GenomeNet

Database: UniProt
Entry: P13686
LinkDB: P13686
Original site: P13686 
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   17-JUN-2020, entry version 197.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 acid
RT   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 localization
RT   of a differentiation-associated protein of the human macrophage.";
RL   Eur. J. Biochem. 189:287-293(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-148 AND 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., 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   [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 project:
RT   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 type-
RT   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 phosphatase
RT   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-resistant
RT   acid phosphatase from human osteoclastoma: evidence for a single
RT   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 IONS,
RP   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 and
RT   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., Bader-Meunier B.,
RA   Baskar K., Baskar S., Baudouin V., Beresford M.W., Black G.C.,
RA   Dearman R.J., de Zegher F., Foster E.S., Frances C., Hayman A.R.,
RA   Hilton E., Job-Deslandre C., Kulkarni M.L., Le Merrer M., Linglart A.,
RA   Lovell S.C., Maurer K., Musset L., Navarro V., Picard C., Puel A.,
RA   Rieux-Laucat F., Roifman C.M., Scholl-Burgi S., Smith N., Szynkiewicz M.,
RA   Wiedeman A., Wouters C., Zeef L.A., Casanova J.L., Elkon K.B., Janckila A.,
RA   Lebon P., Crow Y.J.;
RT   "Tartrate-resistant acid phosphatase deficiency causes a bone dysplasia
RT   with autoimmunity and a type I interferon expression 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 AND
RP   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 with
RT   skeletal dysplasia, cerebral calcifications and autoimmunity.";
RL   Nat. Genet. 43:132-137(2011).
CC   -!- FUNCTION: Involved in osteopontin/bone sialoprotein dephosphorylation.
CC       Its expression seems to increase in certain pathological states such as
CC       Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-
CC       cell leukemias.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
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 processing, as
CC       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 (SPENCDI)
CC       [MIM:607944]: A disease characterized by vertebral and metaphyseal
CC       dysplasia, spasticity with cerebral calcifications, and strong
CC       predisposition to autoimmune diseases. The skeletal dysplasia is
CC       characterized by radiolucent and irregular spondylar and metaphyseal
CC       lesions that represent islands of chondroid tissue within bone.
CC       {ECO:0000269|PubMed:21217752, ECO:0000269|PubMed:21217755}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry. ACP5 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. Purple
CC       acid phosphatase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Tartrate-resistant acid phosphatase
CC       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   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   SMR; P13686; -.
DR   BioGRID; 106570; 25.
DR   IntAct; P13686; 12.
DR   MINT; P13686; -.
DR   STRING; 9606.ENSP00000468767; -.
DR   DrugBank; DB02325; Isopropyl alcohol.
DR   DEPOD; P13686; -.
DR   iPTMnet; P13686; -.
DR   PhosphoSitePlus; P13686; -.
DR   BioMuta; ACP5; -.
DR   DMDM; 56757583; -.
DR   jPOST; P13686; -.
DR   MassIVE; P13686; -.
DR   PaxDb; P13686; -.
DR   PeptideAtlas; P13686; -.
DR   PRIDE; P13686; -.
DR   ProteomicsDB; 52960; -.
DR   Antibodypedia; 25921; 556 antibodies.
DR   DNASU; 54; -.
DR   Ensembl; ENST00000218758; ENSP00000218758; ENSG00000102575.
DR   Ensembl; ENST00000412435; ENSP00000392374; ENSG00000102575.
DR   Ensembl; ENST00000648477; ENSP00000496973; ENSG00000102575.
DR   GeneID; 54; -.
DR   KEGG; hsa:54; -.
DR   UCSC; uc002msg.5; human.
DR   CTD; 54; -.
DR   DisGeNET; 54; -.
DR   EuPathDB; HostDB:ENSG00000102575.10; -.
DR   GeneCards; ACP5; -.
DR   HGNC; HGNC:124; ACP5.
DR   HPA; ENSG00000102575; Tissue enhanced (adipose tissue, lung).
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   HOGENOM; CLU_043332_1_0_1; -.
DR   InParanoid; P13686; -.
DR   KO; K14379; -.
DR   OMA; RFHYGSE; -.
DR   OrthoDB; 711825at2759; -.
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   SIGNOR; P13686; -.
DR   BioGRID-ORCS; 54; 5 hits in 786 CRISPR screens.
DR   ChiTaRS; ACP5; human.
DR   EvolutionaryTrace; P13686; -.
DR   GeneWiki; Tartrate-resistant_acid_phosphatase; -.
DR   GenomeRNAi; 54; -.
DR   Pharos; P13686; Tbio.
DR   PRO; PR:P13686; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P13686; protein.
DR   Bgee; ENSG00000102575; Expressed in periodontal ligament and 158 other tissues.
DR   ExpressionAtlas; P13686; baseline and differential.
DR   Genevisible; P13686; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IBA:GO_Central.
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; IBA:GO_Central.
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:0001503; P:ossification; IBA:GO_Central.
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   CDD; cd07378; MPP_ACP5; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024927; Acid_PPase.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disease mutation; Disulfide bond;
KW   Glycoprotein; Hydrolase; Iron; Lysosome; Metal-binding; Polymorphism;
KW   Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1477968,
FT                   ECO:0000269|PubMed:2334436, ECO:0000269|PubMed:2610679,
FT                   ECO:0000269|PubMed:2775236"
FT   CHAIN           22..325
FT                   /note="Tartrate-resistant acid phosphatase type 5"
FT                   /id="PRO_0000023981"
FT   METAL           33
FT                   /note="Iron 1"
FT   METAL           71
FT                   /note="Iron 1"
FT   METAL           71
FT                   /note="Iron 2"
FT   METAL           74
FT                   /note="Iron 1"
FT   METAL           110
FT                   /note="Iron 2"
FT   METAL           205
FT                   /note="Iron 2"
FT   METAL           240
FT                   /note="Iron 2"
FT   METAL           242
FT                   /note="Iron 1"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15993892"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        161..219
FT                   /evidence="ECO:0000250"
FT   VARIANT         52
FT                   /note="K -> M (in SPENCDI)"
FT                   /evidence="ECO:0000269|PubMed:21217752"
FT                   /id="VAR_065920"
FT   VARIANT         89
FT                   /note="T -> I (in SPENCDI; dbSNP:rs387906668)"
FT                   /evidence="ECO:0000269|PubMed:21217755"
FT                   /id="VAR_065921"
FT   VARIANT         109
FT                   /note="G -> R (in SPENCDI; dbSNP:rs781050795)"
FT                   /evidence="ECO:0000269|PubMed:21217752"
FT                   /id="VAR_065922"
FT   VARIANT         148
FT                   /note="V -> M (in dbSNP:rs2305799)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_020602"
FT   VARIANT         200
FT                   /note="V -> M (in dbSNP:rs2229531)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_020603"
FT   VARIANT         201
FT                   /note="L -> P (in SPENCDI; dbSNP:rs387906672)"
FT                   /evidence="ECO:0000269|PubMed:21217752"
FT                   /id="VAR_065923"
FT   VARIANT         215
FT                   /note="G -> R (in SPENCDI; dbSNP:rs781199182)"
FT                   /evidence="ECO:0000269|PubMed:21217752,
FT                   ECO:0000269|PubMed:21217755"
FT                   /id="VAR_065924"
FT   VARIANT         221
FT                   /note="V -> I (in dbSNP:rs2229532)"
FT                   /id="VAR_029288"
FT   VARIANT         241
FT                   /note="D -> N (in SPENCDI)"
FT                   /evidence="ECO:0000269|PubMed:21217755"
FT                   /id="VAR_065925"
FT   VARIANT         262
FT                   /note="N -> H (in SPENCDI; dbSNP:rs1449857485)"
FT                   /evidence="ECO:0000269|PubMed:21217752"
FT                   /id="VAR_065926"
FT   VARIANT         264
FT                   /note="M -> K (in SPENCDI; dbSNP:rs387906670)"
FT                   /evidence="ECO:0000269|PubMed:21217752,
FT                   ECO:0000269|PubMed:21217755"
FT                   /id="VAR_065927"
FT   VARIANT         278
FT                   /note="Missing (in SPENCDI)"
FT                   /evidence="ECO:0000269|PubMed:21217752"
FT                   /id="VAR_065928"
FT   CONFLICT        45..46
FT                   /note="AR -> GP (in Ref. 1; AAA76849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="E -> G (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="E -> Q (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="N -> W (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177..180
FT                   /note="DVKL -> LT (in Ref. 1; AAA76849)"
FT                   /evidence="ECO:0000305"
FT   STRAND          26..31
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           45..61
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          64..68
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   TURN            74..76
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           85..89
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   TURN            90..93
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           97..100
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          104..106
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           110..113
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           117..122
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           123..125
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          128..131
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          134..142
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          149..154
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           157..161
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           164..166
FT                   /evidence="ECO:0000244|PDB:1WAR"
FT   HELIX           178..194
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          198..203
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          211..214
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           218..223
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           225..230
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          235..238
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          240..248
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          254..258
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   HELIX           271..273
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          279..283
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          291..297
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          299..308
FT                   /evidence="ECO:0000244|PDB:2BQ8"
FT   STRAND          313..320
FT                   /evidence="ECO:0000244|PDB:2BQ8"
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
//
DBGET integrated database retrieval system