ERMP1_XENLA
ID ERMP1_XENLA Reviewed; 876 AA.
AC Q0VGW4; Q2VPF2; Q7SXS0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Endoplasmic reticulum metallopeptidase 1 {ECO:0000250|UniProtKB:Q6UPR8};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-like protease {ECO:0000305};
GN Name=ermp1 {ECO:0000250|UniProtKB:Q7Z2K6};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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; BC055270; AAH55270.1; -; mRNA.
DR EMBL; BC080427; AAH80427.1; -; mRNA.
DR EMBL; BC108865; AAI08866.1; -; mRNA.
DR RefSeq; NP_001082713.1; NM_001089244.1.
DR AlphaFoldDB; Q0VGW4; -.
DR SMR; Q0VGW4; -.
DR GeneID; 398673; -.
DR KEGG; xla:398673; -.
DR CTD; 398673; -.
DR Xenbase; XB-GENE-984736; ermp1.L.
DR OrthoDB; 248924at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398673; Expressed in stomach and 19 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; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..876
FT /note="Endoplasmic reticulum metallopeptidase 1"
FT /id="PRO_0000259495"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..381
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 382..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 428..448
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..462
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 463..483
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 495..515
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..519
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 520..540
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 556..576
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..593
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 594..614
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 624..644
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..876
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 178
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 190
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 190
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 225
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 251
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 327
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 326
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 177..195
FT /evidence="ECO:0000250"
SQ SEQUENCE 876 AA; 97793 MW; DA8BD4587D434A12 CRC64;
MESTVDGLTI RRPRYNVSAE SASGYRREAG VREEKKPRQR DAGFGAAVPV LLLLYVLSVR
GLVHISLRQL VTPGGHSTGF NASTAREYLQ QITSIDSRTA GSPENEIIAV NYLLGKIKDI
EEKINSVHRI TVDVQRPTGT FSIDFLGGFT SYYDNITNIA VKLEPEHRAE HAVLANCHFD
TVANTPGASD DAVSCAVMLE ILGSLSSSSK PLKHAIIFLF NGAEENILQG SHGFITQHPW
AKMVRAFINL EAAGVGGKEL VFQTGPENPW LVQAYASAAV HPFASVVAQE VFQSGIIPSD
TDFRIYRDFG NIPGIDLAFI ENGYIYHTKY DTWDRILTES IQRAGDNILG VLHYLATSSQ
LAESSQFRHG NMVFFDVCGL FVLSYPARLG TIINYITAAV TLFYISKKMI KYKQGGTNYV
RDLVYGLIIT LVSWVSALVT VLIIAVLVSL AGKALSWYTH FYVSIFLYGS AAVAKFILVH
SLAKTYFFAG ASSQYLGDLF FDISLITWCI PLVLLTQSGL CSAYFFAAWI IFPLLTKLLL
QPDIIHQGSP YKFTAVYLLG LFPPYLHTMY HVWAVFEMFT PILGRSGTEI PPDIVLGFLI
IACTIILITY FISFIYLLKS TKKIIVTLAV LSVLTLLLVC SGMFFPYSSS NDSPKPKRIF
LQHTTRTFHS LTGEVVKRDS GIWINGFDYT GISYVTPHIP ELNETVRAPC DDAPLCGFPW
YFPVHHLIRK NWYLPAPPAP INEHTDFKLV SREEMSWGAT RLFFEVKGPS HMTVYVRPNT
NTVLSSWSLG DGIPVASGET DYFIFYSHGL YAPAWKFWIE LKNSAKESKG IVTVAVGSHY
FFGDSRNSPD LETLELKFPD WSFPSSWVCT YDLYEY
