SPRN_MOUSE
ID SPRN_MOUSE Reviewed; 147 AA.
AC Q8BWU1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Shadow of prion protein;
DE Short=Protein shadoo;
DE Flags: Precursor;
GN Name=Sprn; Synonyms=Gm169;
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 [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=14527721; DOI=10.1016/s0378-1119(03)00707-8;
RA Premzl M., Sangiorgio L., Strumbo B., Marshall Graves J.A., Simonic T.,
RA Gready J.E.;
RT "Shadoo, a new protein highly conserved from fish to mammals and with
RT similarity to prion protein.";
RL Gene 314:89-102(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 [4]
RP IDENTIFICATION.
RX PubMed=17199895; DOI=10.1186/1471-2164-8-1;
RA Premzl M., Gamulin V.;
RT "Comparative genomic analysis of prion genes.";
RL BMC Genomics 8:1-1(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, GLYCOSYLATION, AND GPI-ANCHOR.
RX PubMed=17703189; DOI=10.1038/sj.emboj.7601830;
RA Watts J.C., Drisaldi B., Ng V., Yang J., Strome B., Horne P., Sy M.-S.,
RA Yoong L., Young R., Mastrangelo P., Bergeron C., Fraser P.E., Carlson G.A.,
RA Mount H.T.J., Schmitt-Ulms G., Westaway D.;
RT "The CNS glycoprotein Shadoo has PrP(C)-like protective properties and
RT displays reduced levels in prion infections.";
RL EMBO J. 26:4038-4050(2007).
CC -!- FUNCTION: Prion-like protein that has PrP(C)-like neuroprotective
CC activity. May act as a modulator for the biological actions of normal
CC and abnormal PrP. {ECO:0000269|PubMed:17703189}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17703189};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17703189}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain (at protein level). In
CC brain, it is highly expressed in the hippocampus and cerebellum and is
CC also expressed at lower level in other areas of the brain including the
CC cerebral cortex, the thalamus and the medulla. In hippocampus and
CC cerebellum it is highly expressed in the cell bodies of pyramidal cells
CC and Purkinje cells, respectively. {ECO:0000269|PubMed:17703189}.
CC -!- DEVELOPMENTAL STAGE: Appears at embryonic day 16 and persists in early
CC postnatal life and in the brains of adults (at protein level).
CC {ECO:0000269|PubMed:17703189}.
CC -!- INDUCTION: Strongly down-regulated in prion-infected brains (at protein
CC level). {ECO:0000269|PubMed:17703189}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17703189}.
CC -!- MISCELLANEOUS: This protein is a candidate for 'Pi' factor, a PrP(C)-
CC like protein able to compensate for the absence of PrPC in mice lacking
CC Prnp.
CC -!- SIMILARITY: Belongs to the SPRN family. {ECO:0000305}.
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DR EMBL; AJ621426; CAF18554.1; -; mRNA.
DR EMBL; AK049995; BAC34022.1; -; mRNA.
DR EMBL; BC056484; AAH56484.1; -; mRNA.
DR EMBL; BN000519; CAG34289.1; -; Genomic_DNA.
DR CCDS; CCDS21966.1; -.
DR RefSeq; NP_898970.1; NM_183147.2.
DR AlphaFoldDB; Q8BWU1; -.
DR STRING; 10090.ENSMUSP00000053901; -.
DR GlyGen; Q8BWU1; 1 site.
DR iPTMnet; Q8BWU1; -.
DR PhosphoSitePlus; Q8BWU1; -.
DR PaxDb; Q8BWU1; -.
DR PRIDE; Q8BWU1; -.
DR ProteomicsDB; 263329; -.
DR Antibodypedia; 55899; 103 antibodies from 15 providers.
DR DNASU; 212518; -.
DR Ensembl; ENSMUST00000059241; ENSMUSP00000053901; ENSMUSG00000045733.
DR GeneID; 212518; -.
DR KEGG; mmu:212518; -.
DR UCSC; uc009khe.1; mouse.
DR CTD; 503542; -.
DR MGI; MGI:3582583; Sprn.
DR VEuPathDB; HostDB:ENSMUSG00000045733; -.
DR eggNOG; ENOG502SCEE; Eukaryota.
DR GeneTree; ENSGT00730000111694; -.
DR HOGENOM; CLU_1776846_0_0_1; -.
DR InParanoid; Q8BWU1; -.
DR OMA; MNWTAAT; -.
DR OrthoDB; 1621494at2759; -.
DR PhylomeDB; Q8BWU1; -.
DR TreeFam; TF330766; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 212518; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sprn; mouse.
DR PRO; PR:Q8BWU1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BWU1; protein.
DR Bgee; ENSMUSG00000045733; Expressed in dentate gyrus of hippocampal formation granule cell and 84 other tissues.
DR ExpressionAtlas; Q8BWU1; baseline and differential.
DR Genevisible; Q8BWU1; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR InterPro; IPR029238; Shadoo.
DR PANTHER; PTHR28552; PTHR28552; 1.
DR Pfam; PF14999; Shadoo; 1.
PE 1: Evidence at protein level;
KW Amyloid; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Prion; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..122
FT /note="Shadow of prion protein"
FT /id="PRO_0000320167"
FT PROPEP 123..147
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000320168"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 122
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:17703189"
SQ SEQUENCE 147 AA; 14591 MW; 94B8943C916D96C6 CRC64;
MNWTAATCWA LLLAAAFLCD SCSAKGGRGG ARGSARGVRG GARGASRVRV RPAPRYGSSL
RVAAAGAAAG AAAGVAAGLA TGSGWRRTSG PGELGLEDDE NGAMGGNGTD RGVYSYWAWT
SGSGSVHSPR ICLLLGGTLG ALELLRP
