ID   SAP_CAVPO               Reviewed;          81 AA.
AC   P20097;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Saposin-C;
DE   AltName: Full=Co-beta-glucosidase;
DE   AltName: Full=Glucosylceramidase activator;
DE   AltName: Full=Sphingolipid activator protein 2;
DE            Short=SAP-2;
GN   Name=PSAP;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=3198642; DOI=10.1016/s0021-9258(19)77678-9;
RA   Sano A., Radin N.S., Johnson L.L., Tarr G.E.;
RT   "The activator protein for glucosylceramide beta-glucosidase from guinea
RT   pig liver. Improved isolation method and complete amino acid sequence.";
RL   J. Biol. Chem. 263:19597-19601(1988).
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.
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DR   PIR; A32026; A32026.
DR   AlphaFoldDB; P20097; -.
DR   SMR; P20097; -.
DR   STRING; 10141.ENSCPOP00000001595; -.
DR   eggNOG; KOG1340; Eukaryota.
DR   HOGENOM; CLU_2579898_0_0_1; -.
DR   InParanoid; P20097; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR008373; Saposin.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR01797; SAPOSIN.
DR   SMART; SM00741; SapB; 1.
DR   SUPFAM; SSF47862; SSF47862; 1.
DR   PROSITE; PS50015; SAP_B; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid metabolism;
KW   Reference proteome; Sphingolipid metabolism.
FT   CHAIN           1..81
FT                   /note="Saposin-C"
FT                   /id="PRO_0000175239"
FT   DOMAIN          1..81
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        5..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        8..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        36..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ   SEQUENCE   81 AA;  8852 MW;  E564CE1F0A292596 CRC64;
     ESVTCKACEY VVKKVMELID NNRTEEKIIH ALDSVCALLP ESVSEVCQEV VDTYGDSIVA
     LLLQEMSPEL VCSELGLCMS G