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 27-MAR-2024, entry version 214. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 31. DR IntAct; P13686; 12. DR MINT; P13686; -. DR STRING; 9606.ENSP00000218758; -. DR DEPOD; ACP5; -. DR GlyCosmos; P13686; 2 sites, No reported glycans. 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; 9606-ENSP00000468767; -. DR PeptideAtlas; P13686; -. DR ProteomicsDB; 52960; -. DR Antibodypedia; 25921; 671 antibodies from 34 providers. DR DNASU; 54; -. DR Ensembl; ENST00000218758.10; ENSP00000218758.4; ENSG00000102575.14. DR Ensembl; ENST00000412435.7; ENSP00000392374.1; ENSG00000102575.14. DR Ensembl; ENST00000589792.6; ENSP00000468685.2; ENSG00000102575.14. DR Ensembl; ENST00000590832.2; ENSP00000465127.2; ENSG00000102575.14. DR Ensembl; ENST00000591319.2; ENSP00000464831.2; ENSG00000102575.14. DR Ensembl; ENST00000592659.2; ENSP00000465498.2; ENSG00000102575.14. DR Ensembl; ENST00000592828.7; ENSP00000468767.3; ENSG00000102575.14. DR Ensembl; ENST00000648477.1; ENSP00000496973.1; ENSG00000102575.14. DR Ensembl; ENST00000649386.2; ENSP00000497140.2; ENSG00000102575.14. DR Ensembl; ENST00000695791.1; ENSP00000512173.1; ENSG00000102575.14. DR Ensembl; ENST00000695811.1; ENSP00000512191.1; ENSG00000102575.14. 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 AGR; HGNC:124; -. 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; 364192at2759; -. 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; 19 hits in 1157 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 153 other cell types or tissues. DR ExpressionAtlas; P13686; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. 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 PANTHER; PTHR10161; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1. DR PANTHER; PTHR10161:SF14; TARTRATE-RESISTANT ACID PHOSPHATASE TYPE 5; 1. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000898; Acid_Ptase_5; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR Genevisible; P13686; HS. 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 //