SAP_CHICK
ID SAP_CHICK Reviewed; 518 AA.
AC O13035;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Prosaposin;
DE AltName: Full=Proactivator polypeptide;
DE Contains:
DE RecName: Full=Saposin-A;
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 194-203.
RC TISSUE=Brain, and Liver;
RX PubMed=9461526; DOI=10.1042/bj3300321;
RA Azuma N., Seo H.-C., Lie O., Fu Q., Gould R.M., Hiraiwa M., Burt D.W.,
RA Paton I.R., Morrice D.R., O'Brien J.S., Kishimoto Y.;
RT "Cloning, expression and map assignment of chicken prosaposin.";
RL Biochem. J. 330:321-327(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Altman N., Horowitz M.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The lysosomal degradation of sphingolipids takes place by the
CC sequential action of specific hydrolases. Some of these enzymes require
CC specific low-molecular mass, non-enzymatic proteins: the sphingolipids
CC activator proteins (coproteins). {ECO:0000250|UniProtKB:P07602}.
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 -!- SUBUNIT: Saposin-B is a homodimer. {ECO:0000250|UniProtKB:P07602}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07602}.
CC -!- SUBCELLULAR LOCATION: [Prosaposin]: Secreted
CC {ECO:0000250|UniProtKB:Q61207}. Note=Secreted as a fully glycosylated
CC 70 kDa protein composed of complex glycans.
CC {ECO:0000250|UniProtKB:Q61207}.
CC -!- PTM: This precursor is proteolytically processed to 4 small peptides,
CC which are similar to each other and are sphingolipid hydrolase
CC activator proteins. {ECO:0000250}.
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DR EMBL; AB003471; BAA19914.1; -; mRNA.
DR EMBL; AF108656; AAF05899.1; -; mRNA.
DR RefSeq; NP_990142.1; NM_204811.2.
DR AlphaFoldDB; O13035; -.
DR SMR; O13035; -.
DR STRING; 9031.ENSGALP00000007593; -.
DR PaxDb; O13035; -.
DR GeneID; 395602; -.
DR KEGG; gga:395602; -.
DR CTD; 5660; -.
DR VEuPathDB; HostDB:geneid_395602; -.
DR eggNOG; KOG1340; Eukaryota.
DR InParanoid; O13035; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; O13035; -.
DR PRO; PR:O13035; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
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; 4.
DR PROSITE; PS51110; SAP_A; 2.
DR PROSITE; PS50015; SAP_B; 4.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gangliosidosis; Glycoprotein; Lipid metabolism; Lysosome;
KW Reference proteome; Repeat; Secreted; Signal; Sphingolipid metabolism.
FT SIGNAL 1..17
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT CHAIN 18..518
FT /note="Prosaposin"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434973"
FT PROPEP 18..60
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031630"
FT CHAIN 61..143
FT /note="Saposin-A"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031631"
FT PROPEP 144..193
FT /evidence="ECO:0000305|PubMed:9461526"
FT /id="PRO_0000031632"
FT CHAIN 194..276
FT /note="Saposin-B"
FT /evidence="ECO:0000269|PubMed:9461526"
FT /id="PRO_0000031633"
FT PROPEP 277..306
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031634"
FT CHAIN 307..387
FT /note="Saposin-C"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031635"
FT PROPEP 388..398
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031636"
FT CHAIN 399..479
FT /note="Saposin-D"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031637"
FT PROPEP 480..518
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000031638"
FT DOMAIN 19..59
FT /note="Saposin A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 60..143
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 193..277
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 307..388
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 399..480
FT /note="Saposin B-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 482..518
FT /note="Saposin A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT CARBOHYD 81
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 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 64..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 67..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 95..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 197..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 200..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 229..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 311..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 314..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 342..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 403..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 406..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 434..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CONFLICT 94
FT /note="R -> T (in Ref. 2; AAF05899)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="E -> D (in Ref. 2; AAF05899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57601 MW; B803000E891C3963 CRC64;
MARRLLTLLG LLAAAVASPV LWQKDCAKGP EVWCQSLRTA SQCGAVKHCQ QNVWSKPAVN
SIPCDLCKEL VTVVGKVLKD NGTEDEIRSY LEKRCEFLPD QGLASECKEI VDSYLPVIMD
MIKEEFDKPE VVCSALSLCQ SLQKHLAAMK LQKQLQSNKI PELDFSELTS PFMANVPLLL
YPQDKPKQKS KATEDVCQDC IRLVTDVQEA VRTNATFVKS LVAHAKEECD RLGPGMSDMC
KSYISEYSDL AIQMMMHMKD QQPKDICAMV GFCPSVKSVP LQTLVPAQVV HEVKMETVEK
ATVQEKTFSV CEICETMVKE VTGLLESNKT EEEIVHEMEV VCYLLPASVK DQCKDFIEVY
GQALIDMLLE ATNPEAVCVM LKCCAANKPP QQPVVVKPAG GFCDICKMIV AYADKELEKN
ATTTEIEALL EKVCHFLPES VSDQCVQFVE QYEPVVVQLL AEMMDPTFVC TKLGVCGAAK
KPLLGEDACV WGPGYWCKNM ETAAQCNAVD HCRRHVWN
