EPDR1_HUMAN
ID EPDR1_HUMAN Reviewed; 224 AA.
AC Q9UM22; A8K4C0; C9JYS3; Q06BL0; Q99M77;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Mammalian ependymin-related protein 1;
DE Short=MERP-1 {ECO:0000303|PubMed:11749721};
DE AltName: Full=Upregulated in colorectal cancer gene 1 protein;
DE Flags: Precursor;
GN Name=EPDR1; Synonyms=MERP1, UCC1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
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] (ISOFORMS 1 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-224 (ISOFORM 1).
RA Nimmrich I., Erdmann S., Melchers U.;
RT "Genes that are differentially expressed in colon cancer.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 38-224, SUBUNIT, SUBCELLULAR
RP LOCATION, GLYCOSYLATION AT ASN-130, AND DISULFIDE BOND.
RX PubMed=30729188; DOI=10.1038/s42003-018-0262-9;
RA Wei Y., Xiong Z.J., Li J., Zou C., Cairo C.W., Klassen J.S., Prive G.G.;
RT "Crystal structures of human lysosomal EPDR1 reveal homology with the
RT superfamily of bacterial lipoprotein transporters.";
RL Commun. Biol. 2:52-52(2019).
CC -!- FUNCTION: Binds anionic lipids and gangliosides at acidic pH.
CC {ECO:0000269|PubMed:30729188}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30729188}.
CC -!- INTERACTION:
CC Q9UM22; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-946972, EBI-10173507;
CC Q9UM22; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-946972, EBI-744366;
CC Q9UM22; P49639: HOXA1; NbExp=3; IntAct=EBI-946972, EBI-740785;
CC Q9UM22; P24592: IGFBP6; NbExp=3; IntAct=EBI-946972, EBI-947015;
CC Q9UM22; Q15323: KRT31; NbExp=3; IntAct=EBI-946972, EBI-948001;
CC Q9UM22; O76011: KRT34; NbExp=3; IntAct=EBI-946972, EBI-1047093;
CC Q9UM22; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-946972, EBI-10171774;
CC Q9UM22; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-946972, EBI-11953846;
CC Q9UM22; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-946972, EBI-10302392;
CC Q9UM22; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-946972, EBI-11339910;
CC Q9UM22; Q63HR2: TNS2; NbExp=3; IntAct=EBI-946972, EBI-949753;
CC Q9UM22; Q15654: TRIP6; NbExp=3; IntAct=EBI-946972, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:30729188}.
CC Secreted {ECO:0000269|PubMed:30729188}. Note=Lysosomal and also
CC secreted. {ECO:0000269|PubMed:30729188}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UM22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UM22-2; Sequence=VSP_031976;
CC Name=3;
CC IsoId=Q9UM22-3; Sequence=VSP_046829;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, heart, skeletal
CC muscle, kidney, testis, ovary and prostate.
CC {ECO:0000269|PubMed:11749721}.
CC -!- PTM: N-glycosylated; the glycan contains mannose-6-phosphate moieties.
CC {ECO:0000250|UniProtKB:Q99M71}.
CC -!- SIMILARITY: Belongs to the ependymin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00686.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB60269.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF361252; AAK26441.1; -; Genomic_DNA.
DR EMBL; AY027861; AAK15787.1; -; mRNA.
DR EMBL; DQ914439; ABI84106.1; -; mRNA.
DR EMBL; AK290885; BAF83574.1; -; mRNA.
DR EMBL; AK309180; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC018634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW94086.1; -; Genomic_DNA.
DR EMBL; BC000686; AAH00686.2; ALT_INIT; mRNA.
DR EMBL; BC018299; AAH18299.1; -; mRNA.
DR EMBL; AJ250475; CAB60269.1; ALT_INIT; mRNA.
DR CCDS; CCDS5454.2; -. [Q9UM22-1]
DR CCDS; CCDS59051.1; -. [Q9UM22-2]
DR CCDS; CCDS59052.1; -. [Q9UM22-3]
DR RefSeq; NP_001229875.2; NM_001242946.1. [Q9UM22-2]
DR RefSeq; NP_001229877.1; NM_001242948.1. [Q9UM22-3]
DR RefSeq; NP_060019.2; NM_017549.4. [Q9UM22-1]
DR PDB; 6E7O; X-ray; 3.00 A; A/B/C/D=38-224.
DR PDB; 6E8N; X-ray; 3.20 A; A/B=38-224.
DR PDB; 6JLD; X-ray; 2.00 A; A/B/C/D=38-224.
DR PDBsum; 6E7O; -.
DR PDBsum; 6E8N; -.
DR PDBsum; 6JLD; -.
DR AlphaFoldDB; Q9UM22; -.
DR SMR; Q9UM22; -.
DR BioGRID; 120127; 87.
DR IntAct; Q9UM22; 27.
DR STRING; 9606.ENSP00000199448; -.
DR GlyGen; Q9UM22; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UM22; -.
DR MetOSite; Q9UM22; -.
DR PhosphoSitePlus; Q9UM22; -.
DR BioMuta; EPDR1; -.
DR DMDM; 13124620; -.
DR EPD; Q9UM22; -.
DR jPOST; Q9UM22; -.
DR MassIVE; Q9UM22; -.
DR MaxQB; Q9UM22; -.
DR PaxDb; Q9UM22; -.
DR PeptideAtlas; Q9UM22; -.
DR PRIDE; Q9UM22; -.
DR ProteomicsDB; 12296; -.
DR ProteomicsDB; 85173; -. [Q9UM22-1]
DR ProteomicsDB; 85174; -. [Q9UM22-2]
DR Antibodypedia; 34976; 185 antibodies from 19 providers.
DR DNASU; 54749; -.
DR Ensembl; ENST00000199448.9; ENSP00000199448.4; ENSG00000086289.12. [Q9UM22-1]
DR Ensembl; ENST00000423717.1; ENSP00000409211.1; ENSG00000086289.12. [Q9UM22-2]
DR Ensembl; ENST00000425345.1; ENSP00000413359.1; ENSG00000086289.12. [Q9UM22-3]
DR GeneID; 54749; -.
DR KEGG; hsa:54749; -.
DR MANE-Select; ENST00000199448.9; ENSP00000199448.4; NM_017549.5; NP_060019.2.
DR UCSC; uc003tfp.5; human. [Q9UM22-1]
DR CTD; 54749; -.
DR DisGeNET; 54749; -.
DR GeneCards; EPDR1; -.
DR HGNC; HGNC:17572; EPDR1.
DR HPA; ENSG00000086289; Tissue enhanced (brain, skeletal muscle).
DR MIM; 619734; gene.
DR neXtProt; NX_Q9UM22; -.
DR OpenTargets; ENSG00000086289; -.
DR PharmGKB; PA142671908; -.
DR VEuPathDB; HostDB:ENSG00000086289; -.
DR eggNOG; ENOG502QQ8T; Eukaryota.
DR GeneTree; ENSGT00940000164413; -.
DR HOGENOM; CLU_097673_0_0_1; -.
DR InParanoid; Q9UM22; -.
DR OMA; WVVYDHS; -.
DR PhylomeDB; Q9UM22; -.
DR PathwayCommons; Q9UM22; -.
DR SignaLink; Q9UM22; -.
DR BioGRID-ORCS; 54749; 7 hits in 1056 CRISPR screens.
DR ChiTaRS; EPDR1; human.
DR GenomeRNAi; 54749; -.
DR Pharos; Q9UM22; Tbio.
DR PRO; PR:Q9UM22; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UM22; protein.
DR Bgee; ENSG00000086289; Expressed in pons and 174 other tissues.
DR ExpressionAtlas; Q9UM22; baseline and differential.
DR Genevisible; Q9UM22; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:1905573; F:ganglioside GM1 binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IPI:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:1990764; P:myofibroblast contraction; IMP:UniProtKB.
DR InterPro; IPR001299; Ependymin.
DR InterPro; IPR018224; Ependymin_CS.
DR PANTHER; PTHR10697; PTHR10697; 1.
DR Pfam; PF00811; Ependymin; 1.
DR PRINTS; PR00317; EPENDYMIN.
DR SMART; SM00026; EPEND; 1.
DR PROSITE; PS00898; EPENDYMIN_1; 1.
DR PROSITE; PS00899; EPENDYMIN_2; 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_0000008351"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:30729188"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..172
FT /evidence="ECO:0000269|PubMed:30729188"
FT DISULFID 88..222
FT /evidence="ECO:0000269|PubMed:30729188"
FT DISULFID 113..210
FT /evidence="ECO:0000269|PubMed:30729188"
FT VAR_SEQ 1..89
FT /note="MPGRAPLRTVPGALGAWLLGGLWAWTLCGLCSLGAVGAPRPCQAPQQWEGRQ
FT VMYQQSSGRNSRALLSYDGLNQRVRVLDERKALIPCK -> MVRDWEGRCAHRGRPAGG
FT GLSNTQRGGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046829"
FT VAR_SEQ 91..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_031976"
FT CONFLICT 207
FT /note="P -> S (in Ref. 7; CAB60269)"
FT /evidence="ECO:0000305"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6E8N"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6JLD"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:6E8N"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6JLD"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 184..197
FT /evidence="ECO:0007829|PDB:6JLD"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6JLD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6JLD"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6JLD"
SQ SEQUENCE 224 AA; 25437 MW; 84ADBA3666261611 CRC64;
MPGRAPLRTV PGALGAWLLG GLWAWTLCGL CSLGAVGAPR PCQAPQQWEG RQVMYQQSSG
RNSRALLSYD GLNQRVRVLD ERKALIPCKR LFEYILLYKD GVMFQIDQAT KQCSKMTLTQ
PWDPLDIPQN STFEDQYSIG GPQEQITVQE WSDRKSARSY ETWIGIYTVK DCYPVQETFT
INYSVILSTR FFDIQLGIKD PSVFTPPSTC QMAQLEKMSE DCSW
