ID   MNP1_CAEEL              Reviewed;         781 AA.
AC   P46557;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Matrix non-peptidase homolog 1;
DE   Flags: Precursor;
GN   Name=mnp-1; ORFNames=B0285.7;
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-520, 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).
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DR   EMBL; Z34533; CAA84298.1; -; Genomic_DNA.
DR   PIR; T18693; T18693.
DR   RefSeq; NP_497878.1; NM_065477.4.
DR   AlphaFoldDB; P46557; -.
DR   SMR; P46557; -.
DR   BioGRID; 40800; 1.
DR   STRING; 6239.B0285.7; -.
DR   iPTMnet; P46557; -.
DR   EPD; P46557; -.
DR   PaxDb; P46557; -.
DR   PeptideAtlas; P46557; -.
DR   PRIDE; P46557; -.
DR   EnsemblMetazoa; B0285.7.1; B0285.7.1; WBGene00007139.
DR   GeneID; 175564; -.
DR   KEGG; cel:CELE_B0285.7; -.
DR   UCSC; B0285.7; c. elegans.
DR   CTD; 175564; -.
DR   WormBase; B0285.7; CE00646; WBGene00007139; mnp-1.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_358721_0_0_1; -.
DR   InParanoid; P46557; -.
DR   OMA; NTGETIC; -.
DR   OrthoDB; 273281at2759; -.
DR   PhylomeDB; P46557; -.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Reactome; R-CEL-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   PRO; PR:P46557; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007139; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   SUPFAM; SSF63737; SSF63737; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..781
FT                   /note="Matrix non-peptidase homolog 1"
FT                   /id="PRO_0000014271"
FT   REGION          63..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        520
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   781 AA;  85984 MW;  A9D5BCD8F567B8B0 CRC64;
     MTPPPASPSK KAKSSWLLIA LIAVIIGIIL CAGVITFLTL FNKNGDGPDM DWQNATEVPL
     TTTSKATVST TTTQSATTPS TTTTRIEETT TTTSGAFDES VKNSEASTST IPTTEAVPTT
     TATDAPEIVM PVDVASILKD KTKDFEIVEK CAEIQALPVS CTPSQSPLTS DPSKFQPIHY
     VLNITIRDVR KPVLEGHMQL FASTKDQVQA ISLHSVKIHN LENRDRIHVV NCNTGETICV
     SRVHQIDDLI HLELAQSISS GVNLRVDIDG FISADSGPHV FKQIPTAKWR VPQMIGSVFE
     PTSARHVFPS FDLHNQKSTF NLCLNHGPSM SAIANSLINP NVSTSGISCF EKTVPLIAQQ
     LSFVAFEKTN PLFYNTTTMD GAYLPEIDMI FNLNAKNFKQ YEWIHSEVSK VMALMSKWSG
     FSYPLTRLEI VVAPVQAGHS ALGVITLPAQ AIAYQKHTST HETLIKEVIG QWMEGVVTTE
     HTCFEKALIA YVEWKINEEL QIVKKTRKME VSKIRPRNLN ETADSVRVLR QIKSQSSNLC
     SPRFVEVFYT LDETYGQETV IGMIRVIFDK FAFSTATISD WASAAETATG GRPEAGALIH
     QWYRPSSTIS RPVLRAVVSS NSVEFNQLTE ETWTVPLEIS GSAGTQLAVI SEKKQAIPFV
     SSDYVVVDAG RKSHAFVVYD ADTYLRLIRC FGDSRCPSKE IGGIFSDLGA ALLANILPKP
     ENQDVAKWKS VFKFMAQQNI VEGTAACCVE HAIREMRKCS YWDIQDVCTK IDFNIVLAAV
     A