ERP1A_CAEEL
ID ERP1A_CAEEL Reviewed; 895 AA.
AC Q09216;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Putative endoplasmic reticulum metallopeptidase 1-A {ECO:0000250|UniProtKB:Q6UPR8};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-like protease {ECO:0000305};
GN ORFNames=B0495.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659 AND ASN-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659; ASN-702 AND ASN-758, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6UPR8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; FO080132; CCD61475.1; -; Genomic_DNA.
DR RefSeq; NP_495618.1; NM_063217.4.
DR AlphaFoldDB; Q09216; -.
DR SMR; Q09216; -.
DR STRING; 6239.B0495.7.1; -.
DR MEROPS; M28.A20; -.
DR iPTMnet; Q09216; -.
DR EPD; Q09216; -.
DR PaxDb; Q09216; -.
DR PeptideAtlas; Q09216; -.
DR PRIDE; Q09216; -.
DR EnsemblMetazoa; B0495.7.1; B0495.7.1; WBGene00015206.
DR GeneID; 174245; -.
DR KEGG; cel:CELE_B0495.7; -.
DR UCSC; B0495.7.1; c. elegans.
DR CTD; 174245; -.
DR WormBase; B0495.7; CE29550; WBGene00015206; -.
DR eggNOG; KOG2194; Eukaryota.
DR GeneTree; ENSGT00530000063839; -.
DR HOGENOM; CLU_007536_2_0_1; -.
DR InParanoid; Q09216; -.
DR OMA; YLTHKKC; -.
DR OrthoDB; 248924at2759; -.
DR PhylomeDB; Q09216; -.
DR PRO; PR:Q09216; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015206; Expressed in embryo and 7 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..895
FT /note="Putative endoplasmic reticulum metallopeptidase 1-A"
FT /id="PRO_0000065088"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..383
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..452
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 493..513
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..517
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 518..538
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 545..565
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..586
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 587..607
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 614..634
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..895
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 322
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 895 AA; 102122 MW; C0F3081A64E7AD1E CRC64;
MLRRRGGPNE LRDELNNSKN QPEDDQRTKR GRESIGFRHW IYFVLTVAIV YAGVVALHRK
MPAVRDGTSF EDFSEQRARV LLKQLTALGS RPSGSDNLEV KAFGMIQDRI GKIHSVVDEV
GVNRLESDVQ RPSGCFDLKF LSSFTLCYHK ITNVVVRIGP KKGPSGNSLL LNCHFDTMPD
TPGATDDAVA CTIMMDVLEV LAHSKTELEN DVVFLFNGAE ENFLQAAHGF INQHPWRHDI
RAFINLEGTG SGGREILFQA GPGNSWLLQT YLENAPHPFC SVLAQEIFQS GIIPSDTDFR
IFRDYGRISG LDIAYTKNGW FYHTEFDEEW RIEPGAIQRA GENVLAVVRA ILKSPYLEKP
ATFDEENRWV FYDVVGLFTV YYSVNVGKLL NYIACFATYF LVVLRIRNRL YSVGDLAIAF
KHHVVAFLAM VITMLLIIAF VVQMDLVMCW YKMPEIVGAL YVLPMLIAGA IVHSHYADNN
RIRNVEMVQY DTILLSFASI LFLMTFYNLS SAFYVLNNLI LPVFKDIIIW ALGLFGVIRR
VTPRVLFFTQ LFCFLPTFVF AAYAISQCVD FFVPVMGRLG NAINPEFIMG PLGLVIASGF
ILFVNNLFYI SRRMNYIIRL LFAIFALFIL VLITTKVGNP YEYSHENPRL RRIIALHANR
TIYDFEGHLT QKDNALFVHS LDYRGASDLP DHSFLQGSSA PNCTGVVDEY CRMPYYTAIH
ELFPPEQSLW VPVPSPVVLP YPIDLKLVSR HAMGENLNLT FEIRGGYDKM SLHVTPLNDY
DLLSWSFTDI DIKEFGRRQT YFVFMTYGHE APEVRRFWIL LKNKNGVAPD PEKHENIELS
VATHYAHGIY QDTETLRQLR AMISSRRQTP EQAVGWWRWG ITMVGGRSEI VVKIF
