ERMP1_MOUSE
ID ERMP1_MOUSE Reviewed; 898 AA.
AC Q3UVK0; B2RXD6; Q6ZPH9; Q8BIW0; Q8BYX7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Endoplasmic reticulum metallopeptidase 1 {ECO:0000250|UniProtKB:Q6UPR8};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=Felix-ina {ECO:0000250|UniProtKB:Q6UPR8};
GN Name=Ermp1 {ECO:0000250|UniProtKB:Q7Z2K6};
GN Synonyms=D19Wsu12e, Fxna {ECO:0000250|UniProtKB:Q6UPR8},
GN Kiaa1815 {ECO:0000303|PubMed:14621295};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Thymus, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-898 (ISOFORM 1).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
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: Within the ovary, required for the organization of somatic
CC cells and oocytes into discrete follicular structures.
CC {ECO:0000250|UniProtKB:Q6UPR8}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UVK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UVK0-2; Sequence=VSP_021393, VSP_021394;
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK037287; BAC29784.1; ALT_INIT; mRNA.
DR EMBL; AK081674; BAC38286.1; ALT_INIT; mRNA.
DR EMBL; AK137206; BAE23269.1; -; mRNA.
DR EMBL; BC151181; AAI51182.1; -; mRNA.
DR EMBL; BC151182; AAI51183.1; -; mRNA.
DR EMBL; BC157914; AAI57915.1; -; mRNA.
DR EMBL; AK129447; BAC98257.1; -; mRNA.
DR CCDS; CCDS37952.1; -. [Q3UVK0-1]
DR RefSeq; NP_001074682.1; NM_001081213.1. [Q3UVK0-1]
DR AlphaFoldDB; Q3UVK0; -.
DR SMR; Q3UVK0; -.
DR STRING; 10090.ENSMUSP00000124881; -.
DR MEROPS; M28.018; -.
DR GlyConnect; 2286; 2 N-Linked glycans (1 site).
DR GlyGen; Q3UVK0; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q3UVK0; -.
DR PhosphoSitePlus; Q3UVK0; -.
DR SwissPalm; Q3UVK0; -.
DR EPD; Q3UVK0; -.
DR jPOST; Q3UVK0; -.
DR MaxQB; Q3UVK0; -.
DR PaxDb; Q3UVK0; -.
DR PeptideAtlas; Q3UVK0; -.
DR PRIDE; Q3UVK0; -.
DR ProteomicsDB; 275475; -. [Q3UVK0-1]
DR ProteomicsDB; 275476; -. [Q3UVK0-2]
DR Antibodypedia; 54615; 157 antibodies from 24 providers.
DR DNASU; 226090; -.
DR Ensembl; ENSMUST00000159692; ENSMUSP00000124881; ENSMUSG00000046324. [Q3UVK0-1]
DR GeneID; 226090; -.
DR KEGG; mmu:226090; -.
DR UCSC; uc008hdu.1; mouse. [Q3UVK0-1]
DR UCSC; uc008hdw.1; mouse. [Q3UVK0-2]
DR CTD; 79956; -.
DR MGI; MGI:106250; Ermp1.
DR VEuPathDB; HostDB:ENSMUSG00000046324; -.
DR eggNOG; KOG2194; Eukaryota.
DR GeneTree; ENSGT00530000063839; -.
DR HOGENOM; CLU_007536_2_0_1; -.
DR InParanoid; Q3UVK0; -.
DR OMA; WNNTIGA; -.
DR OrthoDB; 248924at2759; -.
DR PhylomeDB; Q3UVK0; -.
DR TreeFam; TF314836; -.
DR BioGRID-ORCS; 226090; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Ermp1; mouse.
DR PRO; PR:Q3UVK0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UVK0; protein.
DR Bgee; ENSMUSG00000046324; Expressed in urinary bladder urothelium and 266 other tissues.
DR ExpressionAtlas; Q3UVK0; baseline and differential.
DR Genevisible; Q3UVK0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:0001541; P:ovarian follicle development; ISO:MGI.
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; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..898
FT /note="Endoplasmic reticulum metallopeptidase 1"
FT /id="PRO_0000259493"
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..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
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:0000250"
FT VAR_SEQ 209..215
FT /note="ASDDAVS -> RYLYLVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021393"
FT VAR_SEQ 216..898
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021394"
FT CONFLICT 743
FT /note="Y -> H (in Ref. 1; BAE23269)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="F -> S (in Ref. 1; BAC38286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 100148 MW; 4BEEF4F7C3B7EB17 CRC64;
MEWSSESAAV RRHRGTAERR EGEAAASHRQ REASAQEDAK GVGRMWGKTE NGGGSRVAKT
ALSEARTALA LALYLLALRA LVQLSLQRLV LSRTSGLQGE FDARQARDYL EHITAIGPRT
TGSTENEILT VQYLLEQIKL IEAQSNSLHS ISVDIQRPTG SFSIDFLGGF TSYYDNITNV
VVKLEPRDGA ESAILANCHF DSVANSPGAS DDAVSCAVML EVLRVMSASP EPMQHAVVFL
FNGAEENVLQ ASHGFITQHP WASLIRAFIN LEAAGVGGKE LVFQTGPENP WLVQAYVSAA
KHPFASVVAQ EVFQSGIIPS DTDFRIYRDF GNIPGIDLAF IENGYIYHTK YDTADRILID
SIQRAGDNIL AVLKHLATSD TLASSSEYRH GSMVFFDVLG LLVIAYPSRV GSIINYMVVM
AVVLYLGKKL LRPKHRNANY MRDFLCGLGI TFISWFTSLV TVLIIAVFIS LIGQSLSWYN
YFYIAVCLYG TATVAKIIFI HTLAKRFYYM NASDLYLGEL FFDTSLFVHC AFLVALTYQG
FCSAFMSAVW VVFPLLTKLC VYKDFKKHGA QGRFVALYLL GMFIPYLYGL YLIWAVFEMF
TPILGRSGSE IPPDVVLASI LAVCVMILSS YFITFIYLVN STKKTILTLI LVCAVTFLLV
CSGAFFPYSS NPESPKPKRV FLQHVSRTFH NLEGSVVKRD SGIWINGFDY TGMSHVTPHI
PEINDTIRAH CEEDAPLCGF PWYLPVHFLI RKNWYLPAPE VSPRNPAHFR LVSKEKMPWD
SIKLTFEATG PSHMSFYVRT HKGSTLSQWS LGNGIPVTSR GGDYFVFYSH GLQASAWRFW
IEVQVSEEQA EGMVTVAIAA HYLSGENKRS SQLDALKKKF PDWSFPSAWV STYSLFVF
