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 03-AUG-2022, entry version 206.
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; DOI=10.1016/s0021-9258(17)31295-4;
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 variants 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";
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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 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 AlphaFoldDB; P13686; -.
DR SMR; P13686; -.
DR BioGRID; 106570; 30.
DR IntAct; P13686; 12.
DR MINT; P13686; -.
DR STRING; 9606.ENSP00000468767; -.
DR DEPOD; ACP5; -.
DR GlyGen; P13686; 3 sites.
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; 587 antibodies from 34 providers.
DR DNASU; 54; -.
DR Ensembl; ENST00000218758.9; ENSP00000218758.4; ENSG00000102575.13.
DR Ensembl; ENST00000412435.6; ENSP00000392374.1; ENSG00000102575.13.
DR Ensembl; ENST00000648477.1; ENSP00000496973.1; ENSG00000102575.13.
DR GeneID; 54; -.
DR KEGG; hsa:54; -.
DR MANE-Select; ENST00000648477.1; ENSP00000496973.1; NM_001611.5; NP_001602.1.
DR UCSC; uc002msg.5; human.
DR CTD; 54; -.
DR DisGeNET; 54; -.
DR GeneCards; ACP5; -.
DR HGNC; HGNC:124; ACP5.
DR HPA; ENSG00000102575; Tissue enhanced (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 VEuPathDB; HostDB:ENSG00000102575; -.
DR eggNOG; KOG2679; Eukaryota.
DR GeneTree; ENSGT00390000016735; -.
DR HOGENOM; CLU_043332_1_0_1; -.
DR InParanoid; P13686; -.
DR OMA; VTVAIFM; -.
DR OrthoDB; 711825at2759; -.
DR PhylomeDB; P13686; -.
DR TreeFam; TF313175; -.
DR BRENDA; 3.1.3.2; 2681.
DR PathwayCommons; P13686; -.
DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR SABIO-RK; P13686; -.
DR SignaLink; P13686; -.
DR SIGNOR; P13686; -.
DR BioGRID-ORCS; 54; 18 hits in 1068 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 152 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:0016311; P:dephosphorylation; 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:0010936; P:negative regulation of macrophage cytokine 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:0006809; P:nitric oxide biosynthetic process; 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:0042554; P:superoxide anion generation; IEA:Ensembl.
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.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Hydrolase; Iron; Lysosome; Metal-binding; Reference proteome;
KW 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 BINDING 33
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 71
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 71
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="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:0007829|PDB:2BQ8"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2BQ8"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2BQ8"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1WAR"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2BQ8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:2BQ8"
FT STRAND 313..320
FT /evidence="ECO:0007829|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
