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 10-MAY-2017, entry version 172.
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";
CC -----------------------------------------------------------------------
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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 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: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...) asparagine.
FT {ECO:0000269|PubMed:15993892}.
FT CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
FT {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
//
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