EPDR1_MOUSE
ID EPDR1_MOUSE Reviewed; 224 AA.
AC Q99M71; Q06BK9; Q8BQY1; Q8CAI2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mammalian ependymin-related protein 1;
DE Short=MERP-1 {ECO:0000303|PubMed:11749721};
DE Flags: Precursor;
GN Name=Epdr1; Synonyms=Epdr2, Merp1, Merp2;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11749721; DOI=10.1089/104454901753340613;
RA Apostolopoulos J., Sparrow R.L., McLeod J.L., Collier F.M., Darcy P.K.,
RA Slater H.R., Ngu C., Gregorio-King C.C., Kirkland M.A.;
RT "Identification and characterization of a novel family of mammalian
RT ependymin-related proteins (MERPs) in hematopoietic, nonhematopoietic, and
RT malignant tissues.";
RL DNA Cell Biol. 20:625-635(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Gregorio-King C.C., Collier F.M., Elliott K.L., Kirkland M.A.;
RT "Characterization of mammalian ependymin proteins.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Diencephalon, and Hypothalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=16954209; DOI=10.1074/jbc.m606208200;
RA Della Valle M.C., Sleat D.E., Sohar I., Wen T., Pintar J.E., Jadot M.,
RA Lobel P.;
RT "Demonstration of lysosomal localization for the mammalian ependymin-
RT related protein using classical approaches combined with a novel density
RT shift method.";
RL J. Biol. Chem. 281:35436-35445(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds anionic lipids and gangliosides at acidic pH.
CC {ECO:0000250|UniProtKB:Q9UM22}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UM22}.
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:16954209}.
CC Secreted {ECO:0000250|UniProtKB:Q9UM22}. Note=Lysosomal and also
CC secreted. {ECO:0000250|UniProtKB:Q9UM22}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99M71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99M71-2; Sequence=VSP_031977;
CC -!- TISSUE SPECIFICITY: Detected in brain, small intestine and in soleus,
CC extensor digitorum longus and white gastrocnemius (at protein level)
CC (PubMed:16954209). Detected in brain and skeletal muscle, and at lower
CC leavels in heart (PubMed:11749721). {ECO:0000269|PubMed:11749721,
CC ECO:0000269|PubMed:16954209}.
CC -!- PTM: N-glycosylated; the glycan contains mannose-6-phosphate moieties.
CC {ECO:0000269|PubMed:16954209}.
CC -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
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DR EMBL; AY028709; AAK29146.1; -; Genomic_DNA.
DR EMBL; AF353717; AAK51799.1; -; mRNA.
DR EMBL; DQ914440; ABI84107.1; -; mRNA.
DR EMBL; AK034083; BAC28576.1; -; mRNA.
DR EMBL; AK038733; BAC30113.1; -; mRNA.
DR EMBL; AK046185; BAC32624.1; -; mRNA.
DR EMBL; AK160413; BAE35778.1; -; mRNA.
DR EMBL; BC014708; AAH14708.1; -; mRNA.
DR CCDS; CCDS26260.1; -. [Q99M71-1]
DR RefSeq; NP_598826.3; NM_134065.4. [Q99M71-1]
DR PDB; 6JLA; X-ray; 2.40 A; A/B/C/D=38-224.
DR PDBsum; 6JLA; -.
DR AlphaFoldDB; Q99M71; -.
DR SMR; Q99M71; -.
DR BioGRID; 222817; 10.
DR STRING; 10090.ENSMUSP00000002885; -.
DR GlyConnect; 2502; 8 N-Linked glycans (1 site).
DR GlyGen; Q99M71; 2 sites, 8 N-linked glycans (1 site).
DR PhosphoSitePlus; Q99M71; -.
DR MaxQB; Q99M71; -.
DR PaxDb; Q99M71; -.
DR PeptideAtlas; Q99M71; -.
DR PRIDE; Q99M71; -.
DR ProteomicsDB; 275932; -. [Q99M71-1]
DR ProteomicsDB; 275933; -. [Q99M71-2]
DR Antibodypedia; 34976; 185 antibodies from 19 providers.
DR DNASU; 105298; -.
DR Ensembl; ENSMUST00000002885; ENSMUSP00000002885; ENSMUSG00000002808. [Q99M71-1]
DR Ensembl; ENSMUST00000221014; ENSMUSP00000152111; ENSMUSG00000002808. [Q99M71-2]
DR GeneID; 105298; -.
DR KEGG; mmu:105298; -.
DR UCSC; uc007ppe.2; mouse. [Q99M71-1]
DR CTD; 54749; -.
DR MGI; MGI:2145369; Epdr1.
DR VEuPathDB; HostDB:ENSMUSG00000002808; -.
DR eggNOG; ENOG502QQ8T; Eukaryota.
DR GeneTree; ENSGT00940000161910; -.
DR HOGENOM; CLU_097673_0_0_1; -.
DR InParanoid; Q99M71; -.
DR OMA; WVVYDHS; -.
DR OrthoDB; 1284695at2759; -.
DR PhylomeDB; Q99M71; -.
DR TreeFam; TF328581; -.
DR BioGRID-ORCS; 105298; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Epdr1; mouse.
DR PRO; PR:Q99M71; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99M71; protein.
DR Bgee; ENSMUSG00000002808; Expressed in sciatic nerve and 236 other tissues.
DR ExpressionAtlas; Q99M71; baseline and differential.
DR Genevisible; Q99M71; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:1905573; F:ganglioside GM1 binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:1990764; P:myofibroblast contraction; ISO:MGI.
DR InterPro; IPR001299; Ependymin.
DR PANTHER; PTHR10697; PTHR10697; 1.
DR Pfam; PF00811; Ependymin; 1.
DR PRINTS; PR00317; EPENDYMIN.
DR SMART; SM00026; EPEND; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Lipid-binding; Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..224
FT /note="Mammalian ependymin-related protein 1"
FT /id="PRO_0000322976"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..172
FT /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT DISULFID 88..222
FT /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT DISULFID 113..210
FT /evidence="ECO:0000250|UniProtKB:Q9UM22"
FT VAR_SEQ 91..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_031977"
FT CONFLICT 122
FT /note="W -> S (in Ref. 3; BAC32624)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="G -> S (in Ref. 3; BAC30113)"
FT /evidence="ECO:0000305"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:6JLA"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:6JLA"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6JLA"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6JLA"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6JLA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6JLA"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:6JLA"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6JLA"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6JLA"
SQ SEQUENCE 224 AA; 25485 MW; D49BAC79CB1C57BB CRC64;
MPARAPRRLV QGPRGTWLLG SLWVWVLCGL GMAGSLGTPQ PCQAPQQWEG RQVLYQQSSG
HNNRALVSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKE GVMFQIEQAT KQCAKIPLVE
SWDPLDIPQN STFEDQYSIG GPQEQILVQE WSDRRTARSY ETWIGVYTAK DCYPVQETFI
RNYTVVMSTR FFDVQLGIKD PSVFTPPSTC QAAQPEKMSD GCSL
