ID Q5BJH1_HUMAN Unreviewed; 240 AA. AC Q5BJH1; DT 12-APR-2005, integrated into UniProtKB/TrEMBL. DT 12-APR-2005, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Prosaposin {ECO:0000256|ARBA:ARBA00040265}; GN Name=PSAP {ECO:0000313|EMBL:AAH91483.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAH91483.1}; RN [1] {ECO:0000313|EMBL:AAH91483.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Peripheral Nervous System {ECO:0000313|EMBL:AAH91483.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [4] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). 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:0000256|ARBA:ARBA00037150}. 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:0000256|ARBA:ARBA00037606}. CC -!- FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase CC activator (EC 3.1.4.12). {ECO:0000256|ARBA:ARBA00037231}. CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC091483; AAH91483.1; -; mRNA. DR AlphaFoldDB; Q5BJH1; -. DR SMR; Q5BJH1; -. DR IntAct; Q5BJH1; 2. DR MassIVE; Q5BJH1; -. DR MaxQB; Q5BJH1; -. DR ProteomicsDB; 62690; -. DR Antibodypedia; 1388; 561 antibodies from 35 providers. DR UCSC; uc057twu.1; human. DR VEuPathDB; HostDB:ENSG00000197746; -. DR HOGENOM; CLU_1192198_0_0_1; -. DR ChiTaRS; PSAP; human. DR Bgee; ENSG00000197746; Expressed in monocyte and 211 other cell types or tissues. DR ExpressionAtlas; Q5BJH1; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro. DR Gene3D; 1.10.225.10; Saposin-like; 2. 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; IPR008139; SaposinB_dom. DR PANTHER; PTHR11480:SF36; PROSAPOSIN; 1. DR PANTHER; PTHR11480; SAPOSIN-RELATED; 1. DR Pfam; PF02199; SapA; 2. DR Pfam; PF05184; SapB_1; 2. DR Pfam; PF03489; SapB_2; 1. DR PRINTS; PR01797; SAPOSIN. DR SMART; SM00162; SAPA; 2. DR SMART; SM00741; SapB; 2. DR SUPFAM; SSF47862; Saposin; 2. DR PROSITE; PS51110; SAP_A; 2. DR PROSITE; PS50015; SAP_B; 1. PE 1: Evidence at protein level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. SQ SEQUENCE 240 AA; 26309 MW; 19E645E7952E5AB6 CRC64; MYALFLLASL LGAALAGPVL GLKECTRGSA VWCQNVKTAS DCGAVKHCLQ TVWNKPTVKS LPCDICKDVV TAAGDMLKDN ATEEEILVYL EVSPELVCSM LHLCSGTRLP ALTVHVTQPK DGGFCEVCKK LVGYLDRNLE KNSTKQEILA ALEKGCSFLP DPYQKQCDQF VAEYEPVLIE ILVEVMDPSF VCLKIGACPS AHKPLLGTEK CIWGPSYWCQ NTETAAQCNA VEHCKRHVWN //