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Protein

Prosaposin

Gene

Psap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication
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.By similarity
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.By similarity
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).By similarity
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.By similarity

GO - Molecular functioni

  • enzyme activator activity Source: GO_Central
  • G-protein coupled receptor binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: ParkinsonsUK-UCL
  • cellular response to organic substance Source: MGI
  • developmental growth Source: MGI
  • epithelial cell differentiation involved in prostate gland development Source: MGI
  • glycosphingolipid metabolic process Source: GO_Central
  • negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
  • positive regulation of MAPK cascade Source: ParkinsonsUK-UCL
  • prostate gland growth Source: MGI
  • regulation of lipid metabolic process Source: MGI
  • regulation of MAPK cascade Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-375276. Peptide ligand-binding receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Prosaposin
Alternative name(s):
Sulfated glycoprotein 1
Short name:
SGP-1
Cleaved into the following 5 chains:
Gene namesi
Name:Psap
Synonyms:Sgp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97783. Psap.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • lysosome Source: InterPro
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 557541ProsaposinPRO_0000031626Add
BLAST
Propeptidei17 – 5943By similarityPRO_0000434953Add
BLAST
Chaini60 – 14283Saposin-ABy similarityPRO_0000434954Add
BLAST
Propeptidei143 – 19351By similarityPRO_0000434955Add
BLAST
Chaini194 – 27683Saposin-B-ValBy similarityPRO_0000434956Add
BLAST
Chaini194 – 27582Saposin-BBy similarityPRO_0000434957Add
BLAST
Propeptidei277 – 31236By similarityPRO_0000434958Add
BLAST
Chaini313 – ?39280Saposin-CBy similarityPRO_0000434959Add
BLAST
Propeptidei?393 – 43745By similarityPRO_0000434960Add
BLAST
Chaini438 – 51982Saposin-DBy similarityPRO_0000434961Add
BLAST
Propeptidei520 – 55738By similarityPRO_0000434962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 ↔ 138PROSITE-ProRule annotation
Disulfide bondi66 ↔ 132PROSITE-ProRule annotation
Glycosylationi80 – 801N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
Disulfide bondi94 ↔ 106PROSITE-ProRule annotation
Disulfide bondi197 ↔ 273PROSITE-ProRule annotation
Disulfide bondi200 ↔ 267PROSITE-ProRule annotation
Glycosylationi214 – 2141N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi229 ↔ 240PROSITE-ProRule annotation
Disulfide bondi317 ↔ 390PROSITE-ProRule annotation
Disulfide bondi320 ↔ 384PROSITE-ProRule annotation
Glycosylationi334 – 3341N-linked (GlcNAc...)PROSITE-ProRule annotation1 Publication
Disulfide bondi348 ↔ 359PROSITE-ProRule annotation
Disulfide bondi442 ↔ 515PROSITE-ProRule annotation
Disulfide bondi445 ↔ 509PROSITE-ProRule annotation
Glycosylationi459 – 4591N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi473 ↔ 484PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ61207.
MaxQBiQ61207.
PaxDbiQ61207.
PeptideAtlasiQ61207.
PRIDEiQ61207.

PTM databases

PhosphoSiteiQ61207.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004207.
CleanExiMM_PSAP.
ExpressionAtlasiQ61207. baseline and differential.
GenevisibleiQ61207. MM.

Interactioni

GO - Molecular functioni

  • G-protein coupled receptor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi202410. 2 interactions.
IntActiQ61207. 6 interactions.
MINTiMINT-1734080.
STRINGi10090.ENSMUSP00000137476.

Structurei

3D structure databases

ProteinModelPortaliQ61207.
SMRiQ61207. Positions 60-139, 195-274, 315-391, 439-517.
ModBaseiSearch...
MobiDBiSearch...

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
Domaini193 – 27785Saposin B-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini313 – 39482Saposin B-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini438 – 51982Saposin B-type 4PROSITE-ProRule annotationAdd
BLAST
Domaini521 – 55737Saposin 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

eggNOGiKOG1340. Eukaryota.
ENOG410XSI5. LUCA.
GeneTreeiENSGT00530000063434.
HOGENOMiHOG000049216.
HOVERGENiHBG002617.
InParanoidiQ61207.
KOiK12382.
OMAiQPKANED.
PhylomeDBiQ61207.

Family and domain databases

Gene3Di1.10.225.10. 4 hits.
InterProiIPR003119. SAP_A.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB_dom.
[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. 3 hits.
PROSITEiPS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYALALFASL LATALTSPVQ DPKTCSGGSA VLCRDVKTAV DCGAVKHCQQ
60 70 80 90 100
MVWSKPTAKS LPCDICKTVV TEAGNLLKDN ATQEEILHYL EKTCEWIHDS
110 120 130 140 150
SLSASCKEVV DSYLPVILDM IKGEMSNPGE VCSALNLCQS LQEYLAEQNQ
160 170 180 190 200
KQLESNKIPE VDMARVVAPF MSNIPLLLYP QDHPRSQPQP KANEDVCQDC
210 220 230 240 250
MKLVSDVQTA VKTNSSFIQG FVDHVKEDCD RLGPGVSDIC KNYVDQYSEV
260 270 280 290 300
CVQMLMHMQD QQPKEICVLA GFCNEVKRVP MKTLVPATET IKNILPALEM
310 320 330 340 350
MDPYEQNLVQ AHNVILCQTC QFVMNKFSEL IVNNATEELL VKGLSNACAL
360 370 380 390 400
LPDPARTKCQ EVVGTFGPSL LDIFIHEVNP SSLCGVIGLC AARPELVEAL
410 420 430 440 450
EQPAPAIVSA LLKEPTPPKQ PAQPKQSALP AHVPPQKNGG FCEVCKKLVL
460 470 480 490 500
YLEHNLEKNS TKEEILAALE KGCSFLPDPY QKQCDDFVAE YEPLLLEILV
510 520 530 540 550
EVMDPGFVCS KIGVCPSAYK LLLGTEKCVW GPSYWCQNME TAARCNAVDH

CKRHVWN
Length:557
Mass (Da):61,422
Last modified:December 15, 1998 - v2
Checksum:i134593E20499E35E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831Q → E in AAB31059 (PubMed:8334382).Curated
Sequence conflicti158 – 1581I → V in AAA92567 (PubMed:8565332).Curated
Sequence conflicti160 – 1601Missing in AAB31059 (PubMed:8334382).Curated
Sequence conflicti171 – 1722MS → SA in AAA92567 (PubMed:8565332).Curated
Sequence conflicti244 – 2441V → L in AAB31059 (PubMed:8334382).Curated
Sequence conflicti254 – 2541M → I in AAA92567 (PubMed:8565332).Curated
Sequence conflicti255 – 2551L → W in AAB31059 (PubMed:8334382).Curated
Sequence conflicti260 – 2623Missing (PubMed:8565332).Curated
Sequence conflicti307 – 3071N → D in AAB31059 (PubMed:8334382).Curated
Sequence conflicti322 – 3221F → L in AAB31059 (PubMed:8334382).Curated
Sequence conflicti349 – 3502AL → GV in AAB22175 (PubMed:1590788).Curated
Sequence conflicti367 – 3671G → D in AAA92567 (PubMed:8565332).Curated
Sequence conflicti370 – 3701L → Q in AAB31059 (PubMed:8334382).Curated
Sequence conflicti373 – 3731I → D in AAA92567 (PubMed:8565332).Curated
Sequence conflicti391 – 3911A → T (PubMed:8565332).Curated
Sequence conflicti393 – 3931R → L (PubMed:8565332).Curated
Sequence conflicti406 – 4061A → R (PubMed:8334382).Curated
Sequence conflicti406 – 4061A → R (PubMed:8565332).Curated
Sequence conflicti430 – 4301P → R in AAB31059 (PubMed:8334382).Curated
Sequence conflicti445 – 4451C → F in AAA92567 (PubMed:8565332).Curated
Sequence conflicti448 – 4481L → P in AAB02695 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S36200 mRNA. Translation: AAB22175.1.
S71616 mRNA. Translation: AAB31059.1.
U27340 mRNA. Translation: AAA92567.1.
U57999 Genomic DNA. Translation: AAB02695.1.
CCDSiCCDS35911.1.
PIRiJH0604.
RefSeqiNP_001139592.1. NM_001146120.1.
NP_001139593.1. NM_001146121.1.
NP_001139594.1. NM_001146122.1.
NP_001139595.1. NM_001146123.1.
NP_001139596.1. NM_001146124.1.
NP_035309.3. NM_011179.3.
UniGeneiMm.277498.

Genome annotation databases

EnsembliENSMUST00000179238; ENSMUSP00000137476; ENSMUSG00000004207.
GeneIDi19156.
KEGGimmu:19156.
UCSCiuc033fpi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S36200 mRNA. Translation: AAB22175.1.
S71616 mRNA. Translation: AAB31059.1.
U27340 mRNA. Translation: AAA92567.1.
U57999 Genomic DNA. Translation: AAB02695.1.
CCDSiCCDS35911.1.
PIRiJH0604.
RefSeqiNP_001139592.1. NM_001146120.1.
NP_001139593.1. NM_001146121.1.
NP_001139594.1. NM_001146122.1.
NP_001139595.1. NM_001146123.1.
NP_001139596.1. NM_001146124.1.
NP_035309.3. NM_011179.3.
UniGeneiMm.277498.

3D structure databases

ProteinModelPortaliQ61207.
SMRiQ61207. Positions 60-139, 195-274, 315-391, 439-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202410. 2 interactions.
IntActiQ61207. 6 interactions.
MINTiMINT-1734080.
STRINGi10090.ENSMUSP00000137476.

PTM databases

PhosphoSiteiQ61207.

Proteomic databases

EPDiQ61207.
MaxQBiQ61207.
PaxDbiQ61207.
PeptideAtlasiQ61207.
PRIDEiQ61207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000179238; ENSMUSP00000137476; ENSMUSG00000004207.
GeneIDi19156.
KEGGimmu:19156.
UCSCiuc033fpi.1. mouse.

Organism-specific databases

CTDi5660.
MGIiMGI:97783. Psap.

Phylogenomic databases

eggNOGiKOG1340. Eukaryota.
ENOG410XSI5. LUCA.
GeneTreeiENSGT00530000063434.
HOGENOMiHOG000049216.
HOVERGENiHBG002617.
InParanoidiQ61207.
KOiK12382.
OMAiQPKANED.
PhylomeDBiQ61207.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-375276. Peptide ligand-binding receptors.

Miscellaneous databases

ChiTaRSiPsap. mouse.
PROiQ61207.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004207.
CleanExiMM_PSAP.
ExpressionAtlasiQ61207. baseline and differential.
GenevisibleiQ61207. MM.

Family and domain databases

Gene3Di1.10.225.10. 4 hits.
InterProiIPR003119. SAP_A.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR008373. Saposin.
IPR011001. Saposin-like.
IPR021165. Saposin_chordata.
IPR008139. SaposinB_dom.
[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. 3 hits.
PROSITEiPS51110. SAP_A. 2 hits.
PS50015. SAP_B. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAP_MOUSE
AccessioniPrimary (citable) accession number: Q61207
Secondary accession number(s): Q60861, Q64006, Q64219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: September 7, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.