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P07602

- SAP_HUMAN

UniProt

P07602 - SAP_HUMAN

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Protein

Prosaposin

Gene

PSAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).
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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei215 – 2151Not glycosylated; in variant MLD-SAPB Ile-217

GO - Molecular functioni

  1. enzyme activator activity Source: ProtInc
  2. lipid binding Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cellular response to organic substance Source: Ensembl
  3. epithelial cell differentiation involved in prostate gland development Source: Ensembl
  4. glycosphingolipid metabolic process Source: Reactome
  5. lipid transport Source: ProtInc
  6. platelet activation Source: Reactome
  7. platelet degranulation Source: Reactome
  8. positive regulation of catalytic activity Source: GOC
  9. prostate gland growth Source: Ensembl
  10. regulation of lipid metabolic process Source: Ensembl
  11. regulation of MAPK cascade Source: Ensembl
  12. small molecule metabolic process Source: Reactome
  13. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.

Protein family/group databases

TCDBi1.C.35.2.1. the amoebapore (amoebapore) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Prosaposin
Alternative name(s):
Proactivator polypeptide
Cleaved into the following 5 chains:
Alternative name(s):
Protein A
Alternative name(s):
Cerebroside sulfate activator
Short name:
CSAct
Dispersin
Sphingolipid activator protein 1
Short name:
SAP-1
Sulfatide/GM1 activator
Alternative name(s):
A1 activator
Co-beta-glucosidase
Glucosylceramidase activator
Sphingolipid activator protein 2
Short name:
SAP-2
Alternative name(s):
Component C
Protein C
Gene namesi
Name:PSAP
Synonyms:GLBA, SAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9498. PSAP.

Subcellular locationi

Lysosome 3 Publications
Chain Prosaposin : Secreted
Note: Secreted as a fully glycosylated 70 kDa protein composed of complex glycans.

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of membrane Source: ProtInc
  5. lysosomal lumen Source: Reactome
  6. lysosomal membrane Source: Reactome
  7. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Involvement in diseasei

Combined saposin deficiency (CSAPD) [MIM:611721]: Due to absence of all saposins, leading to a fatal storage disorder with hepatosplenomegaly and severe neurological involvement.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151N → H in MLD-SAPB; reduces the intracellular activity of the protein significantly. 1 Publication
VAR_031823
Natural varianti215 – 2151N → K in MLD-SAPB. 1 Publication
VAR_031899
Natural varianti217 – 2171T → I in MLD-SAPB; juvenile; affects glycosylation at N-215. 2 Publications
VAR_006943
Natural varianti241 – 2411C → S in MLD-SAPB; severe. 1 Publication
Corresponds to variant rs1130793 [ dbSNP | Ensembl ].
VAR_006944
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti349 – 3491L → P in AGD. 1 Publication
VAR_042441
Natural varianti388 – 3881C → F in AGD. 1 Publication
VAR_006945
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701Missing in AKRD. 1 Publication
VAR_042440
Defects in PSAP saposin-D region are found in a variant of Tay-Sachs disease (GM2-gangliosidosis).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi240 – 2401I → C: Strongly decreases stimulation of cerebroside sulfate hydrolysis. 1 Publication

Keywords - Diseasei

Disease mutation, Gangliosidosis, Gaucher disease, Leukodystrophy, Metachromatic leukodystrophy

Organism-specific databases

MIMi249900. phenotype.
610539. phenotype.
611721. phenotype.
611722. phenotype.
Orphaneti309252. Atypical Gaucher disease due to saposin C deficiency.
139406. Encephalopathy due to prosaposin deficiency.
206436. Infantile Krabbe disease.
309271. Metachromatic leukodystrophy, adult form.
309263. Metachromatic leukodystrophy, juvenile form.
309256. Metachromatic leukodystrophy, late infantile form.
PharmGKBiPA33845.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16162 PublicationsAdd
BLAST
Chaini17 – 524508ProsaposinPRO_0000424774Add
BLAST
Propeptidei17 – 5842PRO_0000031616Add
BLAST
Chaini60 – 14283Saposin-APRO_0000031617Add
BLAST
Propeptidei144 – 19451PRO_0000031618Add
BLAST
Chaini195 – 27480Saposin-B-ValPRO_0000031619Add
BLAST
Chaini195 – 27379Saposin-BPRO_0000031620Add
BLAST
Propeptidei276 – 30934PRO_0000031621Add
BLAST
Chaini311 – 39181Saposin-CPRO_0000031622Add
BLAST
Propeptidei393 – 40311PRO_0000031623Add
BLAST
Chaini405 – 48682Saposin-DPRO_0000031624Add
BLAST
Propeptidei488 – 52437PRO_0000031625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 ↔ 138
Disulfide bondi66 ↔ 132
Glycosylationi80 – 801N-linked (GlcNAc...)3 PublicationsPROSITE-ProRule annotation
Disulfide bondi94 ↔ 106
Glycosylationi101 – 1011N-linked (GlcNAc...)3 PublicationsPROSITE-ProRule annotation
Disulfide bondi198 ↔ 271
Disulfide bondi201 ↔ 265
Glycosylationi215 – 2151N-linked (GlcNAc...) (complex)1 PublicationPROSITE-ProRule annotationCAR_000176
Disulfide bondi230 ↔ 2411 PublicationPROSITE-ProRule annotation
Disulfide bondi315 ↔ 3881 PublicationPROSITE-ProRule annotation
Disulfide bondi318 ↔ 3821 PublicationPROSITE-ProRule annotation
Glycosylationi332 – 3321N-linked (GlcNAc...)2 PublicationsPROSITE-ProRule annotation
Disulfide bondi346 ↔ 3571 PublicationPROSITE-ProRule annotation
Disulfide bondi409 ↔ 482
Disulfide bondi412 ↔ 476
Glycosylationi426 – 4261N-linked (GlcNAc...)2 PublicationsPROSITE-ProRule annotation
Disulfide bondi440 ↔ 451

Post-translational modificationi

The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.
N-linked glycans show a high degree of microheterogeneity.2 Publications
The one residue extended Saposin-B-Val is only found in 5% of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP07602.
PaxDbiP07602.
PRIDEiP07602.

PTM databases

PhosphoSiteiP07602.
UniCarbKBiP07602.

Expressioni

Gene expression databases

BgeeiP07602.
CleanExiHS_PSAP.
ExpressionAtlasiP07602. baseline and differential.
GenevestigatoriP07602.

Organism-specific databases

HPAiCAB004647.
HPA004426.

Interactioni

Subunit structurei

Saposin-B is a homodimer. Prosaposin exists as a roughly half-half mixture of monomers and disulfide-linked dimers. Monomeric prosaposin interacts (via C-terminus) with sortilin/SORT1, the interaction is required for targeting to lysosomes.5 Publications

Protein-protein interaction databases

BioGridi111639. 43 interactions.
DIPiDIP-29803N.
IntActiP07602. 13 interactions.
MINTiMINT-1193270.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi61 – 7818
Helixi82 – 9413
Beta strandi97 – 993
Helixi101 – 12525
Helixi128 – 1347
Helixi196 – 21419
Helixi218 – 22912
Helixi230 – 2334
Helixi237 – 25620
Helixi261 – 2677
Helixi314 – 33017
Helixi335 – 34511
Helixi346 – 3483
Helixi351 – 37323
Helixi378 – 3847
Turni386 – 3883
Helixi409 – 42214
Helixi429 – 43911
Helixi440 – 4423
Helixi445 – 4473
Helixi448 – 46619
Helixi472 – 4787

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M12NMR-A311-390[»]
1N69X-ray2.20A/B/C195-273[»]
1SN6NMR-A311-390[»]
2DOBX-ray2.00A60-140[»]
2GTGX-ray2.40A311-391[»]
2QYPX-ray2.45A/B311-392[»]
2R0RX-ray2.50A/B407-484[»]
2R1QX-ray2.50A407-484[»]
2RB3X-ray2.10A/B/C/D407-484[»]
2Z9AX-ray2.50A/B311-389[»]
3BQPX-ray1.30A/B405-484[»]
3BQQX-ray2.00A/B/C/D405-484[»]
4DDJX-ray1.90A60-140[»]
DisProtiDP00733.
ProteinModelPortaliP07602.
SMRiP07602. Positions 60-139, 195-272, 312-484.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5841Saposin A-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini59 – 14284Saposin B-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini194 – 27582Saposin B-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini311 – 39282Saposin B-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 48682Saposin B-type 4PROSITE-ProRule annotationAdd
BLAST
Domaini488 – 52437Saposin A-type 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 saposin A-type domains.PROSITE-ProRule annotation
Contains 4 saposin B-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG269151.
GeneTreeiENSGT00530000063434.
HOVERGENiHBG002617.
InParanoidiP07602.
KOiK12382.
OrthoDBiEOG7ZSHSC.
PhylomeDBiP07602.
TreeFamiTF316942.

Family and domain databases

Gene3Di1.10.225.10. 4 hits.
InterProiIPR003119. SapA.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB.
[Graphical view]
PfamiPF02199. SapA. 2 hits.
PF05184. SapB_1. 4 hits.
PF03489. SapB_2. 4 hits.
[Graphical view]
PIRSFiPIRSF002431. Saposin. 1 hit.
PRINTSiPR01797. SAPOSIN.
SMARTiSM00162. SAPA. 2 hits.
SM00741. SapB. 4 hits.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 4 hits.
PROSITEiPS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Sap-mu-0 (identifier: P07602-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYALFLLASL LGAALAGPVL GLKECTRGSA VWCQNVKTAS DCGAVKHCLQ
60 70 80 90 100
TVWNKPTVKS LPCDICKDVV TAAGDMLKDN ATEEEILVYL EKTCDWLPKP
110 120 130 140 150
NMSASCKEIV DSYLPVILDI IKGEMSRPGE VCSALNLCES LQKHLAELNH
160 170 180 190 200
QKQLESNKIP ELDMTEVVAP FMANIPLLLY PQDGPRSKPQ PKDNGDVCQD
210 220 230 240 250
CIQMVTDIQT AVRTNSTFVQ ALVEHVKEEC DRLGPGMADI CKNYISQYSE
260 270 280 290 300
IAIQMMMHMQ PKEICALVGF CDEVKEMPMQ TLVPAKVASK NVIPALELVE
310 320 330 340 350
PIKKHEVPAK SDVYCEVCEF LVKEVTKLID NNKTEKEILD AFDKMCSKLP
360 370 380 390 400
KSLSEECQEV VDTYGSSILS ILLEEVSPEL VCSMLHLCSG TRLPALTVHV
410 420 430 440 450
TQPKDGGFCE VCKKLVGYLD RNLEKNSTKQ EILAALEKGC SFLPDPYQKQ
460 470 480 490 500
CDQFVAEYEP VLIEILVEVM DPSFVCLKIG ACPSAHKPLL GTEKCIWGPS
510 520
YWCQNTETAA QCNAVEHCKR HVWN
Length:524
Mass (Da):58,113
Last modified:August 1, 1990 - v2
Checksum:i71977F7A8C9E1533
GO
Isoform Sap-mu-6 (identifier: P07602-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-259: M → MDQ

Show »
Length:526
Mass (Da):58,356
Checksum:i2A6E54624BA9D814
GO
Isoform Sap-mu-9 (identifier: P07602-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     260-260: Q → QDQQ

Show »
Length:527
Mass (Da):58,484
Checksum:i293FBB7472D82BD0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3691L → P in CAG33027. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701Missing in AKRD. 1 Publication
VAR_042440
Natural varianti215 – 2151N → H in MLD-SAPB; reduces the intracellular activity of the protein significantly. 1 Publication
VAR_031823
Natural varianti215 – 2151N → K in MLD-SAPB. 1 Publication
VAR_031899
Natural varianti217 – 2171T → I in MLD-SAPB; juvenile; affects glycosylation at N-215. 2 Publications
VAR_006943
Natural varianti241 – 2411C → S in MLD-SAPB; severe. 1 Publication
Corresponds to variant rs1130793 [ dbSNP | Ensembl ].
VAR_006944
Natural varianti349 – 3491L → P in AGD. 1 Publication
VAR_042441
Natural varianti388 – 3881C → F in AGD. 1 Publication
VAR_006945

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei259 – 2591M → MDQ in isoform Sap-mu-6. CuratedVSP_006014
Alternative sequencei260 – 2601Q → QDQQ in isoform Sap-mu-9. CuratedVSP_006015

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03077 mRNA. Translation: AAA52560.1.
D00422 mRNA. Translation: BAA00321.1.
BT006849 mRNA. Translation: AAP35495.1.
CR456746 mRNA. Translation: CAG33027.1.
AL731541, AC073370 Genomic DNA. Translation: CAI40837.1.
CH471083 Genomic DNA. Translation: EAW54437.1.
BC001503 mRNA. Translation: AAH01503.1.
BC004275 mRNA. Translation: AAH04275.1.
BC007612 mRNA. Translation: AAH07612.1.
M86181 Genomic DNA. No translation available.
X57107 Genomic DNA. Translation: CAA40391.1.
X57108 Genomic DNA. Translation: CAA40392.1.
M12710 mRNA. No translation available.
J03015 mRNA. Translation: AAB59494.1.
M32221 mRNA. Translation: AAA60303.1.
M60257 mRNA. Translation: AAA36595.1.
M60258 mRNA. Translation: AAA36596.1.
M60255 mRNA. Translation: AAA36594.1.
CCDSiCCDS7311.1. [P07602-1]
PIRiJX0061. SAHUP.
RefSeqiNP_001035930.1. NM_001042465.1. [P07602-3]
NP_001035931.1. NM_001042466.1. [P07602-2]
NP_002769.1. NM_002778.2. [P07602-1]
UniGeneiHs.523004.

Genome annotation databases

EnsembliENST00000394936; ENSP00000378394; ENSG00000197746. [P07602-1]
GeneIDi5660.
KEGGihsa:5660.
UCSCiuc001jsm.3. human. [P07602-1]

Polymorphism databases

DMDMi134218.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03077 mRNA. Translation: AAA52560.1 .
D00422 mRNA. Translation: BAA00321.1 .
BT006849 mRNA. Translation: AAP35495.1 .
CR456746 mRNA. Translation: CAG33027.1 .
AL731541 , AC073370 Genomic DNA. Translation: CAI40837.1 .
CH471083 Genomic DNA. Translation: EAW54437.1 .
BC001503 mRNA. Translation: AAH01503.1 .
BC004275 mRNA. Translation: AAH04275.1 .
BC007612 mRNA. Translation: AAH07612.1 .
M86181 Genomic DNA. No translation available.
X57107 Genomic DNA. Translation: CAA40391.1 .
X57108 Genomic DNA. Translation: CAA40392.1 .
M12710 mRNA. No translation available.
J03015 mRNA. Translation: AAB59494.1 .
M32221 mRNA. Translation: AAA60303.1 .
M60257 mRNA. Translation: AAA36595.1 .
M60258 mRNA. Translation: AAA36596.1 .
M60255 mRNA. Translation: AAA36594.1 .
CCDSi CCDS7311.1. [P07602-1 ]
PIRi JX0061. SAHUP.
RefSeqi NP_001035930.1. NM_001042465.1. [P07602-3 ]
NP_001035931.1. NM_001042466.1. [P07602-2 ]
NP_002769.1. NM_002778.2. [P07602-1 ]
UniGenei Hs.523004.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M12 NMR - A 311-390 [» ]
1N69 X-ray 2.20 A/B/C 195-273 [» ]
1SN6 NMR - A 311-390 [» ]
2DOB X-ray 2.00 A 60-140 [» ]
2GTG X-ray 2.40 A 311-391 [» ]
2QYP X-ray 2.45 A/B 311-392 [» ]
2R0R X-ray 2.50 A/B 407-484 [» ]
2R1Q X-ray 2.50 A 407-484 [» ]
2RB3 X-ray 2.10 A/B/C/D 407-484 [» ]
2Z9A X-ray 2.50 A/B 311-389 [» ]
3BQP X-ray 1.30 A/B 405-484 [» ]
3BQQ X-ray 2.00 A/B/C/D 405-484 [» ]
4DDJ X-ray 1.90 A 60-140 [» ]
DisProti DP00733.
ProteinModelPortali P07602.
SMRi P07602. Positions 60-139, 195-272, 312-484.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111639. 43 interactions.
DIPi DIP-29803N.
IntActi P07602. 13 interactions.
MINTi MINT-1193270.

Protein family/group databases

TCDBi 1.C.35.2.1. the amoebapore (amoebapore) family.

PTM databases

PhosphoSitei P07602.
UniCarbKBi P07602.

Polymorphism databases

DMDMi 134218.

Proteomic databases

MaxQBi P07602.
PaxDbi P07602.
PRIDEi P07602.

Protocols and materials databases

DNASUi 5660.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394936 ; ENSP00000378394 ; ENSG00000197746 . [P07602-1 ]
GeneIDi 5660.
KEGGi hsa:5660.
UCSCi uc001jsm.3. human. [P07602-1 ]

Organism-specific databases

CTDi 5660.
GeneCardsi GC10M073576.
HGNCi HGNC:9498. PSAP.
HPAi CAB004647.
HPA004426.
MIMi 176801. gene.
249900. phenotype.
610539. phenotype.
611721. phenotype.
611722. phenotype.
neXtProti NX_P07602.
Orphaneti 309252. Atypical Gaucher disease due to saposin C deficiency.
139406. Encephalopathy due to prosaposin deficiency.
206436. Infantile Krabbe disease.
309271. Metachromatic leukodystrophy, adult form.
309263. Metachromatic leukodystrophy, juvenile form.
309256. Metachromatic leukodystrophy, late infantile form.
PharmGKBi PA33845.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269151.
GeneTreei ENSGT00530000063434.
HOVERGENi HBG002617.
InParanoidi P07602.
KOi K12382.
OrthoDBi EOG7ZSHSC.
PhylomeDBi P07602.
TreeFami TF316942.

Enzyme and pathway databases

Reactomei REACT_116105. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSi PSAP. human.
EvolutionaryTracei P07602.
GeneWikii Prosaposin.
GenomeRNAii 5660.
NextBioi 21992.
PROi P07602.
SOURCEi Search...

Gene expression databases

Bgeei P07602.
CleanExi HS_PSAP.
ExpressionAtlasi P07602. baseline and differential.
Genevestigatori P07602.

Family and domain databases

Gene3Di 1.10.225.10. 4 hits.
InterProi IPR003119. SapA.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB.
[Graphical view ]
Pfami PF02199. SapA. 2 hits.
PF05184. SapB_1. 4 hits.
PF03489. SapB_2. 4 hits.
[Graphical view ]
PIRSFi PIRSF002431. Saposin. 1 hit.
PRINTSi PR01797. SAPOSIN.
SMARTi SM00162. SAPA. 2 hits.
SM00741. SapB. 4 hits.
[Graphical view ]
SUPFAMi SSF47862. SSF47862. 4 hits.
PROSITEi PS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
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Publicationsi

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  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., Grabowski G.A.
    Genomics 5:486-492(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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., Sandhoff K., Stuemper J., Christomanou H., Suzuki K.
    J. Biochem. 105:152-154(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    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.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    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.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SAP-MU-0).
    Tissue: Brain, Eye and Skin.
  8. "Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus."
    O'Brien J.S., Kretz K.A., Dewji N., Wenger D.A., Esch F., Fluharty A.L.
    Science 241:1098-1101(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-524.
  9. "Structure and evolution of the human prosaposin chromosomal gene."
    Rorman E.G., Scheinker V., Grabowski G.A.
    Genomics 13:312-318(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-524.
  10. "Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins)."
    Hiraiwa M., O'Brien J.S., Kishimoto Y., Galdzicka M., Fluharty A.L., Ginns E.I., Martin B.M.
    Arch. Biochem. Biophys. 304:110-116(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-24; 165-172; 180-189 AND 298-302.
  11. "Isolation and characterization of prosaposin from human milk."
    Kondoh K., Hineno T., Sano A., Kakimoto Y.
    Biochem. Biophys. Res. Commun. 181:286-292(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-26.
    Tissue: Milk.
  12. "The organization of the gene for the human cerebroside sulfate activator protein."
    Holtschmidt H., Sandhoff K., Fuerst W., Kwon H.Y., Schnabel D., Suzuki K.
    FEBS Lett. 280:267-270(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-125 AND 304-513.
    Tissue: Brain.
  13. Cited for: PROTEIN SEQUENCE OF 60-142.
  14. "Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis."
    Tyynela J., Palmer D.N., Baumann M., Haltia M.
    FEBS Lett. 330:8-12(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 62-84 AND 410-431.
  15. "Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor."
    Dewji N.N., Wenger D.A., O'Brien J.S.
    Proc. Natl. Acad. Sci. U.S.A. 84:8652-8656(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-524.
  16. "Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator."
    Dewji N.N., Wenger D.A., Fujibayashi S., Donoviel M., Esch F., Hill F., O'Brien J.S.
    Biochem. Biophys. Res. Commun. 134:989-994(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-263.
  17. "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., Christomanou H., Braunitzer G.
    Biol. Chem. Hoppe-Seyler 369:1361-1365(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 195-274.
  18. "The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein."
    Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.
    Eur. J. Biochem. 192:709-714(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 195-274.
    Tissue: Kidney.
  19. "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., Christomanou H., Braunitzer G.
    Biol. Chem. Hoppe-Seyler 368:1571-1578(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 311-390.
  20. Cited for: PROTEIN SEQUENCE OF 405-484.
  21. "The precursor of sulfatide activator protein is processed to three different proteins."
    Furst W., Machleidt W., Sandhoff K.
    Biol. Chem. Hoppe-Seyler 369:317-328(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 407-484.
  22. "Preparation of the cerebroside sulfate activator (CSAct or saposin B) from human urine."
    Fluharty A.L., Lombardo C., Louis A., Stevens R.L., Whitelegge J.P., Waring A.J., To T., Fluharty C.B., Faull K.F.
    Mol. Genet. Metab. 68:391-403(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE (SAPOSIN-B), STRUCTURE OF CARBOHYDRATES.
    Tissue: Urine.
  23. "Structural analysis of saposin C and B. Complete localization of disulfide bridges."
    Vaccaro A.M., Salvioli R., Barca A., Tatti M., Ciaffoni F., Maras B., Siciliano R., Zappacosta F., Amoresano A., Pucci P.
    J. Biol. Chem. 270:9953-9960(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS IN SAPOSINS-B AND C, IDENTIFICATION BY MASS SPECTROMETRY.
  24. "Prosaposin: a myelinotrophic protein that promotes expression of myelin constituents and is secreted after nerve injury."
    Hiraiwa M., Campana W.M., Mizisin A.P., Mohiuddin L., O'Brien J.S.
    Glia 26:353-360(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties."
    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.
    J. Mass Spectrom. 34:1040-1054(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Urine.
  26. "Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein."
    Faull K.F., Johnson J., Kim M.J., To T., Whitelegge J.P., Stevens R.L., Fluharty C.B., Fluharty A.L.
    J. Mass Spectrom. 35:1416-1424(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON ASN-215.
  27. Cited for: DISULFIDE BONDS IN SAPOSIN-D.
  28. "The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin."
    Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.
    EMBO J. 22:6430-6437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SORT1.
  29. "Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B."
    Ahn V.E., Faull K.F., Whitelegge J.P., Higginson J., Fluharty A.L., Prive G.G.
    Protein Expr. Purif. 27:186-193(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS IN SAPOSIN-B.
  30. "Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
    Ruiz-Canada C., Kelleher D.J., Gilmore R.
    Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-80; ASN-101; ASN-215; ASN-332 AND ASN-426.
  31. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80; ASN-101; ASN-332 AND ASN-426.
    Tissue: Liver.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Prosaposin sorting is mediated by oligomerization."
    Yuan L., Morales C.R.
    Exp. Cell Res. 317:2456-2467(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  34. "GPR37 and GPR37L1 are receptors for the neuroprotective and glioprotective factors prosaptide and prosaposin."
    Meyer R.C., Giddens M.M., Schaefer S.A., Hall R.A.
    Proc. Natl. Acad. Sci. U.S.A. 110:9529-9534(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  35. "Crystal structure of saposin B reveals a dimeric shell for lipid binding."
    Ahn V.E., Faull K.F., Whitelegge J.P., Fluharty A.L., Prive G.G.
    Proc. Natl. Acad. Sci. U.S.A. 100:38-43(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 195-273, MUTAGENESIS OF ILE-240.
  36. Cited for: REVIEW ON MLD-SAPB VARIANTS.
  37. "Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy."
    Rafi M.A., Zhang X.-L., Degala G., Wenger D.A.
    Biochem. Biophys. Res. Commun. 166:1017-1023(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLD-SAPB ILE-217.
  38. "Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect."
    Kretz K.A., Carson G.S., Morimoto S., Kishimoto Y., Fluharty A.L., O'Brien J.S.
    Proc. Natl. Acad. Sci. U.S.A. 87:2541-2544(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MLD-SAPB ILE-217.
  39. "Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease."
    Holtschmidt H., Sandhoff K., Kwon H.Y., Harzer K., Nakano T., Suzuki K.
    J. Biol. Chem. 266:7556-7560(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLD-SAPB SER-241, NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  40. "Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene."
    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.
    J. Biol. Chem. 267:3312-3315(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CSAPD.
  41. "Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease."
    Schnabel D., Schroeder M., Sandhoff K.
    FEBS Lett. 284:57-59(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AGD PHE-388.
  42. "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., Filocamo M., Corsolini F., Caroli F., Keulemans J.L.M., van Diggelen O.P., Gatti R.
    Eur. J. Hum. Genet. 7:125-130(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLD-SAPB LYS-215.
  43. "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., Henseler M., Huettler S., Pascual Pascual S.I., Chabas A., Sandhoff K.
    J. Inherit. Metab. Dis. 23:63-76(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MLD-SAPB HIS-215, CHARACTERIZATION OF VARIANT MLD-SAPB HIS-215.
  44. "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., 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.
    Hum. Mol. Genet. 10:927-940(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CSAPD.
  45. "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."
    Spiegel R., Bach G., Sury V., Mengistu G., Meidan B., Shalev S., Shneor Y., Mandel H., Zeigler M.
    Mol. Genet. Metab. 84:160-166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AKRD VAL-70 DEL.
  46. Cited for: VARIANT AGD PRO-349.

Entry informationi

Entry nameiSAP_HUMAN
AccessioniPrimary (citable) accession number: P07602
Secondary accession number(s): P07292
, P15793, P78538, P78541, P78546, P78547, P78558, Q53Y86, Q6IBQ6, Q92739, Q92740, Q92741, Q92742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Saposin-B co-purifies with 1 molecule of phosphatidylethanolamine.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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