ERP1B_CAEEL
ID ERP1B_CAEEL Reviewed; 895 AA.
AC Q18600;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 4.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative endoplasmic reticulum metallopeptidase 1-B {ECO:0000250|UniProtKB:Q6UPR8};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-like protease {ECO:0000305};
GN ORFNames=C44B7.11;
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-679, AND IDENTIFICATION BY MASS
RP 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; FO080141; CCD61567.1; -; Genomic_DNA.
DR PIR; T15804; T15804.
DR RefSeq; NP_495410.4; NM_063009.5.
DR AlphaFoldDB; Q18600; -.
DR SMR; Q18600; -.
DR STRING; 6239.C44B7.11; -.
DR MEROPS; M28.018; -.
DR MEROPS; M28.A20; -.
DR iPTMnet; Q18600; -.
DR EPD; Q18600; -.
DR PaxDb; Q18600; -.
DR PeptideAtlas; Q18600; -.
DR PRIDE; Q18600; -.
DR EnsemblMetazoa; C44B7.11.1; C44B7.11.1; WBGene00016631.
DR GeneID; 183431; -.
DR KEGG; cel:CELE_C44B7.11; -.
DR UCSC; C44B7.11; c. elegans.
DR CTD; 183431; -.
DR WormBase; C44B7.11; CE41617; WBGene00016631; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_007536_2_0_1; -.
DR InParanoid; Q18600; -.
DR OMA; NICEWMF; -.
DR OrthoDB; 248924at2759; -.
DR PhylomeDB; Q18600; -.
DR PRO; PR:Q18600; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016631; Expressed in larva and 3 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 Coiled coil; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..895
FT /note="Putative endoplasmic reticulum metallopeptidase 1-B"
FT /id="PRO_0000174142"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..374
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 425..445
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..457
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..478
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..512
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..515
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..538
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 554..574
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..584
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 585..605
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 620..640
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..895
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 180
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 192
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 192
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 227
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 253
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 329
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 CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 895 AA; 101896 MW; 034D6890AEE1EF69 CRC64;
MSTGIRRRHA DEKKNILEKE SLQNDETQRE MEKDISLLRP AHWNFIGLFF LVLIIGTTFL
HKCLPEPKDP NQEETQFSEK RAVKVLQELS DYGWKPAGSY NCEELTRNRI LKELNDIRSQ
NQNVENLRFD IDTQYVSGCF DIPAHDTEGM NICYRNVSNV MARLGKGEKK DKISVLLNCH
YDSWPTSNAG SDDLSSCALM LELIRLYSKN PHLLNHDVIF LFNGAEESSL LAAHGFITQH
SWRHEIRAFI NLEASGSGGR ELLFQAGPAN QWLLNSYLEA AIHPHCSVIG QEVFQSGVYP
GDTDFRIFRD HGRVPGLDLA FVQNGYWWHT EFDTAERITK GSLQRAGENV YSTLNHLLKS
PYLEKPAEYA DRKTVFFDFL GLFVIIYPLS IAHLVNMLTI CTVIALMSHR FYSKTFITFL
ALRDYVLTIL TIALVLKAMT FMSLFTYGAL RWYTRHWLAL VAYGLPSVWA GISVQGLLTA
RLAPKAREEY GSTLELIHLT LISGILLAFT YYDIASGFLF ALLLVPAIKS IITYFGAWPT
CPTFNTILTL ILSFPGCAMA IYTTEMLLSI FIPIMGRSSY NPEPAVSFFV AFSAGCIVLS
LGGLVAKSRN SRSSNEAGLL ELIYNILGVL LVTLTILYVF SSFWPSPYRF DNVYPTAKRT
QFFHVNQMLY DRNGQISVND TRFYAISHDY RGAEDIPFVK KDPEYTGLQC HYENNPWCET
PFLFPTKGRL NERNIRVRSV DERLKFKHPV KILGISKRHG VDSKDGKGNI EYSFSVIGTG
QISVYIIPDT TWLITNTSVT QPKTPQENMF LYYTCSTPNN ICEWMFKVTI KKTTQTPSDD
KPLLIGISSH YLHGPEMQSE SIKNMIAKIQ ENRVNSPEWT VTASAWNVDQ VYKYF
