; -; mRNA.
DR   EMBL; CR457078; CAG33359.1; -; mRNA.
DR   EMBL; AK290717; BAF83406.1; -; mRNA.
DR   EMBL; BC025414; AAH25414.1; -; mRNA.
DR   EMBL; BC111014; AAI11015.1; -; mRNA.
DR   EMBL; X67123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS12265.1; -.
DR   PIR; S15752; S15752.
DR   RefSeq; NP_001104504.1; NM_001111034.2.
DR   RefSeq; NP_001104505.1; NM_001111035.2.
DR   RefSeq; NP_001104506.1; NM_001111036.2.
DR   RefSeq; NP_001308952.1; NM_001322023.1.
DR   RefSeq; NP_001602.1; NM_001611.4.
DR   RefSeq; XP_005259995.1; XM_005259938.1.
DR   RefSeq; XP_011526371.1; XM_011528069.2.
DR   UniGene; Hs.1211; -.
DR   PDB; 1WAR; X-ray; 2.22 A; A=22-325.
DR   PDB; 2BQ8; X-ray; 2.20 A; X=22-325.
DR   PDBsum; 1WAR; -.
DR   PDBsum; 2BQ8; -.
DR   ProteinModelPortal; P13686; -.
DR   SMR; P13686; -.
DR   BioGrid; 106570; 11.
DR   IntAct; P13686; 9.
DR   MINT; MINT-1387442; -.
DR   STRING; 9606.ENSP00000218758; -.
DR   DrugBank; DB02325; Isopropyl Alcohol.
DR   DEPOD; P13686; -.
DR   iPTMnet; P13686; -.
DR   PhosphoSitePlus; P13686; -.
DR   BioMuta; ACP5; -.
DR   DMDM; 56757583; -.
DR   EPD; P13686; -.
DR   PaxDb; P13686; -.
DR   PeptideAtlas; P13686; -.
DR   PRIDE; P13686; -.
DR   DNASU; 54; -.
DR   Ensembl; ENST00000218758; ENSP00000218758; ENSG00000102575.
DR   Ensembl; ENST00000412435; ENSP00000392374; ENSG00000102575.
DR   Ensembl; ENST00000433365; ENSP00000413456; ENSG00000102575.
DR   Ensembl; ENST00000592828; ENSP00000468767; ENSG00000102575.
DR   GeneID; 54; -.
DR   KEGG; hsa:54; -.
DR   UCSC; uc002msg.5; human.
DR   CTD; 54; -.
DR   DisGeNET; 54; -.
DR   GeneCards; ACP5; -.
DR   HGNC; HGNC:124; ACP5.
DR   HPA; CAB002584; -.
DR   HPA; HPA057655; -.
DR   HPA; HPA059463; -.
DR   MalaCards; ACP5; -.
DR   MIM; 171640; gene.
DR   MIM; 607944; phenotype.
DR   neXtProt; NX_P13686; -.
DR   OpenTargets; ENSG00000102575; -.
DR   Orphanet; 1855; Spondyloenchondrodysplasia.
DR   PharmGKB; PA24448; -.
DR   eggNOG; KOG2679; Eukaryota.
DR   eggNOG; COG1409; LUCA.
DR   GeneTree; ENSGT00390000016735; -.
DR   HOVERGEN; HBG000433; -.
DR   InParanoid; P13686; -.
DR   KO; K14379; -.
DR   OMA; YYTHTET; -.
DR   OrthoDB; EOG091G0J5W; -.
DR   PhylomeDB; P13686; -.
DR   TreeFam; TF313175; -.
DR   BioCyc; ZFISH:HS02398-MONOMER; -.
DR   BRENDA; 3.1.3.2; 2681.
DR   Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR   SABIO-RK; P13686; -.
DR   ChiTaRS; ACP5; human.
DR   EvolutionaryTrace; P13686; -.
DR   GeneWiki; Tartrate-resistant_acid_phosphatase; -.
DR   GenomeRNAi; 54; -.
DR   PMAP-CutDB; P13686; -.
DR   PRO; PR:P13686; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000102575; -.
DR   CleanEx; HS_ACP5; -.
DR   ExpressionAtlas; P13686; baseline and differential.
DR   Genevisible; P13686; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; TAS:Reactome.
DR   GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR   GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032695; P:negative regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032929; P:negative regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024927; Acid_Pase_5.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000898; Acid_Ptase_5; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Iron;
KW   Lysosome; Metal-binding; Polymorphism; Reference proteome; Signal.
FT   SIGNAL        1     21       {ECO:0000269|PubMed:1477968,
FT                                ECO:0000269|PubMed:2334436,
FT                                ECO:0000269|PubMed:2610679,
FT                                ECO:0000269|PubMed:2775236}.
FT   CHAIN        22    325       Tartrate-resistant acid phosphatase type
FT                                5.
FT                                /FTId=PRO_0000023981.
FT   METAL        33     33       Iron 1.
FT   METAL        71     71       Iron 1.
FT   METAL        71     71       Iron 2.
FT   METAL        74     74       Iron 1.
FT   METAL       110    110       Iron 2.
FT   METAL       205    205       Iron 2.
FT   METAL       240    240       Iron 2.
FT   METAL       242    242       Iron 1.
FT   CARBOHYD    116    116       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:15993892}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    161    219       {ECO:0000250}.
FT   VARIANT      52     52       K -> M (in SPENCDI).
FT                                {ECO:0000269|PubMed:21217752}.
FT                                /FTId=VAR_065920.
FT   VARIANT      89     89       T -> I (in SPENCDI; dbSNP:rs387906668).
FT                                {ECO:0000269|PubMed:21217755}.
FT                                /FTId=VAR_065921.
FT   VARIANT     109    109       G -> R (in SPENCDI; dbSNP:rs781050795).
FT                                {ECO:0000269|PubMed:21217752}.
FT                                /FTId=VAR_065922.
FT   VARIANT     148    148       V -> M (in dbSNP:rs2305799).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_020602.
FT   VARIANT     200    200       V -> M (in dbSNP:rs2229531).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_020603.
FT   VARIANT     201    201       L -> P (in SPENCDI; dbSNP:rs387906672).
FT                                {ECO:0000269|PubMed:21217752}.
FT                                /FTId=VAR_065923.
FT   VARIANT     215    215       G -> R (in SPENCDI; dbSNP:rs781199182).
FT                                {ECO:0000269|PubMed:21217752,
FT                                ECO:0000269|PubMed:21217755}.
FT                                /FTId=VAR_065924.
FT   VARIANT     221    221       V -> I (in dbSNP:rs2229532).
FT                                /FTId=VAR_029288.
FT   VARIANT     241    241       D -> N (in SPENCDI).
FT                                {ECO:0000269|PubMed:21217755}.
FT                                /FTId=VAR_065925.
FT   VARIANT     262    262       N -> H (in SPENCDI).
FT                                {ECO:0000269|PubMed:21217752}.
FT                                /FTId=VAR_065926.
FT   VARIANT     264    264       M -> K (in SPENCDI; dbSNP:rs387906670).
FT                                {ECO:0000269|PubMed:21217752,
FT                                ECO:0000269|PubMed:21217755}.
FT                                /FTId=VAR_065927.
FT   VARIANT     278    278       Missing (in SPENCDI).
FT                                {ECO:0000269|PubMed:21217752}.
FT                                /FTId=VAR_065928.
FT   CONFLICT     45     46       AR -> GP (in Ref. 1; AAA76849).
FT                                {ECO:0000305}.
FT   CONFLICT     47     47       E -> G (in Ref. 8; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     47     47       E -> Q (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       N -> W (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    177    180       DVKL -> LT (in Ref. 1; AAA76849).
FT                                {ECO:0000305}.
FT   STRAND       26     31       {ECO:0000244|PDB:2BQ8}.
FT   HELIX        45     61       {ECO:0000244|PDB:2BQ8}.
FT   STRAND       64     68       {ECO:0000244|PDB:2BQ8}.
FT   TURN         74     76       {ECO:0000244|PDB:2BQ8}.
FT   HELIX        85     89       {ECO:0000244|PDB:2BQ8}.
FT   TURN         90     93       {ECO:0000244|PDB:2BQ8}.
FT   HELIX        97    100       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      104    106       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       110    113       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       117    122       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       123    125       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      128    131       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      134    142       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      149    154       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       157    161       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       164    166       {ECO:0000244|PDB:1WAR}.
FT   HELIX       178    194       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      198    203       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      211    214       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       218    223       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       225    230       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      235    238       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      240    248       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      254    258       {ECO:0000244|PDB:2BQ8}.
FT   HELIX       271    273       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      279    283       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      291    297       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      299    308       {ECO:0000244|PDB:2BQ8}.
FT   STRAND      313    320       {ECO:0000244|PDB:2BQ8}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        26    243       ipfam:Metallophos [T]
SQ   SEQUENCE   325 AA;  36599 MW;  079174A71A5BA264 CRC64;
     MDMWTALLIL QALLLPSLAD GATPALRFVA VGDWGGVPNA PFHTAREMAN AKEIARTVQI
     LGADFILSLG DNFYFTGVQD INDKRFQETF EDVFSDRSLR KVPWYVLAGN HDHLGNVSAQ
     IAYSKISKRW NFPSPFYRLH FKIPQTNVSV AIFMLDTVTL CGNSDDFLSQ QPERPRDVKL
     ARTQLSWLKK QLAAAREDYV LVAGHYPVWS IAEHGPTHCL VKQLRPLLAT YGVTAYLCGH
     DHNLQYLQDE NGVGYVLSGA GNFMDPSKRH QRKVPNGYLR FHYGTEDSLG GFAYVEISSK
     EMTVTYIEAS GKSLFKTRLP RRARP
//