ERMP1_RAT
ID ERMP1_RAT Reviewed; 898 AA.
AC Q6UPR8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Endoplasmic reticulum metallopeptidase 1 {ECO:0000305};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=Felix-ina {ECO:0000303|PubMed:17267443};
GN Name=Ermp1 {ECO:0000250|UniProtKB:Q7Z2K6};
GN Synonyms=Fxna {ECO:0000303|PubMed:17267443};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, 3D-STRUCTURE MODELING OF 104-383, AND
RP DISULFIDE BONDS.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=17267443; DOI=10.1242/dev.02795;
RA Garcia-Rudaz C., Luna F., Tapia V., Kerr B., Colgin L., Galimi F.,
RA Dissen G.A., Rawlings N.D., Ojeda S.R.;
RT "Fxna, a novel gene differentially expressed in the rat ovary at the time
RT of folliculogenesis, is required for normal ovarian histogenesis.";
RL Development 134:945-957(2007).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=23679341; DOI=10.1111/1567-1364.12050;
RA Hecht K.A., Wytiaz V.A., Ast T., Schuldiner M., Brodsky J.L.;
RT "Characterization of an M28 metalloprotease family member residing in the
RT yeast vacuole.";
RL FEMS Yeast Res. 13:471-484(2013).
CC -!- FUNCTION: Within the ovary, required for the organization of somatic
CC cells and oocytes into discrete follicular structures.
CC {ECO:0000269|PubMed:17267443}.
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:0000269|PubMed:17267443, ECO:0000269|PubMed:23679341}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in ovary,
CC kidney, hypothalamus and hippocampus. Within the ovarian follicle,
CC expressed in granulosa cells, but not in oocytes. Present in both
CC preantral and antral follicles, but not in atretic antral follicle.
CC {ECO:0000269|PubMed:17267443}.
CC -!- DEVELOPMENTAL STAGE: Increasing expression in the ovary between fetal
CC day 21 and postnatal day 2. Expression decreases thereafter to lower
CC levels in adult ovaries. {ECO:0000269|PubMed:17267443}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; AY364634; AAQ55282.2; -; mRNA.
DR RefSeq; NP_908939.2; NM_184050.2.
DR AlphaFoldDB; Q6UPR8; -.
DR SMR; Q6UPR8; -.
DR BioGRID; 266948; 1.
DR STRING; 10116.ENSRNOP00000021958; -.
DR GlyGen; Q6UPR8; 2 sites.
DR SwissPalm; Q6UPR8; -.
DR jPOST; Q6UPR8; -.
DR PaxDb; Q6UPR8; -.
DR PRIDE; Q6UPR8; -.
DR GeneID; 373544; -.
DR KEGG; rno:373544; -.
DR UCSC; RGD:727831; rat.
DR CTD; 79956; -.
DR RGD; 727831; Ermp1.
DR eggNOG; KOG2194; Eukaryota.
DR InParanoid; Q6UPR8; -.
DR OrthoDB; 248924at2759; -.
DR PhylomeDB; Q6UPR8; -.
DR PRO; PR:Q6UPR8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
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 Acetylation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..898
FT /note="Endoplasmic reticulum metallopeptidase 1"
FT /id="PRO_0000259494"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..393
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..414
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..480
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 481..501
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..538
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..542
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 543..562
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 574..594
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..615
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 616..636
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 646..666
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..898
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 199
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 211
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 211
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 246
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 272
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 348
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 347
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K6"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 198..216
FT /evidence="ECO:0000255"
SQ SEQUENCE 898 AA; 99897 MW; EF1E574C8BFAD1F3 CRC64;
MEWSSESAAV RRHRGTAERR EGQAAASHPQ REASAQEDAR GGGRMRGRTE SGGESRGAKT
ALSEARTALA LALYLLALRA LVQLSLQRLV LSRTSGLQGE FDARQARVYL EHITAIGPRT
TGSAENEILT VQYLLEQITL IEEQSNSLHR ISVDVQRPTG SFSIDFLGGF TSYYDNITNV
VVKLEPQDGA KYAVLANCHF DSVANSPGAS DDAVSCAVML EVLRVMAASP EPLQHAVVFL
FNGAEENVLQ ASHGFITQHP WASLIRAFIN LEAAGVGGKE LVFQTGPENP WLVQAYVSAA
KHPFASVVAQ EVFQSGIIPS DTDFRIYRDF GNIPGIDLAF IENGYIYHTK YDTADRILID
SIQRAGDNIL AVLKYLATSD MLASSSEYRH GSMVFFDVLG LLVIAYPSRV GSIINYMVVM
AVVLYLGRKL LRPNHSNSNY VRDFLCGLGI TFISWFTSLV TVLIIAVFVS LIGQSLSWYN
YFYIAVCLYG TATVAKIILI HTLAKRFYYV NASDLYLGEL FFDTSLFVHC GFLVALTAQG
FCSAFMSAVW VAFPLLTKLC VYKDFKKHGA KGRFIALYLL GMFIPYLYGL YLIWAVFEMF
TPILGRSGSE IPPDVVLASI LAVCVMILSS YFITFIYLVN STKKTILTLI LVCAVTFLLV
CSGAFFPYSS NPDSPKPKRV FLQHVSRTFH NLEGSVVKRD SGIWINGFDY TGMSHVTPHI
PEINDTIRAH CEENAPLCGF PWYLPVHFLI RKNWYLPAPE ISPRNPAHFR LVSKEKMPWD
SIKLTFEATG PSHMSFYVRT HKGSTLSQWS LGNGIPVTSR GGDYFVFYSH GLQASAWQFW
IEVQVSEEQP EGMVTVAIAA HYLSGENKRS SQLDALKEKF PDWSFPSAWV STYSLFVF
