SPRN_RAT
ID SPRN_RAT Reviewed; 147 AA.
AC Q5BIV7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Shadow of prion protein;
DE Short=Protein shadoo;
DE Flags: Precursor;
GN Name=Sprn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Almost exclusively expressed in brain, with weak
CC expression in lung and stomach. {ECO:0000269|PubMed:14527721}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPRN family. {ECO:0000305}.
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DR EMBL; AABR03003407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000520; CAG34290.1; -; Genomic_DNA.
DR RefSeq; NP_001027015.1; NM_001031845.1.
DR RefSeq; XP_006230635.1; XM_006230573.3.
DR AlphaFoldDB; Q5BIV7; -.
DR STRING; 10116.ENSRNOP00000025609; -.
DR GlyGen; Q5BIV7; 1 site.
DR PaxDb; Q5BIV7; -.
DR Ensembl; ENSRNOT00000116404; ENSRNOP00000094166; ENSRNOG00000067971.
DR GeneID; 541462; -.
DR KEGG; rno:541462; -.
DR UCSC; RGD:1561845; rat.
DR CTD; 503542; -.
DR RGD; 1561845; Sprn.
DR eggNOG; ENOG502SCEE; Eukaryota.
DR GeneTree; ENSGT00730000111694; -.
DR HOGENOM; CLU_1776846_0_0_1; -.
DR InParanoid; Q5BIV7; -.
DR OMA; MNWTAAT; -.
DR OrthoDB; 1621494at2759; -.
DR TreeFam; TF330766; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q5BIV7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018927; Expressed in frontal cortex and 13 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0003676; F:nucleic acid binding; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR InterPro; IPR029238; Shadoo.
DR PANTHER; PTHR28552; PTHR28552; 1.
DR Pfam; PF14999; Shadoo; 1.
PE 2: Evidence at transcript 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_5000096017"
FT PROPEP 123..147
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000320169"
FT REGION 26..46
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:0000255"
SQ SEQUENCE 147 AA; 14712 MW; 0B792178D75C65A3 CRC64;
MNWTTATCWA LLLATAFLCD SCSAKGGRGG ARGSARGVRG GARGASRVRV RPAPRYSSSL
RVAAAGAAAG AAAGVAAGLA TGSGWRRTSG PGELGLEDDE NGAMGGNGTD RGVYSYWAWT
SGSGSVHSPR ICLLLSGTLG ALELLRP