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Database: UniProt
Entry: P07602
LinkDB: P07602
Original site: P07602 
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   26-NOV-2014, entry version 189.
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; 165-172; 180-189 AND 298-302.
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   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   [35]
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   [36]
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   [37]
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   [38]
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   [39]
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   [40]
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   [41]
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   [42]
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   [43]
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   [44]
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   [45]
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}.
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   -!- 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";
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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   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   DisProt; DP00733; -.
DR   ProteinModelPortal; P07602; -.
DR   SMR; P07602; 60-139, 195-272, 312-484.
DR   BioGrid; 111639; 43.
DR   DIP; DIP-29803N; -.
DR   IntAct; P07602; 13.
DR   MINT; MINT-1193270; -.
DR   TCDB; 1.C.35.2.1; the amoebapore (amoebapore) family.
DR   PhosphoSite; P07602; -.
DR   UniCarbKB; P07602; -.
DR   DMDM; 134218; -.
DR   MaxQB; P07602; -.
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; GC10M073576; -.
DR   HGNC; HGNC:9498; PSAP.
DR   HPA; CAB004647; -.
DR   HPA; HPA004426; -.
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; NOG269151; -.
DR   GeneTree; ENSGT00530000063434; -.
DR   HOVERGEN; HBG002617; -.
DR   InParanoid; P07602; -.
DR   KO; K12382; -.
DR   OrthoDB; EOG7ZSHSC; -.
DR   PhylomeDB; P07602; -.
DR   TreeFam; TF316942; -.
DR   Reactome; REACT_116105; Glycosphingolipid metabolism.
DR   Reactome; REACT_14819; 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   Bgee; P07602; -.
DR   CleanEx; HS_PSAP; -.
DR   ExpressionAtlas; P07602; baseline and differential.
DR   Genevestigator; P07602; -.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular vesicular exosome; 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:0008289; F:lipid binding; TAS:ProtInc.
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; IEA:Ensembl.
DR   GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR   GO; GO:0006869; P:lipid transport; TAS:ProtInc.
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:0060736; P:prostate gland growth; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
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; SapA.
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.
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:0000269|PubMed:1958198,
FT                                ECO:0000269|PubMed:8323276}.
FT   CHAIN        17    524       Prosaposin.
FT                                /FTId=PRO_0000424774.
FT   PROPEP       17     58
FT                                /FTId=PRO_0000031616.
FT   CHAIN        60    142       Saposin-A.
FT                                /FTId=PRO_0000031617.
FT   PROPEP      144    194
FT                                /FTId=PRO_0000031618.
FT   CHAIN       195    274       Saposin-B-Val.
FT                                /FTId=PRO_0000031619.
FT   CHAIN       195    273       Saposin-B.
FT                                /FTId=PRO_0000031620.
FT   PROPEP      276    309
FT                                /FTId=PRO_0000031621.
FT   CHAIN       311    391       Saposin-C.
FT                                /FTId=PRO_0000031622.
FT   PROPEP      393    403
FT                                /FTId=PRO_0000031623.
FT   CHAIN       405    486       Saposin-D.
FT                                /FTId=PRO_0000031624.
FT   PROPEP      488    524
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
FT   DISULFID     66    132
FT   DISULFID     94    106
FT   DISULFID    198    271
FT   DISULFID    201    265
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
FT   DISULFID    412    476
FT   DISULFID    440    451
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:4DDJ}.
FT   HELIX        82     94       {ECO:0000244|PDB:4DDJ}.
FT   STRAND       97     99       {ECO:0000244|PDB:2DOB}.
FT   HELIX       101    125       {ECO:0000244|PDB:4DDJ}.
FT   HELIX       128    134       {ECO:0000244|PDB:4DDJ}.
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
//
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