SAPL1_MOUSE
ID SAPL1_MOUSE Reviewed; 522 AA.
AC Q8C1C1; Q8BJV5; Q8C1N0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Proactivator polypeptide-like 1;
DE Contains:
DE RecName: Full=Saposin A-like;
DE Contains:
DE RecName: Full=Saposin B-Val-like;
DE Contains:
DE RecName: Full=Saposin B-like;
DE Contains:
DE RecName: Full=Saposin C-like;
DE Contains:
DE RecName: Full=Saposin D-like;
DE Flags: Precursor;
GN Name=Psapl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, Skin, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-312.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
CC -!- FUNCTION: May activate the lysosomal degradation of sphingolipids.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25258.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25961.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC37363.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009408; BAC25258.1; ALT_FRAME; mRNA.
DR EMBL; AK028455; BAC25961.1; ALT_INIT; mRNA.
DR EMBL; AK078699; BAC37363.1; ALT_SEQ; mRNA.
DR RefSeq; NP_780458.2; NM_175249.3.
DR AlphaFoldDB; Q8C1C1; -.
DR SMR; Q8C1C1; -.
DR STRING; 10090.ENSMUSP00000100594; -.
DR GlyGen; Q8C1C1; 2 sites.
DR iPTMnet; Q8C1C1; -.
DR PhosphoSitePlus; Q8C1C1; -.
DR CPTAC; non-CPTAC-4003; -.
DR MaxQB; Q8C1C1; -.
DR PaxDb; Q8C1C1; -.
DR PeptideAtlas; Q8C1C1; -.
DR PRIDE; Q8C1C1; -.
DR ProteomicsDB; 256834; -.
DR DNASU; 76943; -.
DR GeneID; 76943; -.
DR KEGG; mmu:76943; -.
DR UCSC; uc008xem.1; mouse.
DR CTD; 768239; -.
DR MGI; MGI:1924193; Psapl1.
DR eggNOG; KOG1340; Eukaryota.
DR InParanoid; Q8C1C1; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; Q8C1C1; -.
DR TreeFam; TF316942; -.
DR BioGRID-ORCS; 76943; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Psapl1; mouse.
DR PRO; PR:Q8C1C1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C1C1; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IBA:GO_Central.
DR GO; GO:0060736; P:prostate gland growth; 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; 1.
DR Pfam; PF03489; SapB_2; 2.
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 Disulfide bond; Glycoprotein; Lipid metabolism; Reference proteome; Repeat;
KW Secreted; Signal; Sphingolipid metabolism.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..59
FT /evidence="ECO:0000250"
FT /id="PRO_0000280315"
FT CHAIN 61..144
FT /note="Saposin A-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280316"
FT PROPEP 146..183
FT /evidence="ECO:0000250"
FT /id="PRO_0000280317"
FT CHAIN 184..260
FT /note="Saposin B-Val-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280318"
FT CHAIN 184..259
FT /note="Saposin B-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280319"
FT PROPEP 261..290
FT /evidence="ECO:0000250"
FT /id="PRO_0000280320"
FT CHAIN 291..370
FT /note="Saposin C-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280321"
FT PROPEP 371..392
FT /evidence="ECO:0000250"
FT /id="PRO_0000280322"
FT CHAIN 393..474
FT /note="Saposin D-like"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280323"
FT PROPEP 475..522
FT /evidence="ECO:0000250"
FT /id="PRO_0000280324"
FT DOMAIN 19..59
FT /note="Saposin A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 60..144
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 183..261
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 291..371
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 393..474
FT /note="Saposin B-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 476..516
FT /note="Saposin A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:16170054"
FT DISULFID 64..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 67..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 95..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 187..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 190..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 216..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 295..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 298..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 326..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 397..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 400..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 428..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CONFLICT 293
FT /note="L -> Q (in Ref. 1; BAC37363)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="P -> T (in Ref. 1; BAC37363)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="Q -> H (in Ref. 1; BAC37363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57061 MW; 374F7E914CB9EC7A CRC64;
MLCALILWSG LLGAARASPI SVPRECAKGS EVWCQDLQAA AKCRAVRHCQ SAVWNKPTVK
SLPCSVCQDV AAAAGNGVNP GATESDILTS VMKTCEWLPS QESSAKCKWM VNNHSAAVLS
MLSGAQETDL ASVCTALTLC EPLQRHLAET TSERPLTQED ANEVMAPFLS NGALSFHPSQ
MPEGAVCHDC VQLISLLQDA LESNLTLAEV TVQNQCQSMG PGLAALCENY IHRQFVPAKQ
TLQGLPPQEV CRKGGFCERE SAHWLTRVAA VDGVPSLEME MPRTNELQMQ LGLTCDVCLN
LVQELDKWLV TNSTEALISH TLERVCTVVP EPLVQQCITL VDTYSPELVQ LMSKVTPEKV
CETIKLCGSK RRARSISRAV ATTPSLPVDE ENQGSFCQGC KRLLGMSSQN LDHKSTKRDI
LNAFKGGCRI LPLPYVMQCN RFVAEYEPVL IESLKFMMNP TDLCKKMGAC HGPKTPLLGT
DQCVMGPSFW CKSPEAAEMC NALEHCQRLV WKKPVSKINE QP
