Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Prosaposin (Proactivator polypeptide) [Cleaved into: Saposin-A (Protein A); Saposin-B-Val; Saposin-B (Cerebroside sulfate activator) (CSAct) (Dispersin) (Sphingolipid activator protein 1) (SAP-1) (Sulfatide/GM1 activator); Saposin-C (A1 activator) (Co-beta-glucosidase) (Glucosylceramidase activator) (Sphingolipid activator protein 2) (SAP-2); Saposin-D (Component C) (Protein C)]

 SAP_HUMAN               Reviewed;         524 AA.
P07602; P07292; P15793; P78538; P78541; P78546; P78547; P78558;
Q53Y86; Q6IBQ6; Q92739; Q92740; Q92741; Q92742;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 2.
10-OCT-2018, entry version 227.
RecName: Full=Prosaposin;
AltName: Full=Proactivator polypeptide;
Contains:
RecName: Full=Saposin-A;
AltName: Full=Protein A;
Contains:
RecName: Full=Saposin-B-Val;
Contains:
RecName: Full=Saposin-B;
AltName: Full=Cerebroside sulfate activator;
Short=CSAct;
AltName: Full=Dispersin;
AltName: Full=Sphingolipid activator protein 1;
Short=SAP-1;
AltName: Full=Sulfatide/GM1 activator;
Contains:
RecName: Full=Saposin-C;
AltName: Full=A1 activator;
AltName: Full=Co-beta-glucosidase;
AltName: Full=Glucosylceramidase activator;
AltName: Full=Sphingolipid activator protein 2;
Short=SAP-2;
Contains:
RecName: Full=Saposin-D;
AltName: Full=Component C;
AltName: Full=Protein C;
Flags: Precursor;
Name=PSAP; Synonyms=GLBA, SAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2515150; DOI=10.1016/0888-7543(89)90014-1;
Rorman E.G., Grabowski G.A.;
"Molecular cloning of a human co-beta-glucosidase cDNA: evidence that
four sphingolipid hydrolase activator proteins are encoded by single
genes in humans and rats.";
Genomics 5:486-492(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2498298;
Nakano T., Sandhoff K., Stuemper J., Christomanou H., Suzuki K.;
"Structure of full-length cDNA coding for sulfatide activator, a Co-
beta-glucosidase and two other homologous proteins: two alternate
forms of the sulfatide activator.";
J. Biochem. 105:152-154(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SAP-MU-0).
TISSUE=Brain, Eye, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-524.
PubMed=2842863; DOI=10.1126/science.2842863;
O'Brien J.S., Kretz K.A., Dewji N., Wenger D.A., Esch F.,
Fluharty A.L.;
"Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by
same genetic locus.";
Science 241:1098-1101(1988).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-524.
PubMed=1612590; DOI=10.1016/0888-7543(92)90247-P;
Rorman E.G., Scheinker V., Grabowski G.A.;
"Structure and evolution of the human prosaposin chromosomal gene.";
Genomics 13:312-318(1992).
[10]
PROTEIN SEQUENCE OF 17-24 AND 165-172.
PubMed=8323276; DOI=10.1006/abbi.1993.1328;
Hiraiwa M., O'Brien J.S., Kishimoto Y., Galdzicka M., Fluharty A.L.,
Ginns E.I., Martin B.M.;
"Isolation, characterization, and proteolysis of human prosaposin, the
precursor of saposins (sphingolipid activator proteins).";
Arch. Biochem. Biophys. 304:110-116(1993).
[11]
PROTEIN SEQUENCE OF 17-26.
TISSUE=Milk;
PubMed=1958198; DOI=10.1016/S0006-291X(05)81415-9;
Kondoh K., Hineno T., Sano A., Kakimoto Y.;
"Isolation and characterization of prosaposin from human milk.";
Biochem. Biophys. Res. Commun. 181:286-292(1991).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-125 AND 304-513.
TISSUE=Brain;
PubMed=2013321; DOI=10.1016/0014-5793(91)80308-P;
Holtschmidt H., Sandhoff K., Fuerst W., Kwon H.Y., Schnabel D.,
Suzuki K.;
"The organization of the gene for the human cerebroside sulfate
activator protein.";
FEBS Lett. 280:267-270(1991).
[13]
PROTEIN SEQUENCE OF 60-142.
PubMed=2717620; DOI=10.1073/pnas.86.9.3389;
Morimoto S., Martin B.M., Yamamoto Y., Kretz K.A., O'Brien J.S.,
Kishimoto Y.;
"Saposin A: second cerebrosidase activator protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:3389-3393(1989).
[14]
PROTEIN SEQUENCE OF 62-84 AND 410-431.
PubMed=8370464; DOI=10.1016/0014-5793(93)80908-D;
Tyynela J., Palmer D.N., Baumann M., Haltia M.;
"Storage of saposins A and D in infantile neuronal ceroid-
lipofuscinosis.";
FEBS Lett. 330:8-12(1993).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 164-524.
PubMed=2825202; DOI=10.1073/pnas.84.23.8652;
Dewji N.N., Wenger D.A., O'Brien J.S.;
"Nucleotide sequence of cloned cDNA for human sphingolipid activator
protein 1 precursor.";
Proc. Natl. Acad. Sci. U.S.A. 84:8652-8656(1987).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 195-263.
PubMed=2868718; DOI=10.1016/S0006-291X(86)80518-6;
Dewji N.N., Wenger D.A., Fujibayashi S., Donoviel M., Esch F.,
Hill F., O'Brien J.S.;
"Molecular cloning of the sphingolipid activator protein-1 (SAP-1),
the sulfatide sulfatase activator.";
Biochem. Biophys. Res. Commun. 134:989-994(1986).
[17]
PROTEIN SEQUENCE OF 195-274.
PubMed=3242555;
Kleinschmidt T., Christomanou H., Braunitzer G.;
"Complete amino-acid sequence of the naturally occurring A2 activator
protein for enzymic sphingomyelin degradation: identity to the
sulfatide activator protein (SAP-1).";
Biol. Chem. Hoppe-Seyler 369:1361-1365(1988).
[18]
PROTEIN SEQUENCE OF 195-274.
TISSUE=Kidney;
PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x;
Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.;
"The complete amino-acid sequences of human ganglioside GM2 activator
protein and cerebroside sulfate activator protein.";
Eur. J. Biochem. 192:709-714(1990).
[19]
PROTEIN SEQUENCE OF 311-390.
PubMed=3442600;
Kleinschmidt T., Christomanou H., Braunitzer G.;
"Complete amino-acid sequence and carbohydrate content of the
naturally occurring glucosylceramide activator protein (A1 activator)
absent from a new human Gaucher disease variant.";
Biol. Chem. Hoppe-Seyler 368:1571-1578(1987).
[20]
PROTEIN SEQUENCE OF 405-484.
PubMed=2845979; DOI=10.1016/S0006-291X(88)80855-6;
Morimoto S., Martin B.M., Kishimoto Y., O'Brien J.S.;
"Saposin D: a sphingomyelinase activator.";
Biochem. Biophys. Res. Commun. 156:403-410(1988).
[21]
PROTEIN SEQUENCE OF 407-484.
PubMed=3048308;
Furst W., Machleidt W., Sandhoff K.;
"The precursor of sulfatide activator protein is processed to three
different proteins.";
Biol. Chem. Hoppe-Seyler 369:317-328(1988).
[22]
PARTIAL PROTEIN SEQUENCE (SAPOSIN-B), AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Urine;
PubMed=10562467; DOI=10.1006/mgme.1999.2900;
Fluharty A.L., Lombardo C., Louis A., Stevens R.L., Whitelegge J.P.,
Waring A.J., To T., Fluharty C.B., Faull K.F.;
"Preparation of the cerebroside sulfate activator (CSAct or saposin B)
from human urine.";
Mol. Genet. Metab. 68:391-403(1999).
[23]
DISULFIDE BONDS IN SAPOSINS-B AND C, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7730378; DOI=10.1074/jbc.270.17.9953;
Vaccaro A.M., Salvioli R., Barca A., Tatti M., Ciaffoni F., Maras B.,
Siciliano R., Zappacosta F., Amoresano A., Pucci P.;
"Structural analysis of saposin C and B. Complete localization of
disulfide bridges.";
J. Biol. Chem. 270:9953-9960(1995).
[24]
FUNCTION.
PubMed=10383054;
DOI=10.1002/(SICI)1098-1136(199906)26:4<353::AID-GLIA9>3.3.CO;2-7;
Hiraiwa M., Campana W.M., Mizisin A.P., Mohiuddin L., O'Brien J.S.;
"Prosaposin: a myelinotrophic protein that promotes expression of
myelin constituents and is secreted after nerve injury.";
Glia 26:353-360(1999).
[25]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Urine;
PubMed=10510427;
DOI=10.1002/(SICI)1096-9888(199910)34:10<1040::AID-JMS863>3.0.CO;2-X;
Faull K.F., Whitelegge J.P., Higginson J., To T., Johnson J.,
Krutchinsky A.N., Standing K.G., Waring A.J., Stevens R.L.,
Fluharty C.B., Fluharty A.L.;
"Cerebroside sulfate activator protein (Saposin B): chromatographic
and electrospray mass spectrometric properties.";
J. Mass Spectrom. 34:1040-1054(1999).
[26]
GLYCOSYLATION AT ASN-215, AND STRUCTURE OF CARBOHYDRATE ON ASN-215.
PubMed=11180632;
DOI=10.1002/1096-9888(200012)35:12<1416::AID-JMS75>3.0.CO;2-K;
Faull K.F., Johnson J., Kim M.J., To T., Whitelegge J.P.,
Stevens R.L., Fluharty C.B., Fluharty A.L.;
"Structure of the asparagine-linked sugar chains of porcine kidney and
human urine cerebroside sulfate activator protein.";
J. Mass Spectrom. 35:1416-1424(2000).
[27]
DISULFIDE BONDS IN SAPOSIN-D.
PubMed=10406958; DOI=10.1046/j.1432-1327.1999.00521.x;
Tatti M., Salvioli R., Ciaffoni F., Pucci P., Andolfo A.,
Amoresano A., Vaccaro A.M.;
"Structural and membrane-binding properties of saposin D.";
Eur. J. Biochem. 263:486-494(1999).
[28]
SUBCELLULAR LOCATION, AND INTERACTION WITH SORT1.
PubMed=14657016; DOI=10.1093/emboj/cdg629;
Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.;
"The lysosomal trafficking of sphingolipid activator proteins (SAPs)
is mediated by sortilin.";
EMBO J. 22:6430-6437(2003).
[29]
DISULFIDE BONDS IN SAPOSIN-B.
PubMed=12510003; DOI=10.1016/S1046-5928(02)00597-1;
Ahn V.E., Faull K.F., Whitelegge J.P., Higginson J., Fluharty A.L.,
Prive G.G.;
"Expression, purification, crystallization, and preliminary X-ray
analysis of recombinant human saposin B.";
Protein Expr. Purif. 27:186-193(2003).
[30]
GLYCOSYLATION AT ASN-80; ASN-101; ASN-215; ASN-332 AND ASN-426.
PubMed=19167329; DOI=10.1016/j.cell.2008.11.047;
Ruiz-Canada C., Kelleher D.J., Gilmore R.;
"Cotranslational and posttranslational N-glycosylation of polypeptides
by distinct mammalian OST isoforms.";
Cell 136:272-283(2009).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80; ASN-101; ASN-332 AND
ASN-426.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=21835174; DOI=10.1016/j.yexcr.2011.07.017;
Yuan L., Morales C.R.;
"Prosaposin sorting is mediated by oligomerization.";
Exp. Cell Res. 317:2456-2467(2011).
[34]
INTERACTION WITH SORT1, AND SUBCELLULAR LOCATION.
PubMed=22431521; DOI=10.1128/MCB.06726-11;
Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
"The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in
endosomal sorting.";
Mol. Cell. Biol. 32:1855-1866(2012).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-16, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[37]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 195-273, AND MUTAGENESIS OF
ILE-240.
PubMed=12518053; DOI=10.1073/pnas.0136947100;
Ahn V.E., Faull K.F., Whitelegge J.P., Fluharty A.L., Prive G.G.;
"Crystal structure of saposin B reveals a dimeric shell for lipid
binding.";
Proc. Natl. Acad. Sci. U.S.A. 100:38-43(2003).
[38]
REVIEW ON MLD-SAPB VARIANTS.
PubMed=7866401; DOI=10.1002/humu.1380040402;
Gieselmann V., Zlotogora J., Harris A., Wenger D.A., Morris C.P.;
"Molecular genetics of metachromatic leukodystrophy.";
Hum. Mutat. 4:233-242(1994).
[39]
VARIANT MLD-SAPB ILE-217.
PubMed=2302219; DOI=10.1016/0006-291X(90)90912-7;
Rafi M.A., Zhang X.-L., Degala G., Wenger D.A.;
"Detection of a point mutation in sphingolipid activator protein-1
mRNA in patients with a variant form of metachromatic
leukodystrophy.";
Biochem. Biophys. Res. Commun. 166:1017-1023(1990).
[40]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MLD-SAPB ILE-217.
PubMed=2320574; DOI=10.1073/pnas.87.7.2541;
Kretz K.A., Carson G.S., Morimoto S., Kishimoto Y., Fluharty A.L.,
O'Brien J.S.;
"Characterization of a mutation in a family with saposin B deficiency:
a glycosylation site defect.";
Proc. Natl. Acad. Sci. U.S.A. 87:2541-2544(1990).
[41]
VARIANT MLD-SAPB SER-241, NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE
SPLICING.
PubMed=2019586;
Holtschmidt H., Sandhoff K., Kwon H.Y., Harzer K., Nakano T.,
Suzuki K.;
"Sulfatide activator protein. Alternative splicing that generates
three mRNAs and a newly found mutation responsible for a clinical
disease.";
J. Biol. Chem. 266:7556-7560(1991).
[42]
INVOLVEMENT IN CSAPD.
PubMed=1371116;
Schnabel D., Schroder M., Furst W., Klein A., Hurwitz R., Zenk T.,
Weber J., Harzer K., Paton B.C., Poulos A., Suzuki K., Sandhoff K.;
"Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is
caused by a mutation in the initiation codon of their common gene.";
J. Biol. Chem. 267:3312-3315(1992).
[43]
VARIANT AGD PHE-388.
PubMed=2060627; DOI=10.1016/0014-5793(91)80760-Z;
Schnabel D., Schroeder M., Sandhoff K.;
"Mutation in the sphingolipid activator protein 2 in a patient with a
variant of Gaucher disease.";
FEBS Lett. 284:57-59(1991).
[44]
VARIANT MLD-SAPB LYS-215.
PubMed=10196694; DOI=10.1038/sj.ejhg.5200266;
Regis S., Filocamo M., Corsolini F., Caroli F., Keulemans J.L.M.,
van Diggelen O.P., Gatti R.;
"An Asn > Lys substitution in saposin B involving a conserved amino
acidic residue and leading to the loss of the single N-glycosylation
site in a patient with metachromatic leukodystrophy and normal
arylsulphatase A activity.";
Eur. J. Hum. Genet. 7:125-130(1999).
[45]
VARIANT MLD-SAPB HIS-215, AND CHARACTERIZATION OF VARIANT MLD-SAPB
HIS-215.
PubMed=10682309; DOI=10.1023/A:1005603014401;
Wrobe D., Henseler M., Huettler S., Pascual Pascual S.I., Chabas A.,
Sandhoff K.;
"A non-glycosylated and functionally deficient mutant (N215H) of the
sphingolipid activator protein B (SAP-B) in a novel case of
metachromatic leukodystrophy (MLD).";
J. Inherit. Metab. Dis. 23:63-76(2000).
[46]
INVOLVEMENT IN CSAPD.
PubMed=11309366; DOI=10.1093/hmg/10.9.927;
Hulkova H., Cervenkova M., Ledvinova J., Tochackova M., Hrebicek M.,
Poupetova H., Befekadu A., Berna L., Paton B.C., Harzer K., Boor A.,
Smid F., Elleder M.;
"A novel mutation in the coding region of the prosaposin gene leads to
a complete deficiency of prosaposin and saposins, and is associated
with a complex sphingolipidosis dominated by lactosylceramide
accumulation.";
Hum. Mol. Genet. 10:927-940(2001).
[47]
VARIANT AKRD VAL-70 DEL.
PubMed=15773042; DOI=10.1016/j.ymgme.2004.10.004;
Spiegel R., Bach G., Sury V., Mengistu G., Meidan B., Shalev S.,
Shneor Y., Mandel H., Zeigler M.;
"A mutation in the saposin A coding region of the prosaposin gene in
an infant presenting as Krabbe disease: first report of saposin A
deficiency in humans.";
Mol. Genet. Metab. 84:160-166(2005).
[48]
VARIANT AGD PRO-349.
PubMed=17919309; DOI=10.1111/j.1399-0004.2007.00899.x;
Tylki-Szymanska A., Czartoryska B., Vanier M.T., Poorthuis B.J.,
Groener J.A., Lugowska A., Millat G., Vaccaro A.M., Jurkiewicz E.;
"Non-neuronopathic Gaucher disease due to saposin C deficiency.";
Clin. Genet. 72:538-542(2007).
-!- FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of
glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and
galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46).
Saposin-C apparently acts by combining with the enzyme and acidic
lipid to form an activated complex, rather than by solubilizing
the substrate.
-!- FUNCTION: Saposin-B stimulates the hydrolysis of galacto-
cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1
gangliosides by beta-galactosidase (EC 3.2.1.23) and
globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22).
Saposin-B forms a solubilizing complex with the substrates of the
sphingolipid hydrolases.
-!- FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase
activator (EC 3.1.4.12).
-!- FUNCTION: Prosaposin: Behaves as a myelinotrophic and neurotrophic
factor, these effects are mediated by its G-protein-coupled
receptors, GPR37 and GPR37L1, undergoing ligand-mediated
internalization followed by ERK phosphorylation signaling.
{ECO:0000250|UniProtKB:Q61207, ECO:0000269|PubMed:10383054}.
-!- FUNCTION: Saposins are specific low-molecular mass non-enzymic
proteins, they participate in the lysosomal degradation of
sphingolipids, which takes place by the sequential action of
specific hydrolases.
-!- SUBUNIT: Saposin-B is a homodimer. Prosaposin exists as a roughly
half-half mixture of monomers and disulfide-linked dimers
(PubMed:10406958, PubMed:12510003, PubMed:7730378,
PubMed:21835174). Monomeric prosaposin interacts (via C-terminus)
with sortilin/SORT1, the interaction is required for targeting to
lysosomes (PubMed:14657016, PubMed:22431521).
{ECO:0000269|PubMed:10406958, ECO:0000269|PubMed:12510003,
ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:21835174,
ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:7730378}.
-!- INTERACTION:
P31944:CASP14; NbExp=3; IntAct=EBI-716699, EBI-2510738;
P55072:VCP; NbExp=3; IntAct=EBI-10635648, EBI-355164;
O96006:ZBED1; NbExp=3; IntAct=EBI-716699, EBI-740037;
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14657016,
ECO:0000269|PubMed:21835174, ECO:0000269|PubMed:22431521}.
-!- SUBCELLULAR LOCATION: Prosaposin: Secreted
{ECO:0000250|UniProtKB:Q61207}. Note=Secreted as a fully
glycosylated 70 kDa protein composed of complex glycans.
{ECO:0000250|UniProtKB:Q61207}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=Sap-mu-0;
IsoId=P07602-1; Sequence=Displayed;
Name=Sap-mu-6;
IsoId=P07602-2; Sequence=VSP_006014;
Name=Sap-mu-9;
IsoId=P07602-3; Sequence=VSP_006015;
-!- PTM: The lysosomal precursor is proteolytically processed to 4
small peptides, which are similar to each other and are
sphingolipid hydrolase activator proteins.
-!- PTM: N-linked glycans show a high degree of microheterogeneity.
{ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329}.
-!- PTM: The one residue extended Saposin-B-Val is only found in 5% of
the chains.
-!- DISEASE: Combined saposin deficiency (CSAPD) [MIM:611721]: Due to
absence of all saposins, leading to a fatal storage disorder with
hepatosplenomegaly and severe neurological involvement.
{ECO:0000269|PubMed:11309366, ECO:0000269|PubMed:1371116}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Leukodystrophy metachromatic due to saposin-B deficiency
(MLD-SAPB) [MIM:249900]: An atypical form of metachromatic
leukodystrophy. It is characterized by tissue accumulation of
cerebroside-3-sulfate, demyelination, periventricular white matter
abnormalities, peripheral neuropathy. Additional neurological
features include dysarthria, ataxic gait, psychomotor regression,
seizures, cognitive decline and spastic quadriparesis.
{ECO:0000269|PubMed:10196694, ECO:0000269|PubMed:10682309,
ECO:0000269|PubMed:2019586, ECO:0000269|PubMed:2302219,
ECO:0000269|PubMed:2320574}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Gaucher disease, atypical, due to saposin C deficiency
(AGD) [MIM:610539]: A disease characterized by marked
glucosylceramide accumulation in the spleen without having a
deficiency of glucosylceramide-beta glucosidase characteristic of
classic Gaucher disease. Gaucher disease is a lysosomal storage
disorder characterized by skeletal deterioration,
hepatosplenomegaly, and organ dysfunction. There are several
subtypes based on the presence and severity of neurological
involvement. {ECO:0000269|PubMed:17919309,
ECO:0000269|PubMed:2060627}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Krabbe disease, atypical, due to saposin A deficiency
(AKRD) [MIM:611722]: A disorder of galactosylceramide metabolism.
Clinical features include neurologic regression around age 3
months, loss of spontaneous movements, hyporeflexia, generalized
brain atrophy, and diffuse white matter dysmyelination.
{ECO:0000269|PubMed:15773042}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in PSAP saposin-D region are found in a
variant of Tay-Sachs disease (GM2-gangliosidosis).
-!- MISCELLANEOUS: Saposin-B co-purifies with 1 molecule of
phosphatidylethanolamine.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PSAPID42980ch10q22.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J03077; AAA52560.1; -; mRNA.
EMBL; D00422; BAA00321.1; -; mRNA.
EMBL; BT006849; AAP35495.1; -; mRNA.
EMBL; CR456746; CAG33027.1; -; mRNA.
EMBL; AC073370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54437.1; -; Genomic_DNA.
EMBL; BC001503; AAH01503.1; -; mRNA.
EMBL; BC004275; AAH04275.1; -; mRNA.
EMBL; BC007612; AAH07612.1; -; mRNA.
EMBL; M86181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X57107; CAA40391.1; -; Genomic_DNA.
EMBL; X57108; CAA40392.1; -; Genomic_DNA.
EMBL; M12710; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; J03015; AAB59494.1; -; mRNA.
EMBL; M32221; AAA60303.1; -; mRNA.
EMBL; M60257; AAA36595.1; -; mRNA.
EMBL; M60258; AAA36596.1; -; mRNA.
EMBL; M60255; AAA36594.1; -; mRNA.
CCDS; CCDS7311.1; -. [P07602-1]
PIR; JX0061; SAHUP.
RefSeq; NP_001035930.1; NM_001042465.2. [P07602-3]
RefSeq; NP_001035931.1; NM_001042466.2. [P07602-2]
RefSeq; NP_002769.1; NM_002778.3. [P07602-1]
UniGene; Hs.523004; -.
PDB; 1M12; NMR; -; A=311-390.
PDB; 1N69; X-ray; 2.20 A; A/B/C=195-273.
PDB; 1SN6; NMR; -; A=311-390.
PDB; 2DOB; X-ray; 2.00 A; A=60-140.
PDB; 2GTG; X-ray; 2.40 A; A=311-391.
PDB; 2QYP; X-ray; 2.45 A; A/B=311-392.
PDB; 2R0R; X-ray; 2.50 A; A/B=407-484.
PDB; 2R1Q; X-ray; 2.50 A; A=407-484.
PDB; 2RB3; X-ray; 2.10 A; A/B/C/D=407-484.
PDB; 2Z9A; X-ray; 2.50 A; A/B=311-389.
PDB; 3BQP; X-ray; 1.30 A; A/B=405-484.
PDB; 3BQQ; X-ray; 2.00 A; A/B/C/D=405-484.
PDB; 4DDJ; X-ray; 1.90 A; A=60-140.
PDB; 4UEX; X-ray; 1.80 A; A/B=60-142.
PDB; 4V2O; X-ray; 2.13 A; A/B/C=195-273.
PDBsum; 1M12; -.
PDBsum; 1N69; -.
PDBsum; 1SN6; -.
PDBsum; 2DOB; -.
PDBsum; 2GTG; -.
PDBsum; 2QYP; -.
PDBsum; 2R0R; -.
PDBsum; 2R1Q; -.
PDBsum; 2RB3; -.
PDBsum; 2Z9A; -.
PDBsum; 3BQP; -.
PDBsum; 3BQQ; -.
PDBsum; 4DDJ; -.
PDBsum; 4UEX; -.
PDBsum; 4V2O; -.
DisProt; DP00733; -.
ProteinModelPortal; P07602; -.
SMR; P07602; -.
BioGrid; 111639; 44.
DIP; DIP-29803N; -.
IntAct; P07602; 23.
MINT; P07602; -.
STRING; 9606.ENSP00000378394; -.
ChEMBL; CHEMBL3580523; -.
DrugBank; DB01966; Di-Stearoyl-3-Sn-Phosphatidylethanolamine.
TCDB; 1.C.35.2.1; the amoebapore (amoebapore) family.
GlyConnect; 1645; -.
GlyConnect; 545; -.
GlyConnect; 546; -.
GlyConnect; 548; -.
GlyConnect; 549; -.
iPTMnet; P07602; -.
PhosphoSitePlus; P07602; -.
UniCarbKB; P07602; -.
BioMuta; PSAP; -.
DMDM; 134218; -.
EPD; P07602; -.
PaxDb; P07602; -.
PeptideAtlas; P07602; -.
PRIDE; P07602; -.
ProteomicsDB; 52019; -.
ProteomicsDB; 52020; -. [P07602-2]
ProteomicsDB; 52021; -. [P07602-3]
TopDownProteomics; P07602-1; -. [P07602-1]
DNASU; 5660; -.
Ensembl; ENST00000394936; ENSP00000378394; ENSG00000197746. [P07602-1]
GeneID; 5660; -.
KEGG; hsa:5660; -.
UCSC; uc001jsm.4; human. [P07602-1]
CTD; 5660; -.
DisGeNET; 5660; -.
EuPathDB; HostDB:ENSG00000197746.13; -.
GeneCards; PSAP; -.
HGNC; HGNC:9498; PSAP.
HPA; CAB004647; -.
HPA; HPA004426; -.
MalaCards; PSAP; -.
MIM; 176801; gene.
MIM; 249900; phenotype.
MIM; 610539; phenotype.
MIM; 611721; phenotype.
MIM; 611722; phenotype.
neXtProt; NX_P07602; -.
OpenTargets; ENSG00000197746; -.
Orphanet; 309252; Atypical Gaucher disease due to saposin C deficiency.
Orphanet; 139406; Encephalopathy due to prosaposin deficiency.
Orphanet; 206436; Infantile Krabbe disease.
Orphanet; 309271; Metachromatic leukodystrophy, adult form.
Orphanet; 309263; Metachromatic leukodystrophy, juvenile form.
Orphanet; 309256; Metachromatic leukodystrophy, late infantile form.
PharmGKB; PA33845; -.
eggNOG; KOG1340; Eukaryota.
eggNOG; ENOG410XSI5; LUCA.
GeneTree; ENSGT00530000063434; -.
HOVERGEN; HBG002617; -.
InParanoid; P07602; -.
KO; K12382; -.
PhylomeDB; P07602; -.
TreeFam; TF316942; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; PSAP; human.
EvolutionaryTrace; P07602; -.
GeneWiki; Prosaposin; -.
GenomeRNAi; 5660; -.
PRO; PR:P07602; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000197746; Expressed in 243 organ(s), highest expression level in visceral pleura.
CleanEx; HS_PSAP; -.
ExpressionAtlas; P07602; baseline and differential.
Genevisible; P07602; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004565; F:beta-galactosidase activity; IDA:CAFA.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:1905573; F:ganglioside GM1 binding; IDA:CAFA.
GO; GO:1905574; F:ganglioside GM2 binding; IDA:CAFA.
GO; GO:1905575; F:ganglioside GM3 binding; IDA:CAFA.
GO; GO:1905577; F:ganglioside GP1c binding; IDA:CAFA.
GO; GO:1905576; F:ganglioside GT1b binding; IDA:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; TAS:ProtInc.
GO; GO:0005543; F:phospholipid binding; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:1905572; P:ganglioside GM1 transport to membrane; IDA:CAFA.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:ProtInc.
GO; GO:0006869; P:lipid transport; TAS:ProtInc.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0060736; P:prostate gland growth; IBA:GO_Central.
GO; GO:0010506; P:regulation of autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
InterPro; IPR003119; SAP_A.
InterPro; IPR007856; SapB_1.
InterPro; IPR008138; SapB_2.
InterPro; IPR008373; Saposin.
InterPro; IPR011001; Saposin-like.
InterPro; IPR021165; Saposin_chordata.
InterPro; IPR008139; SaposinB_dom.
Pfam; PF02199; SapA; 2.
Pfam; PF05184; SapB_1; 4.
Pfam; PF03489; SapB_2; 4.
PIRSF; PIRSF002431; Saposin; 1.
PRINTS; PR01797; SAPOSIN.
SMART; SM00162; SAPA; 2.
SMART; SM00741; SapB; 4.
SUPFAM; SSF47862; SSF47862; 4.
PROSITE; PS51110; SAP_A; 2.
PROSITE; PS50015; SAP_B; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Gangliosidosis; Gaucher disease; Glycoprotein; Leukodystrophy;
Lipid metabolism; Lysosome; Metachromatic leukodystrophy;
Reference proteome; Repeat; Secreted; Signal; Sphingolipid metabolism.
SIGNAL 1 16 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:1958198,
ECO:0000269|PubMed:8323276}.
CHAIN 17 524 Prosaposin. {ECO:0000269|PubMed:8323276}.
/FTId=PRO_0000424774.
PROPEP 17 59 {ECO:0000305}.
/FTId=PRO_0000031616.
CHAIN 60 142 Saposin-A. {ECO:0000269|PubMed:2717620}.
/FTId=PRO_0000031617.
PROPEP 143 194 {ECO:0000305}.
/FTId=PRO_0000031618.
CHAIN 195 274 Saposin-B-Val.
{ECO:0000269|PubMed:2209618,
ECO:0000269|PubMed:3242555}.
/FTId=PRO_0000031619.
CHAIN 195 273 Saposin-B. {ECO:0000269|PubMed:2209618}.
/FTId=PRO_0000031620.
PROPEP 275 310 {ECO:0000305}.
/FTId=PRO_0000031621.
CHAIN 311 390 Saposin-C. {ECO:0000269|PubMed:3442600}.
/FTId=PRO_0000031622.
PROPEP 393 404 {ECO:0000305}.
/FTId=PRO_0000031623.
CHAIN 405 486 Saposin-D. {ECO:0000269|PubMed:2845979}.
/FTId=PRO_0000031624.
PROPEP 487 524 {ECO:0000305}.
/FTId=PRO_0000031625.
DOMAIN 18 58 Saposin A-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00414}.
DOMAIN 59 142 Saposin B-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00415}.
DOMAIN 194 275 Saposin B-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00415}.
DOMAIN 311 392 Saposin B-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00415}.
DOMAIN 405 486 Saposin B-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00415}.
DOMAIN 488 524 Saposin A-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00414}.
SITE 215 215 Not glycosylated; in variant MLD-SAPB
Ile-217.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:2842863}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19167329,
ECO:0000269|PubMed:2842863}.
CARBOHYD 215 215 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000255|PROSITE-
ProRule:PRU00415,
ECO:0000269|PubMed:11180632,
ECO:0000269|PubMed:19167329}.
/FTId=CAR_000176.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19167329}.
CARBOHYD 426 426 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19167329}.
DISULFID 63 138 {ECO:0000305|PubMed:2717620}.
DISULFID 66 132 {ECO:0000305|PubMed:2717620}.
DISULFID 94 106 {ECO:0000305|PubMed:2717620}.
DISULFID 198 271 {ECO:0000269|PubMed:12510003}.
DISULFID 201 265 {ECO:0000269|PubMed:12510003}.
DISULFID 230 241 {ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:7730378}.
DISULFID 315 388 {ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:7730378}.
DISULFID 318 382 {ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:7730378}.
DISULFID 346 357 {ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:7730378}.
DISULFID 409 482 {ECO:0000269|PubMed:10406958}.
DISULFID 412 476 {ECO:0000269|PubMed:10406958}.
DISULFID 440 451 {ECO:0000269|PubMed:10406958}.
VAR_SEQ 259 259 M -> MDQ (in isoform Sap-mu-6).
{ECO:0000305}.
/FTId=VSP_006014.
VAR_SEQ 260 260 Q -> QDQQ (in isoform Sap-mu-9).
{ECO:0000305}.
/FTId=VSP_006015.
VARIANT 70 70 Missing (in AKRD).
{ECO:0000269|PubMed:15773042}.
/FTId=VAR_042440.
VARIANT 215 215 N -> H (in MLD-SAPB; reduces the
intracellular activity of the protein
significantly; dbSNP:rs121918107).
{ECO:0000269|PubMed:10682309}.
/FTId=VAR_031823.
VARIANT 215 215 N -> K (in MLD-SAPB; dbSNP:rs770171865).
{ECO:0000269|PubMed:10196694}.
/FTId=VAR_031899.
VARIANT 217 217 T -> I (in MLD-SAPB; juvenile; affects
glycosylation at N-215;
dbSNP:rs121918103).
{ECO:0000269|PubMed:2302219,
ECO:0000269|PubMed:2320574}.
/FTId=VAR_006943.
VARIANT 241 241 C -> S (in MLD-SAPB; severe;
dbSNP:rs121918104).
{ECO:0000269|PubMed:2019586}.
/FTId=VAR_006944.
VARIANT 349 349 L -> P (in AGD; dbSNP:rs121918110).
{ECO:0000269|PubMed:17919309}.
/FTId=VAR_042441.
VARIANT 388 388 C -> F (in AGD).
{ECO:0000269|PubMed:2060627}.
/FTId=VAR_006945.
MUTAGEN 240 240 I->C: Strongly decreases stimulation of
cerebroside sulfate hydrolysis.
{ECO:0000269|PubMed:12518053}.
CONFLICT 369 369 L -> P (in Ref. 4; CAG33027).
{ECO:0000305}.
HELIX 61 78 {ECO:0000244|PDB:4UEX}.
HELIX 83 96 {ECO:0000244|PDB:4UEX}.
STRAND 97 99 {ECO:0000244|PDB:4UEX}.
HELIX 100 122 {ECO:0000244|PDB:4UEX}.
HELIX 128 134 {ECO:0000244|PDB:4UEX}.
HELIX 196 214 {ECO:0000244|PDB:4V2O}.
HELIX 218 229 {ECO:0000244|PDB:4V2O}.
HELIX 230 233 {ECO:0000244|PDB:4V2O}.
HELIX 237 257 {ECO:0000244|PDB:4V2O}.
HELIX 261 267 {ECO:0000244|PDB:4V2O}.
HELIX 314 330 {ECO:0000244|PDB:2GTG}.
HELIX 335 345 {ECO:0000244|PDB:2GTG}.
HELIX 346 348 {ECO:0000244|PDB:1M12}.
HELIX 351 373 {ECO:0000244|PDB:2GTG}.
HELIX 378 384 {ECO:0000244|PDB:2GTG}.
TURN 386 388 {ECO:0000244|PDB:1SN6}.
HELIX 409 422 {ECO:0000244|PDB:3BQP}.
HELIX 429 439 {ECO:0000244|PDB:3BQP}.
HELIX 440 442 {ECO:0000244|PDB:3BQP}.
HELIX 445 447 {ECO:0000244|PDB:3BQP}.
HELIX 448 466 {ECO:0000244|PDB:3BQP}.
HELIX 472 478 {ECO:0000244|PDB:3BQP}.
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


Related products :

Catalog number Product name Quantity
EIAAB37274 Cerebroside sulfate activator protein,Ganglioside GM2 activator,GM2A,GM2-AP,Homo sapiens,Human,SAP-3,Shingolipid activator protein 3
EIAAB37275 Cerebroside sulfate activator protein,Ganglioside GM2 activator,Gm2a,GM2-AP,Mouse,Mus musculus,SAP-3,Shingolipid activator protein 3
orb71952 Saposin C18 peptide This is Saposin C18 peptide. For research use only. 1 mg
orb71013 Saposin C12 peptide This is Saposin C12 peptide. For research use only. 1 mg
orb71953 Saposin C22 peptide This is Saposin C22 peptide. For research use only. 1 mg
EIAAB32394 Homo sapiens,HSD14,HSD-14,Human,Interferon-inducible double stranded RNA-dependent protein kinase activator A,PACT,PKR-associated protein X,PKR-associating protein X,PRKRA,Protein activator of the int
EIAAB34351 A1 140 kDa subunit,A1-P145,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,Differentiation-specific element-binding protein,Ibf-1,ISRE-binding protein,Mouse,Mus musculus,Re
EIAAB32395 Interferon-inducible double stranded RNA-dependent protein kinase activator A,Mouse,Mus musculus,PKR-associated protein X,PKR-associating protein X,Prkra,Protein activator of the interferon-induced pr
EIAAB08267 Cnpy2,MIR-interacting saposin-like protein,Mouse,Msap,Mus musculus,Protein canopy homolog 2,Putative secreted protein ZSIG9,Tmem4,Transmembrane protein 4,Zsig9
EIAAB08268 CNPY2,Homo sapiens,Human,MIR-interacting saposin-like protein,MSAP,Protein canopy homolog 2,Putative secreted protein Zsig9,TMEM4,Transmembrane protein 4,UNQ1943_PRO4426,ZSIG9
EIAAB27577 Antigen NY-CO-31,Homo sapiens,Human,NADPH oxidase activator 1,NCF2-like protein,NOX activator 1,NOXA1,P51NOX,p51-nox,P67phox-like factor
EIAAB32881 Kiaa0077,Mouse,Mus musculus,Proteasome activator complex subunit 4,Proteasome activator PA200,Protein TEMO,Psme4
KP1496 Saposin C22 5 mg
EIAAB34352 A1 140 kDa subunit,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,DNA-binding protein PO-GA,Homo sapiens,Human,Replication factor C 140 kDa subunit,Replication factor C la
EIAAB39992 Homo sapiens,Human,RBT1,Replication protein-binding trans-activator,RPA-binding trans-activator,SERTA domain-containing protein 3,SERTAD3
orb90285 Human Tissue Plasminogen Activator protein Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a mole 20
EIAAB39991 Mouse,Mus musculus,Rbt1,Replication protein-binding trans-activator,RPA-binding trans-activator,SERTA domain-containing protein 3,Sertad3
SP-86870-1 Saposin C18 (AA: Val-Lys-Glu-Val-Thr-Lys-Leu-Ile-Asp-Asn-Asn-Lys-Thr-Glu-Lys-Glu-Ile-Leu) (MW: 2114.49) 1 mg
SP-86871-5 Saposin C12 (AA: Leu-Ile-Asp-Asn-Asn-Lys-Thr-Glu-Lys-Glu-Ile-Leu) (MW: 1429.65) 5 mg
SP-86869-1 Saposin C22 (AA Cys_Glu_Phe_Leu_Val_Lys_Glu_Val_Thr_Lys_Leu_Ile_Asp_Asn_Asn_Lys_Thr_Glu_Lys_Glu_Ile_Leu) (MW 2607.08) 1 mg
SP-86869-1 Saposin C22 (AA: Cys-Glu-Phe-Leu-Val-Lys-Glu-Val-Thr-Lys-Leu-Ile-Asp-Asn-Asn-Lys-Thr-Glu-Lys-Glu-Ile-Leu) (MW: 2607.08) 1 mg
EIAAB32876 11S regulator complex subunit beta,Activator of multicatalytic protease subunit 2,Homo sapiens,Human,PA28b,PA28beta,Proteasome activator 28 subunit beta,Proteasome activator complex subunit 2,PSME2,RE
SP-86871-5 Saposin C12 (AA Leu_Ile_Asp_Asn_Asn_Lys_Thr_Glu_Lys_Glu_Ile_Leu) (MW 1429.65) 5 mg
EIAAB37267 Pig,PSAP,Saposin-B-Val,Sus scrofa
SP-86870-1 Saposin C18 (AA Val_Lys_Glu_Val_Thr_Lys_Leu_Ile_Asp_Asn_Asn_Lys_Thr_Glu_Lys_Glu_Ile_Leu) (MW 2114.49) 1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur