ERMP1_SCHPO
ID ERMP1_SCHPO Reviewed; 822 AA.
AC O94702;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative endoplasmic reticulum metallopeptidase 1 {ECO:0000250|UniProtKB:Q6UPR8};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-like protease {ECO:0000305};
GN Name=erm1 {ECO:0000312|PomBase:SPCC1259.02c};
GN ORFNames=SPCC1259.02c {ECO:0000312|PomBase:SPCC1259.02c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA22540.1; -; Genomic_DNA.
DR PIR; T40891; T40891.
DR RefSeq; NP_588058.1; NM_001023050.2.
DR AlphaFoldDB; O94702; -.
DR SMR; O94702; -.
DR BioGRID; 275613; 2.
DR STRING; 4896.SPCC1259.02c.1; -.
DR SwissPalm; O94702; -.
DR MaxQB; O94702; -.
DR PaxDb; O94702; -.
DR PRIDE; O94702; -.
DR EnsemblFungi; SPCC1259.02c.1; SPCC1259.02c.1:pep; SPCC1259.02c.
DR PomBase; SPCC1259.02c; erm1.
DR VEuPathDB; FungiDB:SPCC1259.02c; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_015120_0_0_1; -.
DR InParanoid; O94702; -.
DR OMA; HAEGHNI; -.
DR PhylomeDB; O94702; -.
DR PRO; PR:O94702; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:PomBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..822
FT /note="Putative endoplasmic reticulum metallopeptidase 1"
FT /id="PRO_0000372386"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..365
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 366..384
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 393..413
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..431
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 432..452
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..484
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 486..506
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 515..535
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..547
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 548..568
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 576..596
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..822
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 161
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 173
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 173
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 208
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 234
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 307
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 306
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 822 AA; 91843 MW; FBB4DAE6857E671F CRC64;
MVLVCASSSK CKRNTFLQLA MVLFAVVMAR IALYFHNHLD EPLVDPYDAN GNPQFSEANA
LKHVIHLSDD IGYRILGTIE QERAREYIMN EVLALQKQLQ DGPNADIHQM EVSLESGDGA
HRFDFMNKYV IKKYQNLKNI VVRLSNGTEA CKEEAVLINA HVDSTLPSPG ATDDALAVAI
LLEAIRIFIS RPVPLTHSIV FLFNDAEESL QDASHMFITQ SPLRDTIKCV VNLEACGTTG
SEILFQATSN EMIKAYSHVP HPFGTVLADD VFRTGLILSD TDFRQFVQYG NLTGLDMAVV
KNSYLYHTKK DLAPYISPGT PQNFGENILA ILTYLVSPEA DLNNMKSSGT VYFSVFNSLF
FMYSKLTSKI LNTLVGGLGI LLTLRGSEGS FTVALIAQVI SIAGIFVIPN IWAYILGNVL
DCGMSWFRNE YWPLFIYLPA IFASLFFTES LFKRSEHLAL RATIFIFSLL TFIPLPSAYL
FTIIDFFMVF ALFLNDKILA KPGTVHPLTY FIGSIGAMTV GFESAINLLE IFVPLTGRIG
TDKVADNVVA TVCVCGFNIY FPLMSPWIQR FRSRCCFRLG LLFSIFVVGF SSFILAKQDT
YYDSLHPRRI FVQRMENITS NEVSLHIASA DSAPGFDKLS SDLSSLLTDE PVVKTEMDDW
NSDWDTVYPF SQFLGSYRIP LNDTVDVTTL PSIKFSNKVV KDNVVNVTVT VEHPGLIWTV
VSFDADVLSW SLPEVPSTVR RHHVREVSAY GLDSYSFNMS YLEAPIYFDF VGVDGVGHYP
SKASEGRDRA SIQLCEKLTN DYLPDWTDTL CIGVVSGNFK LE
