ID SAP_HUMAN Reviewed; 524 AA. AC P07602; P07292; P15793; P78538; P78541; P78546; P78547; P78558; AC Q53Y86; Q6IBQ6; Q92739; Q92740; Q92741; Q92742; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 2. DT 09-DEC-2015, entry version 201. DE RecName: Full=Prosaposin; DE AltName: Full=Proactivator polypeptide; DE Contains: DE RecName: Full=Saposin-A; DE AltName: Full=Protein A; DE Contains: DE RecName: Full=Saposin-B-Val; DE Contains: DE RecName: Full=Saposin-B; DE AltName: Full=Cerebroside sulfate activator; DE Short=CSAct; DE AltName: Full=Dispersin; DE AltName: Full=Sphingolipid activator protein 1; DE Short=SAP-1; DE AltName: Full=Sulfatide/GM1 activator; DE Contains: DE RecName: Full=Saposin-C; DE AltName: Full=A1 activator; DE AltName: Full=Co-beta-glucosidase; DE AltName: Full=Glucosylceramidase activator; DE AltName: Full=Sphingolipid activator protein 2; DE Short=SAP-2; DE Contains: DE RecName: Full=Saposin-D; DE AltName: Full=Component C; DE AltName: Full=Protein C; DE Flags: Precursor; GN Name=PSAP; Synonyms=GLBA, SAP1; 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=Liver; RX PubMed=2515150; DOI=10.1016/0888-7543(89)90014-1; RA Rorman E.G., Grabowski G.A.; RT "Molecular cloning of a human co-beta-glucosidase cDNA: evidence that RT four sphingolipid hydrolase activator proteins are encoded by single RT genes in humans and rats."; RL Genomics 5:486-492(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2498298; RA Nakano T., Sandhoff K., Stuemper J., Christomanou H., Suzuki K.; RT "Structure of full-length cDNA coding for sulfatide activator, a Co- RT beta-glucosidase and two other homologous proteins: two alternate RT forms of the sulfatide activator."; RL J. Biochem. 105:152-154(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SAP-MU-0). RC TISSUE=Brain, Eye, 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-524. RX PubMed=2842863; DOI=10.1126/science.2842863; RA O'Brien J.S., Kretz K.A., Dewji N., Wenger D.A., Esch F., RA Fluharty A.L.; RT "Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by RT same genetic locus."; RL Science 241:1098-1101(1988). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-524. RX PubMed=1612590; DOI=10.1016/0888-7543(92)90247-P; RA Rorman E.G., Scheinker V., Grabowski G.A.; RT "Structure and evolution of the human prosaposin chromosomal gene."; RL Genomics 13:312-318(1992). RN [10] RP PROTEIN SEQUENCE OF 17-24 AND 165-172. RX PubMed=8323276; DOI=10.1006/abbi.1993.1328; RA Hiraiwa M., O'Brien J.S., Kishimoto Y., Galdzicka M., Fluharty A.L., RA Ginns E.I., Martin B.M.; RT "Isolation, characterization, and proteolysis of human prosaposin, the RT precursor of saposins (sphingolipid activator proteins)."; RL Arch. Biochem. Biophys. 304:110-116(1993). RN [11] RP PROTEIN SEQUENCE OF 17-26. RC TISSUE=Milk; RX PubMed=1958198; DOI=10.1016/S0006-291X(05)81415-9; RA Kondoh K., Hineno T., Sano A., Kakimoto Y.; RT "Isolation and characterization of prosaposin from human milk."; RL Biochem. Biophys. Res. Commun. 181:286-292(1991). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-125 AND 304-513. RC TISSUE=Brain; RX PubMed=2013321; DOI=10.1016/0014-5793(91)80308-P; RA Holtschmidt H., Sandhoff K., Fuerst W., Kwon H.Y., Schnabel D., RA Suzuki K.; RT "The organization of the gene for the human cerebroside sulfate RT activator protein."; RL FEBS Lett. 280:267-270(1991). RN [13] RP PROTEIN SEQUENCE OF 60-142. RX PubMed=2717620; DOI=10.1073/pnas.86.9.3389; RA Morimoto S., Martin B.M., Yamamoto Y., Kretz K.A., O'Brien J.S., RA Kishimoto Y.; RT "Saposin A: second cerebrosidase activator protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:3389-3393(1989). RN [14] RP PROTEIN SEQUENCE OF 62-84 AND 410-431. RX PubMed=8370464; DOI=10.1016/0014-5793(93)80908-D; RA Tyynela J., Palmer D.N., Baumann M., Haltia M.; RT "Storage of saposins A and D in infantile neuronal ceroid- RT lipofuscinosis."; RL FEBS Lett. 330:8-12(1993). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 164-524. RX PubMed=2825202; DOI=10.1073/pnas.84.23.8652; RA Dewji N.N., Wenger D.A., O'Brien J.S.; RT "Nucleotide sequence of cloned cDNA for human sphingolipid activator RT protein 1 precursor."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8652-8656(1987). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 195-263. RX PubMed=2868718; DOI=10.1016/S0006-291X(86)80518-6; RA Dewji N.N., Wenger D.A., Fujibayashi S., Donoviel M., Esch F., RA Hill F., O'Brien J.S.; RT "Molecular cloning of the sphingolipid activator protein-1 (SAP-1), RT the sulfatide sulfatase activator."; RL Biochem. Biophys. Res. Commun. 134:989-994(1986). RN [17] RP PROTEIN SEQUENCE OF 195-274. RX PubMed=3242555; RA Kleinschmidt T., Christomanou H., Braunitzer G.; RT "Complete amino-acid sequence of the naturally occurring A2 activator RT protein for enzymic sphingomyelin degradation: identity to the RT sulfatide activator protein (SAP-1)."; RL Biol. Chem. Hoppe-Seyler 369:1361-1365(1988). RN [18] RP PROTEIN SEQUENCE OF 195-274. RC TISSUE=Kidney; RX PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x; RA Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.; RT "The complete amino-acid sequences of human ganglioside GM2 activator RT protein and cerebroside sulfate activator protein."; RL Eur. J. Biochem. 192:709-714(1990). RN [19] RP PROTEIN SEQUENCE OF 311-390. RX PubMed=3442600; RA Kleinschmidt T., Christomanou H., Braunitzer G.; RT "Complete amino-acid sequence and carbohydrate content of the RT naturally occurring glucosylceramide activator protein (A1 activator) RT absent from a new human Gaucher disease variant."; RL Biol. Chem. Hoppe-Seyler 368:1571-1578(1987). RN [20] RP PROTEIN SEQUENCE OF 405-484. RX PubMed=2845979; DOI=10.1016/S0006-291X(88)80855-6; RA Morimoto S., Martin B.M., Kishimoto Y., O'Brien J.S.; RT "Saposin D: a sphingomyelinase activator."; RL Biochem. Biophys. Res. Commun. 156:403-410(1988). RN [21] RP PROTEIN SEQUENCE OF 407-484. RX PubMed=3048308; RA Furst W., Machleidt W., Sandhoff K.; RT "The precursor of sulfatide activator protein is processed to three RT different proteins."; RL Biol. Chem. Hoppe-Seyler 369:317-328(1988). RN [22] RP PARTIAL PROTEIN SEQUENCE (SAPOSIN-B), AND STRUCTURE OF CARBOHYDRATES. RC TISSUE=Urine; RX PubMed=10562467; DOI=10.1006/mgme.1999.2900; RA Fluharty A.L., Lombardo C., Louis A., Stevens R.L., Whitelegge J.P., RA Waring A.J., To T., Fluharty C.B., Faull K.F.; RT "Preparation of the cerebroside sulfate activator (CSAct or saposin B) RT from human urine."; RL Mol. Genet. Metab. 68:391-403(1999). RN [23] RP DISULFIDE BONDS IN SAPOSINS-B AND C, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=7730378; DOI=10.1074/jbc.270.17.9953; RA Vaccaro A.M., Salvioli R., Barca A., Tatti M., Ciaffoni F., Maras B., RA Siciliano R., Zappacosta F., Amoresano A., Pucci P.; RT "Structural analysis of saposin C and B. Complete localization of RT disulfide bridges."; RL J. Biol. Chem. 270:9953-9960(1995). RN [24] RP FUNCTION. RX PubMed=10383054; RX DOI=10.1002/(SICI)1098-1136(199906)26:4<353::AID-GLIA9>3.3.CO;2-7; RA Hiraiwa M., Campana W.M., Mizisin A.P., Mohiuddin L., O'Brien J.S.; RT "Prosaposin: a myelinotrophic protein that promotes expression of RT myelin constituents and is secreted after nerve injury."; RL Glia 26:353-360(1999). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Urine; RX PubMed=10510427; RX DOI=10.1002/(SICI)1096-9888(199910)34:10<1040::AID-JMS863>3.0.CO;2-X; RA Faull K.F., Whitelegge J.P., Higginson J., To T., Johnson J., RA Krutchinsky A.N., Standing K.G., Waring A.J., Stevens R.L., RA Fluharty C.B., Fluharty A.L.; RT "Cerebroside sulfate activator protein (Saposin B): chromatographic RT and electrospray mass spectrometric properties."; RL J. Mass Spectrom. 34:1040-1054(1999). RN [26] RP STRUCTURE OF CARBOHYDRATE ON ASN-215. RX PubMed=11180632; RX DOI=10.1002/1096-9888(200012)35:12<1416::AID-JMS75>3.0.CO;2-K; RA Faull K.F., Johnson J., Kim M.J., To T., Whitelegge J.P., RA Stevens R.L., Fluharty C.B., Fluharty A.L.; RT "Structure of the asparagine-linked sugar chains of porcine kidney and RT human urine cerebroside sulfate activator protein."; RL J. Mass Spectrom. 35:1416-1424(2000). RN [27] RP DISULFIDE BONDS IN SAPOSIN-D. RX PubMed=10406958; DOI=10.1046/j.1432-1327.1999.00521.x; RA Tatti M., Salvioli R., Ciaffoni F., Pucci P., Andolfo A., RA Amoresano A., Vaccaro A.M.; RT "Structural and membrane-binding properties of saposin D."; RL Eur. J. Biochem. 263:486-494(1999). RN [28] RP SUBCELLULAR LOCATION, AND INTERACTION WITH SORT1. RX PubMed=14657016; DOI=10.1093/emboj/cdg629; RA Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.; RT "The lysosomal trafficking of sphingolipid activator proteins (SAPs) RT is mediated by sortilin."; RL EMBO J. 22:6430-6437(2003). RN [29] RP DISULFIDE BONDS IN SAPOSIN-B. RX PubMed=12510003; DOI=10.1016/S1046-5928(02)00597-1; RA Ahn V.E., Faull K.F., Whitelegge J.P., Higginson J., Fluharty A.L., RA Prive G.G.; RT "Expression, purification, crystallization, and preliminary X-ray RT analysis of recombinant human saposin B."; RL Protein Expr. Purif. 27:186-193(2003). RN [30] RP GLYCOSYLATION AT ASN-80; ASN-101; ASN-215; ASN-332 AND ASN-426. RX PubMed=19167329; DOI=10.1016/j.cell.2008.11.047; RA Ruiz-Canada C., Kelleher D.J., Gilmore R.; RT "Cotranslational and posttranslational N-glycosylation of polypeptides RT by distinct mammalian OST isoforms."; RL Cell 136:272-283(2009). RN [31] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80; ASN-101; ASN-332 AND RP ASN-426. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [33] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=21835174; DOI=10.1016/j.yexcr.2011.07.017; RA Yuan L., Morales C.R.; RT "Prosaposin sorting is mediated by oligomerization."; RL Exp. Cell Res. 317:2456-2467(2011). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [35] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-16, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 195-273, AND MUTAGENESIS OF RP ILE-240. RX PubMed=12518053; DOI=10.1073/pnas.0136947100; RA Ahn V.E., Faull K.F., Whitelegge J.P., Fluharty A.L., Prive G.G.; RT "Crystal structure of saposin B reveals a dimeric shell for lipid RT binding."; RL Proc. Natl. Acad. Sci. U.S.A. 100:38-43(2003). RN [37] RP REVIEW ON MLD-SAPB VARIANTS. RX PubMed=7866401; DOI=10.1002/humu.1380040402; RA Gieselmann V., Zlotogora J., Harris A., Wenger D.A., Morris C.P.; RT "Molecular genetics of metachromatic leukodystrophy."; RL Hum. Mutat. 4:233-242(1994). RN [38] RP VARIANT MLD-SAPB ILE-217. RX PubMed=2302219; DOI=10.1016/0006-291X(90)90912-7; RA Rafi M.A., Zhang X.-L., Degala G., Wenger D.A.; RT "Detection of a point mutation in sphingolipid activator protein-1 RT mRNA in patients with a variant form of metachromatic RT leukodystrophy."; RL Biochem. Biophys. Res. Commun. 166:1017-1023(1990). RN [39] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MLD-SAPB ILE-217. RX PubMed=2320574; DOI=10.1073/pnas.87.7.2541; RA Kretz K.A., Carson G.S., Morimoto S., Kishimoto Y., Fluharty A.L., RA O'Brien J.S.; RT "Characterization of a mutation in a family with saposin B deficiency: RT a glycosylation site defect."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2541-2544(1990). RN [40] RP VARIANT MLD-SAPB SER-241, NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE RP SPLICING. RX PubMed=2019586; RA Holtschmidt H., Sandhoff K., Kwon H.Y., Harzer K., Nakano T., RA Suzuki K.; RT "Sulfatide activator protein. Alternative splicing that generates RT three mRNAs and a newly found mutation responsible for a clinical RT disease."; RL J. Biol. Chem. 266:7556-7560(1991). RN [41] RP INVOLVEMENT IN CSAPD. RX PubMed=1371116; RA Schnabel D., Schroder M., Furst W., Klein A., Hurwitz R., Zenk T., RA Weber J., Harzer K., Paton B.C., Poulos A., Suzuki K., Sandhoff K.; RT "Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is RT caused by a mutation in the initiation codon of their common gene."; RL J. Biol. Chem. 267:3312-3315(1992). RN [42] RP VARIANT AGD PHE-388. RX PubMed=2060627; DOI=10.1016/0014-5793(91)80760-Z; RA Schnabel D., Schroeder M., Sandhoff K.; RT "Mutation in the sphingolipid activator protein 2 in a patient with a RT variant of Gaucher disease."; RL FEBS Lett. 284:57-59(1991). RN [43] RP VARIANT MLD-SAPB LYS-215. RX PubMed=10196694; DOI=10.1038/sj.ejhg.5200266; RA Regis S., Filocamo M., Corsolini F., Caroli F., Keulemans J.L.M., RA van Diggelen O.P., Gatti R.; RT "An Asn > Lys substitution in saposin B involving a conserved amino RT acidic residue and leading to the loss of the single N-glycosylation RT site in a patient with metachromatic leukodystrophy and normal RT arylsulphatase A activity."; RL Eur. J. Hum. Genet. 7:125-130(1999). RN [44] RP VARIANT MLD-SAPB HIS-215, AND CHARACTERIZATION OF VARIANT MLD-SAPB RP HIS-215. RX PubMed=10682309; DOI=10.1023/A:1005603014401; RA Wrobe D., Henseler M., Huettler S., Pascual Pascual S.I., Chabas A., RA Sandhoff K.; RT "A non-glycosylated and functionally deficient mutant (N215H) of the RT sphingolipid activator protein B (SAP-B) in a novel case of RT metachromatic leukodystrophy (MLD)."; RL J. Inherit. Metab. Dis. 23:63-76(2000). RN [45] RP INVOLVEMENT IN CSAPD. RX PubMed=11309366; DOI=10.1093/hmg/10.9.927; RA Hulkova H., Cervenkova M., Ledvinova J., Tochackova M., Hrebicek M., RA Poupetova H., Befekadu A., Berna L., Paton B.C., Harzer K., Boor A., RA Smid F., Elleder M.; RT "A novel mutation in the coding region of the prosaposin gene leads to RT a complete deficiency of prosaposin and saposins, and is associated RT with a complex sphingolipidosis dominated by lactosylceramide RT accumulation."; RL Hum. Mol. Genet. 10:927-940(2001). RN [46] RP VARIANT AKRD VAL-70 DEL. RX PubMed=15773042; DOI=10.1016/j.ymgme.2004.10.004; RA Spiegel R., Bach G., Sury V., Mengistu G., Meidan B., Shalev S., RA Shneor Y., Mandel H., Zeigler M.; RT "A mutation in the saposin A coding region of the prosaposin gene in RT an infant presenting as Krabbe disease: first report of saposin A RT deficiency in humans."; RL Mol. Genet. Metab. 84:160-166(2005). RN [47] RP VARIANT AGD PRO-349. RX PubMed=17919309; DOI=10.1111/j.1399-0004.2007.00899.x; RA Tylki-Szymanska A., Czartoryska B., Vanier M.T., Poorthuis B.J., RA Groener J.A., Lugowska A., Millat G., Vaccaro A.M., Jurkiewicz E.; RT "Non-neuronopathic Gaucher disease due to saposin C deficiency."; RL Clin. Genet. 72:538-542(2007). CC -!- FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of CC glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and CC galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). CC Saposin-C apparently acts by combining with the enzyme and acidic CC lipid to form an activated complex, rather than by solubilizing CC the substrate. CC -!- FUNCTION: Saposin-B stimulates the hydrolysis of galacto- CC cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 CC gangliosides by beta-galactosidase (EC 3.2.1.23) and CC globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). CC Saposin-B forms a solubilizing complex with the substrates of the CC sphingolipid hydrolases. CC -!- FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase CC activator (EC 3.1.4.12). CC -!- FUNCTION: Prosaposin: Behaves as a myelinotrophic and neurotrophic CC factor, these effects are mediated by its G-protein-coupled CC receptors, GPR37 and GPR37L1, undergoing ligand-mediated CC internalization followed by ERK phosphorylation signaling. CC {ECO:0000250|UniProtKB:Q61207, ECO:0000269|PubMed:10383054}. CC -!- FUNCTION: Saposins are specific low-molecular mass non-enzymic CC proteins, they participate in the lysosomal degradation of CC sphingolipids, which takes place by the sequential action of CC specific hydrolases. CC -!- SUBUNIT: Saposin-B is a homodimer. Prosaposin exists as a roughly CC half-half mixture of monomers and disulfide-linked dimers. CC Monomeric prosaposin interacts (via C-terminus) with CC sortilin/SORT1, the interaction is required for targeting to CC lysosomes. {ECO:0000269|PubMed:10406958, CC ECO:0000269|PubMed:12510003, ECO:0000269|PubMed:14657016, CC ECO:0000269|PubMed:21835174, ECO:0000269|PubMed:7730378}. CC -!- INTERACTION: CC P31944:CASP14; NbExp=3; IntAct=EBI-716699, EBI-2510738; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14657016, CC ECO:0000269|PubMed:21835174}. CC -!- SUBCELLULAR LOCATION: Prosaposin: Secreted. Note=Secreted as a CC fully glycosylated 70 kDa protein composed of complex glycans. CC {ECO:0000250|UniProtKB:Q61207}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=Sap-mu-0; CC IsoId=P07602-1; Sequence=Displayed; CC Name=Sap-mu-6; CC IsoId=P07602-2; Sequence=VSP_006014; CC Name=Sap-mu-9; CC IsoId=P07602-3; Sequence=VSP_006015; CC -!- PTM: The lysosomal precursor is proteolytically processed to 4 CC small peptides, which are similar to each other and are CC sphingolipid hydrolase activator proteins. CC -!- PTM: N-linked glycans show a high degree of microheterogeneity. CC {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329}. CC -!- PTM: The one residue extended Saposin-B-Val is only found in 5% of CC the chains. CC -!- DISEASE: Combined saposin deficiency (CSAPD) [MIM:611721]: Due to CC absence of all saposins, leading to a fatal storage disorder with CC hepatosplenomegaly and severe neurological involvement. CC {ECO:0000269|PubMed:11309366, ECO:0000269|PubMed:1371116}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Leukodystrophy metachromatic due to saposin-B deficiency CC (MLD-SAPB) [MIM:249900]: An atypical form of metachromatic CC leukodystrophy. It is characterized by tissue accumulation of CC cerebroside-3-sulfate, demyelination, periventricular white matter CC abnormalities, peripheral neuropathy. Additional neurological CC features include dysarthria, ataxic gait, psychomotor regression, CC seizures, cognitive decline and spastic quadriparesis. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Gaucher disease, atypical, due to saposin C deficiency CC (AGD) [MIM:610539]: A disease characterized by marked CC glucosylceramide accumulation in the spleen without having a CC deficiency of glucosylceramide-beta glucosidase characteristic of CC classic Gaucher disease. Gaucher disease is a lysosomal storage CC disorder characterized by skeletal deterioration, CC hepatosplenomegaly, and organ dysfunction. There are several CC subtypes based on the presence and severity of neurological CC involvement. {ECO:0000269|PubMed:17919309, CC ECO:0000269|PubMed:2060627}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Krabbe disease, atypical, due to saposin A deficiency CC (AKRD) [MIM:611722]: A disorder of galactosylceramide metabolism. CC Clinical features include neurologic regression around age 3 CC months, loss of spontaneous movements, hyporeflexia, generalized CC brain atrophy, and diffuse white matter dysmyelination. CC {ECO:0000269|PubMed:15773042}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Note=Defects in PSAP saposin-D region are found in a CC variant of Tay-Sachs disease (GM2-gangliosidosis). CC -!- MISCELLANEOUS: Saposin-B co-purifies with 1 molecule of CC phosphatidylethanolamine. CC -!- SIMILARITY: Contains 2 saposin A-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00414}. CC -!- SIMILARITY: Contains 4 saposin B-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00415}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PSAPID42980ch10q22.html"; 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; J03077; AAA52560.1; -; mRNA. DR EMBL; D00422; BAA00321.1; -; mRNA. DR EMBL; BT006849; AAP35495.1; -; mRNA. DR EMBL; CR456746; CAG33027.1; -; mRNA. DR EMBL; AL731541; CAI40837.1; -; Genomic_DNA. DR EMBL; AC073370; CAI40837.1; JOINED; Genomic_DNA. DR EMBL; CH471083; EAW54437.1; -; Genomic_DNA. DR EMBL; BC001503; AAH01503.1; -; mRNA. DR EMBL; BC004275; AAH04275.1; -; mRNA. DR EMBL; BC007612; AAH07612.1; -; mRNA. DR EMBL; M86181; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X57107; CAA40391.1; -; Genomic_DNA. DR EMBL; X57108; CAA40392.1; -; Genomic_DNA. DR EMBL; M12710; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; J03015; AAB59494.1; -; mRNA. DR EMBL; M32221; AAA60303.1; -; mRNA. DR EMBL; M60257; AAA36595.1; -; mRNA. DR EMBL; M60258; AAA36596.1; -; mRNA. DR EMBL; M60255; AAA36594.1; -; mRNA. DR CCDS; CCDS7311.1; -. [P07602-1] DR PIR; JX0061; SAHUP. DR RefSeq; NP_001035930.1; NM_001042465.1. [P07602-3] DR RefSeq; NP_001035931.1; NM_001042466.1. [P07602-2] DR RefSeq; NP_002769.1; NM_002778.2. [P07602-1] DR UniGene; Hs.523004; -. DR PDB; 1M12; NMR; -; A=311-390. DR PDB; 1N69; X-ray; 2.20 A; A/B/C=195-273. DR PDB; 1SN6; NMR; -; A=311-390. DR PDB; 2DOB; X-ray; 2.00 A; A=60-140. DR PDB; 2GTG; X-ray; 2.40 A; A=311-391. DR PDB; 2QYP; X-ray; 2.45 A; A/B=311-392. DR PDB; 2R0R; X-ray; 2.50 A; A/B=407-484. DR PDB; 2R1Q; X-ray; 2.50 A; A=407-484. DR PDB; 2RB3; X-ray; 2.10 A; A/B/C/D=407-484. DR PDB; 2Z9A; X-ray; 2.50 A; A/B=311-389. DR PDB; 3BQP; X-ray; 1.30 A; A/B=405-484. DR PDB; 3BQQ; X-ray; 2.00 A; A/B/C/D=405-484. DR PDB; 4DDJ; X-ray; 1.90 A; A=60-140. DR PDB; 4UEX; X-ray; 1.80 A; A/B=60-142. DR PDBsum; 1M12; -. DR PDBsum; 1N69; -. DR PDBsum; 1SN6; -. DR PDBsum; 2DOB; -. DR PDBsum; 2GTG; -. DR PDBsum; 2QYP; -. DR PDBsum; 2R0R; -. DR PDBsum; 2R1Q; -. DR PDBsum; 2RB3; -. DR PDBsum; 2Z9A; -. DR PDBsum; 3BQP; -. DR PDBsum; 3BQQ; -. DR PDBsum; 4DDJ; -. DR PDBsum; 4UEX; -. DR DisProt; DP00733; -. DR ProteinModelPortal; P07602; -. DR SMR; P07602; 60-139, 195-272, 312-484. DR BioGrid; 111639; 41. DR DIP; DIP-29803N; -. DR IntAct; P07602; 17. DR MINT; MINT-1193270; -. DR STRING; 9606.ENSP00000378394; -. DR TCDB; 1.C.35.2.1; the amoebapore (amoebapore) family. DR PhosphoSite; P07602; -. DR UniCarbKB; P07602; -. DR BioMuta; PSAP; -. DR DMDM; 134218; -. DR PaxDb; P07602; -. DR PRIDE; P07602; -. DR DNASU; 5660; -. DR Ensembl; ENST00000394936; ENSP00000378394; ENSG00000197746. [P07602-1] DR GeneID; 5660; -. DR KEGG; hsa:5660; -. DR UCSC; uc001jsm.3; human. [P07602-1] DR CTD; 5660; -. DR GeneCards; PSAP; -. DR HGNC; HGNC:9498; PSAP. DR HPA; CAB004647; -. DR HPA; HPA004426; -. DR HPA; HPA052900; -. DR MalaCards; PSAP; -. DR MIM; 176801; gene. DR MIM; 249900; phenotype. DR MIM; 610539; phenotype. DR MIM; 611721; phenotype. DR MIM; 611722; phenotype. DR neXtProt; NX_P07602; -. DR Orphanet; 309252; Atypical Gaucher disease due to saposin C deficiency. DR Orphanet; 139406; Encephalopathy due to prosaposin deficiency. DR Orphanet; 206436; Infantile Krabbe disease. DR Orphanet; 309271; Metachromatic leukodystrophy, adult form. DR Orphanet; 309263; Metachromatic leukodystrophy, juvenile form. DR Orphanet; 309256; Metachromatic leukodystrophy, late infantile form. DR PharmGKB; PA33845; -. DR eggNOG; KOG1340; Eukaryota. DR eggNOG; ENOG410XSI5; LUCA. DR GeneTree; ENSGT00530000063434; -. DR HOVERGEN; HBG002617; -. DR InParanoid; P07602; -. DR KO; K12382; -. DR OrthoDB; EOG7ZSHSC; -. DR PhylomeDB; P07602; -. DR TreeFam; TF316942; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR ChiTaRS; PSAP; human. DR EvolutionaryTrace; P07602; -. DR GeneWiki; Prosaposin; -. DR GenomeRNAi; 5660; -. DR NextBio; 21992; -. DR PRO; PR:P07602; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; P07602; -. DR CleanEx; HS_PSAP; -. DR ExpressionAtlas; P07602; baseline and differential. DR Genevisible; P07602; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc. DR GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central. DR GO; GO:0008289; F:lipid binding; TAS:ProtInc. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl. DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IBA:GO_Central. DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome. DR GO; GO:0006869; P:lipid transport; TAS:ProtInc. DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEA:Ensembl. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0043085; P:positive regulation of catalytic activity; TAS:GOC. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0060736; P:prostate gland growth; IBA:GO_Central. DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006665; P:sphingolipid metabolic process; TAS:Reactome. DR Gene3D; 1.10.225.10; -; 4. DR InterPro; IPR003119; SAP_A. DR InterPro; IPR007856; SapB_1. DR InterPro; IPR008138; SapB_2. DR InterPro; IPR008373; Saposin. DR InterPro; IPR011001; Saposin-like. DR InterPro; IPR021165; Saposin_chordata. DR InterPro; IPR008139; SaposinB_dom. DR Pfam; PF02199; SapA; 2. DR Pfam; PF05184; SapB_1; 4. DR Pfam; PF03489; SapB_2; 4. DR PIRSF; PIRSF002431; Saposin; 1. DR PRINTS; PR01797; SAPOSIN. DR SMART; SM00162; SAPA; 2. DR SMART; SM00741; SapB; 4. DR SUPFAM; SSF47862; SSF47862; 4. DR PROSITE; PS51110; SAP_A; 2. DR PROSITE; PS50015; SAP_B; 4. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Gangliosidosis; Gaucher disease; Glycoprotein; Leukodystrophy; KW Lipid metabolism; Lysosome; Metachromatic leukodystrophy; KW Reference proteome; Repeat; Secreted; Signal; Sphingolipid metabolism. FT SIGNAL 1 16 {ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:1958198, FT ECO:0000269|PubMed:8323276}. FT CHAIN 17 524 Prosaposin. {ECO:0000269|PubMed:8323276}. FT /FTId=PRO_0000424774. FT PROPEP 17 59 {ECO:0000305}. FT /FTId=PRO_0000031616. FT CHAIN 60 142 Saposin-A. {ECO:0000269|PubMed:2717620}. FT /FTId=PRO_0000031617. FT PROPEP 143 194 {ECO:0000305}. FT /FTId=PRO_0000031618. FT CHAIN 195 274 Saposin-B-Val. FT {ECO:0000269|PubMed:2209618, FT ECO:0000269|PubMed:3242555}. FT /FTId=PRO_0000031619. FT CHAIN 195 273 Saposin-B. {ECO:0000269|PubMed:2209618}. FT /FTId=PRO_0000031620. FT PROPEP 275 310 {ECO:0000305}. FT /FTId=PRO_0000031621. FT CHAIN 311 390 Saposin-C. {ECO:0000269|PubMed:3442600}. FT /FTId=PRO_0000031622. FT PROPEP 393 404 {ECO:0000305}. FT /FTId=PRO_0000031623. FT CHAIN 405 486 Saposin-D. {ECO:0000269|PubMed:2845979}. FT /FTId=PRO_0000031624. FT PROPEP 487 524 {ECO:0000305}. FT /FTId=PRO_0000031625. FT DOMAIN 18 58 Saposin A-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00414}. FT DOMAIN 59 142 Saposin B-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00415}. FT DOMAIN 194 275 Saposin B-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00415}. FT DOMAIN 311 392 Saposin B-type 3. {ECO:0000255|PROSITE- FT ProRule:PRU00415}. FT DOMAIN 405 486 Saposin B-type 4. {ECO:0000255|PROSITE- FT ProRule:PRU00415}. FT DOMAIN 488 524 Saposin A-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00414}. FT SITE 215 215 Not glycosylated; in variant MLD-SAPB FT Ile-217. FT CARBOHYD 80 80 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19167329, FT ECO:0000269|PubMed:2842863}. FT CARBOHYD 101 101 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19167329, FT ECO:0000269|PubMed:2842863}. FT CARBOHYD 215 215 N-linked (GlcNAc...) (complex). FT {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:19167329}. FT /FTId=CAR_000176. FT CARBOHYD 332 332 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19167329}. FT CARBOHYD 426 426 N-linked (GlcNAc...). FT {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19167329}. FT DISULFID 63 138 {ECO:0000305|PubMed:2717620}. FT DISULFID 66 132 {ECO:0000305|PubMed:2717620}. FT DISULFID 94 106 {ECO:0000305|PubMed:2717620}. FT DISULFID 198 271 {ECO:0000269|PubMed:12510003}. FT DISULFID 201 265 {ECO:0000269|PubMed:12510003}. FT DISULFID 230 241 {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:7730378}. FT DISULFID 315 388 {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:7730378}. FT DISULFID 318 382 {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:7730378}. FT DISULFID 346 357 {ECO:0000255|PROSITE-ProRule:PRU00415, FT ECO:0000269|PubMed:7730378}. FT DISULFID 409 482 {ECO:0000269|PubMed:10406958}. FT DISULFID 412 476 {ECO:0000269|PubMed:10406958}. FT DISULFID 440 451 {ECO:0000269|PubMed:10406958}. FT VAR_SEQ 259 259 M -> MDQ (in isoform Sap-mu-6). FT {ECO:0000305}. FT /FTId=VSP_006014. FT VAR_SEQ 260 260 Q -> QDQQ (in isoform Sap-mu-9). FT {ECO:0000305}. FT /FTId=VSP_006015. FT VARIANT 70 70 Missing (in AKRD). FT {ECO:0000269|PubMed:15773042}. FT /FTId=VAR_042440. FT VARIANT 215 215 N -> H (in MLD-SAPB; reduces the FT intracellular activity of the protein FT significantly). FT {ECO:0000269|PubMed:10682309}. FT /FTId=VAR_031823. FT VARIANT 215 215 N -> K (in MLD-SAPB). FT {ECO:0000269|PubMed:10196694}. FT /FTId=VAR_031899. FT VARIANT 217 217 T -> I (in MLD-SAPB; juvenile; affects FT glycosylation at N-215). FT {ECO:0000269|PubMed:2302219, FT ECO:0000269|PubMed:2320574}. FT /FTId=VAR_006943. FT VARIANT 241 241 C -> S (in MLD-SAPB; severe; FT dbSNP:rs1130793). FT {ECO:0000269|PubMed:2019586}. FT /FTId=VAR_006944. FT VARIANT 349 349 L -> P (in AGD). FT {ECO:0000269|PubMed:17919309}. FT /FTId=VAR_042441. FT VARIANT 388 388 C -> F (in AGD). FT {ECO:0000269|PubMed:2060627}. FT /FTId=VAR_006945. FT MUTAGEN 240 240 I->C: Strongly decreases stimulation of FT cerebroside sulfate hydrolysis. FT {ECO:0000269|PubMed:12518053}. FT CONFLICT 369 369 L -> P (in Ref. 4; CAG33027). FT {ECO:0000305}. FT HELIX 61 78 {ECO:0000244|PDB:4UEX}. FT HELIX 83 96 {ECO:0000244|PDB:4UEX}. FT STRAND 97 99 {ECO:0000244|PDB:4UEX}. FT HELIX 100 122 {ECO:0000244|PDB:4UEX}. FT HELIX 128 134 {ECO:0000244|PDB:4UEX}. FT HELIX 196 214 {ECO:0000244|PDB:1N69}. FT HELIX 218 229 {ECO:0000244|PDB:1N69}. FT HELIX 230 233 {ECO:0000244|PDB:1N69}. FT HELIX 237 256 {ECO:0000244|PDB:1N69}. FT HELIX 261 267 {ECO:0000244|PDB:1N69}. FT HELIX 314 330 {ECO:0000244|PDB:2GTG}. FT HELIX 335 345 {ECO:0000244|PDB:2GTG}. FT HELIX 346 348 {ECO:0000244|PDB:1M12}. FT HELIX 351 373 {ECO:0000244|PDB:2GTG}. FT HELIX 378 384 {ECO:0000244|PDB:2GTG}. FT TURN 386 388 {ECO:0000244|PDB:1SN6}. FT HELIX 409 422 {ECO:0000244|PDB:3BQP}. FT HELIX 429 439 {ECO:0000244|PDB:3BQP}. FT HELIX 440 442 {ECO:0000244|PDB:3BQP}. FT HELIX 445 447 {ECO:0000244|PDB:3BQP}. FT HELIX 448 466 {ECO:0000244|PDB:3BQP}. FT HELIX 472 478 {ECO:0000244|PDB:3BQP}. SQ SEQUENCE 524 AA; 58113 MW; 71977F7A8C9E1533 CRC64; MYALFLLASL LGAALAGPVL GLKECTRGSA VWCQNVKTAS DCGAVKHCLQ TVWNKPTVKS LPCDICKDVV TAAGDMLKDN ATEEEILVYL EKTCDWLPKP NMSASCKEIV DSYLPVILDI IKGEMSRPGE VCSALNLCES LQKHLAELNH QKQLESNKIP ELDMTEVVAP FMANIPLLLY PQDGPRSKPQ PKDNGDVCQD CIQMVTDIQT AVRTNSTFVQ ALVEHVKEEC DRLGPGMADI CKNYISQYSE IAIQMMMHMQ PKEICALVGF CDEVKEMPMQ TLVPAKVASK NVIPALELVE PIKKHEVPAK SDVYCEVCEF LVKEVTKLID NNKTEKEILD AFDKMCSKLP KSLSEECQEV VDTYGSSILS ILLEEVSPEL VCSMLHLCSG TRLPALTVHV TQPKDGGFCE VCKKLVGYLD RNLEKNSTKQ EILAALEKGC SFLPDPYQKQ CDQFVAEYEP VLIEILVEVM DPSFVCLKIG ACPSAHKPLL GTEKCIWGPS YWCQNTETAA QCNAVEHCKR HVWN //