| |
|---|---|
| Accession Number: | P07602 |
| Protein Name: | SAP aka CSAP aka PSAP |
| Length: | 524 |
| Molecular Weight: | 58113.00 |
| Species: | Homo sapiens (Human) [9606] |
| Number of TMSs: | 1 |
| Location1 / Topology2 / Orientation3: | Lysosome1 |
| Substrate | molecule |
Cross database links:
| DIP: | DIP-29803N |
|---|---|
| RefSeq: | NP_001035930.1 NP_001035931.1 NP_002769.1 |
| Entrez Gene ID: | 5660 |
| Pfam: | PF02199 PF05184 PF03489 |
| OMIM: |
176801 gene 249900 phenotype 610539 phenotype 611721 phenotype 611722 phenotype |
| KEGG: | hsa:5660 |
Gene Ontology
GO:0005615
C:extracellular space
GO:0005794
C:Golgi apparatus
GO:0016021
C:integral to membrane
GO:0043202
C:lysosomal lumen
GO:0008047
F:enzyme activator activity
GO:0008289
F:lipid binding
GO:0006687
P:glycosphingolipid metabolic process
GO:0006869
P:lipid transport
| |
References (36)[1] “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.” Rorman E.G.et.al. 2515150 [2] “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.” Nakano T.et.al. 2498298 [3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [4] “Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.” O'Brien J.S.et.al. 2842863 [5] “Structure and evolution of the human prosaposin chromosomal gene.” Rorman E.G.et.al. 1612590 [6] “Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins).” Hiraiwa M.et.al. 8323276 [7] “Isolation and characterization of prosaposin from human milk.” Kondoh K.et.al. 1958198 [8] “The organization of the gene for the human cerebroside sulfate activator protein.” Holtschmidt H.et.al. 2013321 [9] “Saposin A: second cerebrosidase activator protein.” Morimoto S.et.al. 2717620 [10] “Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis.” Tyynela J.et.al. 8370464 [11] “Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor.” Dewji N.N.et.al. 2825202 [12] “Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator.” Dewji N.N.et.al. 2868718 [13] “Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1).” Kleinschmidt T.et.al. 3242555 [14] “The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein.” Furst W.et.al. 2209618 [15] “Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant.” Kleinschmidt T.et.al. 3442600 [16] “Saposin D: a sphingomyelinase activator.” Morimoto S.et.al. 2845979 [17] “The precursor of sulfatide activator protein is processed to three different proteins.” Furst W.et.al. 3048308 [18] “Preparation of the cerebroside sulfate activator (CSAct or saposin B) from human urine.” Fluharty A.L.et.al. 10562467 [19] “Structural analysis of saposin C and B. Complete localization of disulfide bridges.” Vaccaro A.M.et.al. 7730378 [20] “Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.” Faull K.F.et.al. 11180632 [21] “Structural and membrane-binding properties of saposin D.” Tatti M.et.al. 10406958 [22] “Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B.” Ahn V.E.et.al. 12510003 [23] “Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties.” Faull K.F.et.al. 10510427 [24] “Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.” Chen R.et.al. 19159218 [25] “Crystal structure of saposin B reveals a dimeric shell for lipid binding.” Ahn V.E.et.al. 12518053 [26] “Molecular genetics of metachromatic leukodystrophy.” Gieselmann V.et.al. 7866401 [27] “Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy.” Rafi M.A.et.al. 2302219 [28] “Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect.” Kretz K.A.et.al. 2320574 [29] “Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease.” Holtschmidt H.et.al. 2019586 [30] “Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene.” Schnabel D.et.al. 1371116 [31] “Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease.” Schnabel D.et.al. 2060627 [32] “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.” Regis S.et.al. 10196694 [33] “A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD).” Wrobe D.et.al. 10682309 [34] “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.” Hulkova H.et.al. 11309366 | |
| Structure: | |
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| FASTA formatted sequence |
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1: MYALFLLASL LGAALAGPVL GLKECTRGSA VWCQNVKTAS DCGAVKHCLQ TVWNKPTVKS 61: LPCDICKDVV TAAGDMLKDN ATEEEILVYL EKTCDWLPKP NMSASCKEIV DSYLPVILDI 121: IKGEMSRPGE VCSALNLCES LQKHLAELNH QKQLESNKIP ELDMTEVVAP FMANIPLLLY 181: PQDGPRSKPQ PKDNGDVCQD CIQMVTDIQT AVRTNSTFVQ ALVEHVKEEC DRLGPGMADI 241: CKNYISQYSE IAIQMMMHMQ PKEICALVGF CDEVKEMPMQ TLVPAKVASK NVIPALELVE 301: PIKKHEVPAK SDVYCEVCEF LVKEVTKLID NNKTEKEILD AFDKMCSKLP KSLSEECQEV 361: VDTYGSSILS ILLEEVSPEL VCSMLHLCSG TRLPALTVHV TQPKDGGFCE VCKKLVGYLD 421: RNLEKNSTKQ EILAALEKGC SFLPDPYQKQ CDQFVAEYEP VLIEILVEVM DPSFVCLKIG 481: ACPSAHKPLL GTEKCIWGPS YWCQNTETAA QCNAVEHCKR HVWN