SAP_RAT
ID SAP_RAT Reviewed; 554 AA.
AC P10960; Q62841; Q64190;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Prosaposin;
DE AltName: Full=Sulfated glycoprotein 1;
DE Short=SGP-1;
DE Contains:
DE RecName: Full=Saposin-A;
DE Contains:
DE RecName: Full=Saposin-B-Val;
DE Contains:
DE RecName: Full=Saposin-B;
DE Contains:
DE RecName: Full=Saposin-C;
DE Contains:
DE RecName: Full=Saposin-D;
DE Flags: Precursor;
GN Name=Psap; Synonyms=Sgp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Sertoli cell;
RX PubMed=3048385; DOI=10.1021/bi00412a050;
RA Collard M.W., Sylvester S.R., Tsuruta J.K., Griswold M.D.;
RT "Biosynthesis and molecular cloning of sulfated glycoprotein 1 secreted by
RT rat Sertoli cells: sequence similarity with the 70-kilodalton precursor to
RT sulfatide/GM1 activator.";
RL Biochemistry 27:4557-4564(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=8573994;
RA Morales C.R., El-Alfy M., Zhao Q., Igdoura S.A.;
RT "Molecular role of sulfated glycoprotein-1 (SGP-1/prosaposin) in Sertoli
RT cells.";
RL Histol. Histopathol. 10:1023-1034(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=8601692; DOI=10.1177/44.4.8601692;
RA Morales C.R., El-Alfy M., Zhao Q., Igdoura S.A.;
RT "Expression and tissue distribution of rat sulfated glycoprotein-1
RT (prosaposin).";
RL J. Histochem. Cytochem. 44:327-337(1996).
RN [4]
RP PROTEIN SEQUENCE OF 68-78; 108-122; 192-212; 323-343; 444-445 AND 460-479,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: [Prosaposin]: Behaves as a myelinotrophic and neurotrophic
CC factor, these effects are mediated by its G-protein-coupled receptors,
CC GPR37 and GPR37L1, undergoing ligand-mediated internalization followed
CC by ERK phosphorylation signaling. {ECO:0000250|UniProtKB:Q61207}.
CC -!- FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of
CC glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and
CC galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-
CC C apparently acts by combining with the enzyme and acidic lipid to form
CC an activated complex, rather than by solubilizing the substrate.
CC {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside
CC sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-
CC galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-
CC galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex
CC with the substrates of the sphingolipid hydrolases.
CC {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase
CC activator (EC 3.1.4.12). {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposins are specific low-molecular mass non-enzymatic
CC proteins, they participate in the lysosomal degradation of
CC sphingolipids, which takes place by the sequential action of specific
CC hydrolases. {ECO:0000250|UniProtKB:P07602}.
CC -!- SUBUNIT: Saposin-B is a homodimer. Prosaposin exists as a roughly half-
CC half mixture of monomers and disulfide-linked dimers. Monomeric
CC prosaposin interacts (via C-terminus) with sortilin/SORT1, the
CC interaction is required for targeting to lysosomes. Interacts with GRN;
CC facilitates lysosomal delivery of progranulin from the extracellular
CC space and the biosynthetic pathway (By similarity).
CC {ECO:0000250|UniProtKB:P07602}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:8573994,
CC ECO:0000269|PubMed:8601692}.
CC -!- SUBCELLULAR LOCATION: [Prosaposin]: Secreted
CC {ECO:0000269|PubMed:3048385, ECO:0000269|PubMed:8573994,
CC ECO:0000269|PubMed:8601692}. Note=Secreted as a fully glycosylated 70
CC kDa protein composed of complex glycans.
CC {ECO:0000250|UniProtKB:Q61207}.
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DR EMBL; M19936; AAA42136.1; -; mRNA.
DR EMBL; S81353; AAB36042.2; -; mRNA.
DR EMBL; S81373; AAB36233.2; -; mRNA.
DR PIR; A28716; A28716.
DR RefSeq; NP_001177165.1; NM_001190236.1.
DR RefSeq; NP_037145.2; NM_013013.2.
DR AlphaFoldDB; P10960; -.
DR SMR; P10960; -.
DR BioGRID; 247556; 1.
DR STRING; 10116.ENSRNOP00000000696; -.
DR GlyGen; P10960; 4 sites.
DR iPTMnet; P10960; -.
DR PhosphoSitePlus; P10960; -.
DR jPOST; P10960; -.
DR PaxDb; P10960; -.
DR PRIDE; P10960; -.
DR GeneID; 25524; -.
DR KEGG; rno:25524; -.
DR UCSC; RGD:3423; rat.
DR CTD; 5660; -.
DR RGD; 3423; Psap.
DR eggNOG; KOG1340; Eukaryota.
DR InParanoid; P10960; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; P10960; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P10960; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016235; C:aggresome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:1905573; F:ganglioside GM1 binding; ISO:RGD.
DR GO; GO:1905574; F:ganglioside GM2 binding; ISO:RGD.
DR GO; GO:1905575; F:ganglioside GM3 binding; ISO:RGD.
DR GO; GO:1905577; F:ganglioside GP1c binding; ISO:RGD.
DR GO; GO:1905576; F:ganglioside GT1b binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030882; F:lipid antigen binding; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0006672; P:ceramide metabolic process; ISO:RGD.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0003335; P:corneocyte development; ISO:RGD.
DR GO; GO:1903575; P:cornified envelope assembly; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; ISO:RGD.
DR GO; GO:0006683; P:galactosylceramide catabolic process; ISO:RGD.
DR GO; GO:1905572; P:ganglioside GM1 transport to membrane; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0006678; P:glucosylceramide metabolic process; ISO:RGD.
DR GO; GO:0006664; P:glycolipid metabolic process; ISO:RGD.
DR GO; GO:0046836; P:glycolipid transport; NAS:RGD.
DR GO; GO:0070841; P:inclusion body assembly; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISO:RGD.
DR GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR GO; GO:0006643; P:membrane lipid metabolic process; ISO:RGD.
DR GO; GO:0060073; P:micturition; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0001865; P:NK T cell differentiation; ISO:RGD.
DR GO; GO:1903771; P:positive regulation of beta-galactosidase activity; ISO:RGD.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0060736; P:prostate gland growth; ISO:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISO:RGD.
DR GO; GO:0090659; P:walking behavior; ISO:RGD.
DR InterPro; IPR003119; SAP_A.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR008373; Saposin.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR021165; Saposin_chordata.
DR InterPro; IPR008139; SaposinB_dom.
DR Pfam; PF02199; SapA; 2.
DR Pfam; PF05184; SapB_1; 3.
DR Pfam; PF03489; SapB_2; 4.
DR PIRSF; PIRSF002431; Saposin; 1.
DR PRINTS; PR01797; SAPOSIN.
DR SMART; SM00162; SAPA; 2.
DR SMART; SM00741; SapB; 4.
DR SUPFAM; SSF47862; SSF47862; 3.
DR PROSITE; PS51110; SAP_A; 2.
DR PROSITE; PS50015; SAP_B; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lysosome;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT CHAIN 17..554
FT /note="Prosaposin"
FT /id="PRO_0000031629"
FT PROPEP 17..59
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434963"
FT CHAIN 60..142
FT /note="Saposin-A"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434964"
FT PROPEP 143..193
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434965"
FT CHAIN 194..273
FT /note="Saposin-B-Val"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434966"
FT CHAIN 194..272
FT /note="Saposin-B"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434967"
FT PROPEP 274..309
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434968"
FT CHAIN 310..?389
FT /note="Saposin-C"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434969"
FT PROPEP ?390..434
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434970"
FT CHAIN 435..516
FT /note="Saposin-D"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434971"
FT PROPEP 517..554
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434972"
FT DOMAIN 18..58
FT /note="Saposin A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 59..142
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 193..274
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 310..391
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 435..516
FT /note="Saposin B-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 518..554
FT /note="Saposin A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 63..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 66..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 94..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 197..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 200..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 229..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 314..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 317..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 345..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 439..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 442..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 470..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CONFLICT 115
FT /note="P -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="D -> E (in Ref. 2; AAB36042)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="I -> V (in Ref. 3; AAB36233)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="W -> R (in Ref. 3; AAB36233)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="S -> M (in Ref. 3; AAB36233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61124 MW; DFE3F3A3A0520C6B CRC64;
MYALALLASL LVTALTSPVQ DPKICSGGSA VVCRDVKTAV DCRAVKHCQQ MVWSKPTAKS
LPCDICKTVV TEAGNLLKDN ATEEEILHYL EKTCAWIHDS SLSASCKEVV DSYLPVILDM
IKGEMSNPGE VCSALNLCQS LQEYLAEQNQ RQLESNKIPE VDLARVVAPF MSNIPLLLYP
QDRPRSQPQP KANEDVCQDC MKLVTDIQTA VRTNSSFVQG LVDHVKEDCD RLGPGVSDIC
KNYVDQYSEV AVQMMMHMQP KEICVMVGFC DEVKRVPMRT LVPATEAIKN ILPALELTDP
YEQDVIQAQN VIFCQVCQLV MRKLSELIIN NATEELLIKG LSKACSLLPA PASTKCQEVL
VTFGPSLLDV LMHEVNPNFL CGVISLCSAN PNLVGTLEQP AAAIVSALPK EPAPPKQPEE
PKQSALRAHV PPQKNGGFCE VCKKLVIYLE HNLEKNSTKE EILAALEKGC SFLPDPYQKQ
CDEFVAEYEP LLLEILVEVM DPSFVCSKIG VCPSAYKLLL GTEKCVWGPG YWCQNSETAA
RCNAVDHCKR HVWN
