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Protein

Prosaposin

Gene

Psap

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity
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

GO - Biological processi

Complete GO annotation...

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3423. Psap.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616By similarityAdd
BLAST
Chaini17 – 554538ProsaposinPRO_0000031629Add
BLAST
Propeptidei17 – 5943By similarityPRO_0000434963Add
BLAST
Chaini60 – 14283Saposin-ABy similarityPRO_0000434964Add
BLAST
Propeptidei143 – 19351By similarityPRO_0000434965Add
BLAST
Chaini194 – 27380Saposin-B-ValBy similarityPRO_0000434966Add
BLAST
Chaini194 – 27279Saposin-BBy similarityPRO_0000434967Add
BLAST
Propeptidei274 – 30936By similarityPRO_0000434968Add
BLAST
Chaini310 – ?38980Saposin-CBy similarityPRO_0000434969Add
BLAST
Propeptidei?390 – 43445By similarityPRO_0000434970Add
BLAST
Chaini435 – 51682Saposin-DBy similarityPRO_0000434971Add
BLAST
Propeptidei517 – 55438By similarityPRO_0000434972Add
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 annotation
Disulfide bondi94 ↔ 106PROSITE-ProRule annotation
Disulfide bondi197 ↔ 270PROSITE-ProRule annotation
Disulfide bondi200 ↔ 264PROSITE-ProRule annotation
Glycosylationi214 – 2141N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi229 ↔ 240PROSITE-ProRule annotation
Disulfide bondi314 ↔ 387PROSITE-ProRule annotation
Disulfide bondi317 ↔ 381PROSITE-ProRule annotation
Glycosylationi331 – 3311N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi345 ↔ 356PROSITE-ProRule annotation
Disulfide bondi439 ↔ 512PROSITE-ProRule annotation
Disulfide bondi442 ↔ 506PROSITE-ProRule annotation
Glycosylationi456 – 4561N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi470 ↔ 481PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP10960.
PRIDEiP10960.

PTM databases

iPTMnetiP10960.
PhosphoSiteiP10960.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247556. 1 interaction.
STRINGi10116.ENSRNOP00000000696.

Structurei

3D structure databases

ProteinModelPortaliP10960.
SMRiP10960. Positions 60-140, 195-271, 435-514.
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 – 27482Saposin B-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini310 – 39182Saposin B-type 3PROSITE-ProRule annotationAdd
BLAST
Domaini435 – 51682Saposin B-type 4PROSITE-ProRule annotationAdd
BLAST
Domaini518 – 55437Saposin 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.
HOGENOMiHOG000049216.
HOVERGENiHBG002617.
InParanoidiP10960.
KOiK12382.
PhylomeDBiP10960.

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.

P10960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYALALLASL LVTALTSPVQ DPKICSGGSA VVCRDVKTAV DCRAVKHCQQ
60 70 80 90 100
MVWSKPTAKS LPCDICKTVV TEAGNLLKDN ATEEEILHYL EKTCAWIHDS
110 120 130 140 150
SLSASCKEVV DSYLPVILDM IKGEMSNPGE VCSALNLCQS LQEYLAEQNQ
160 170 180 190 200
RQLESNKIPE VDLARVVAPF MSNIPLLLYP QDRPRSQPQP KANEDVCQDC
210 220 230 240 250
MKLVTDIQTA VRTNSSFVQG LVDHVKEDCD RLGPGVSDIC KNYVDQYSEV
260 270 280 290 300
AVQMMMHMQP KEICVMVGFC DEVKRVPMRT LVPATEAIKN ILPALELTDP
310 320 330 340 350
YEQDVIQAQN VIFCQVCQLV MRKLSELIIN NATEELLIKG LSKACSLLPA
360 370 380 390 400
PASTKCQEVL VTFGPSLLDV LMHEVNPNFL CGVISLCSAN PNLVGTLEQP
410 420 430 440 450
AAAIVSALPK EPAPPKQPEE PKQSALRAHV PPQKNGGFCE VCKKLVIYLE
460 470 480 490 500
HNLEKNSTKE EILAALEKGC SFLPDPYQKQ CDEFVAEYEP LLLEILVEVM
510 520 530 540 550
DPSFVCSKIG VCPSAYKLLL GTEKCVWGPG YWCQNSETAA RCNAVDHCKR

HVWN
Length:554
Mass (Da):61,124
Last modified:July 1, 1989 - v1
Checksum:iDFE3F3A3A0520C6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151P → L (PubMed:8573994).Curated
Sequence conflicti115 – 1151P → L (PubMed:8601692).Curated
Sequence conflicti299 – 2991D → E in AAB36042 (PubMed:8573994).Curated
Sequence conflicti462 – 4621I → V in AAB36233 (PubMed:8601692).Curated
Sequence conflicti527 – 5271W → R in AAB36233 (PubMed:8601692).Curated
Sequence conflicti536 – 5361S → M in AAB36233 (PubMed:8601692).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19936 mRNA. Translation: AAA42136.1.
S81353 mRNA. Translation: AAB36042.2.
S81373 mRNA. Translation: AAB36233.2.
PIRiA28716.
RefSeqiNP_001177165.1. NM_001190236.1.
NP_037145.2. NM_013013.2.
UniGeneiRn.97173.

Genome annotation databases

GeneIDi25524.
KEGGirno:25524.
UCSCiRGD:3423. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19936 mRNA. Translation: AAA42136.1.
S81353 mRNA. Translation: AAB36042.2.
S81373 mRNA. Translation: AAB36233.2.
PIRiA28716.
RefSeqiNP_001177165.1. NM_001190236.1.
NP_037145.2. NM_013013.2.
UniGeneiRn.97173.

3D structure databases

ProteinModelPortaliP10960.
SMRiP10960. Positions 60-140, 195-271, 435-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247556. 1 interaction.
STRINGi10116.ENSRNOP00000000696.

PTM databases

iPTMnetiP10960.
PhosphoSiteiP10960.

Proteomic databases

PaxDbiP10960.
PRIDEiP10960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25524.
KEGGirno:25524.
UCSCiRGD:3423. rat.

Organism-specific databases

CTDi5660.
RGDi3423. Psap.

Phylogenomic databases

eggNOGiKOG1340. Eukaryota.
ENOG410XSI5. LUCA.
HOGENOMiHOG000049216.
HOVERGENiHBG002617.
InParanoidiP10960.
KOiK12382.
PhylomeDBiP10960.

Miscellaneous databases

PROiP10960.

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_RAT
AccessioniPrimary (citable) accession number: P10960
Secondary accession number(s): Q62841, Q64190
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 128 of the entry and version 1 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. 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.