ID   YM9I_CAEEL              Reviewed;         540 AA.
AC   P90893;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative serine protease F56F10.1;
DE            EC=3.4.-.-;
DE   Flags: Precursor;
GN   ORFNames=F56F10.1;
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-87, 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   -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO081336; CCD70865.1; -; Genomic_DNA.
DR   PIR; T16490; T16490.
DR   RefSeq; NP_001294837.1; NM_001307908.1.
DR   AlphaFoldDB; P90893; -.
DR   SMR; P90893; -.
DR   STRING; 6239.F56F10.1.2; -.
DR   ESTHER; caeel-ym9i; Prolylcarboxypeptidase.
DR   MEROPS; S28.A14; -.
DR   iPTMnet; P90893; -.
DR   EPD; P90893; -.
DR   PaxDb; P90893; -.
DR   PeptideAtlas; P90893; -.
DR   EnsemblMetazoa; F56F10.1.1; F56F10.1.1; WBGene00018984.
DR   GeneID; 24104657; -.
DR   KEGG; cel:CELE_F56F10.1; -.
DR   UCSC; F56F10.1.1; c. elegans.
DR   CTD; 24104657; -.
DR   WormBase; F56F10.1; CE34034; WBGene00018984; -.
DR   eggNOG; KOG2182; Eukaryota.
DR   GeneTree; ENSGT00940000164087; -.
DR   HOGENOM; CLU_020959_3_1_1; -.
DR   InParanoid; P90893; -.
DR   OMA; HCGDMYP; -.
DR   OrthoDB; 555765at2759; -.
DR   PhylomeDB; P90893; -.
DR   PRO; PR:P90893; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00018984; Expressed in larva and 3 other tissues.
DR   GO; GO:0045121; C:membrane raft; HDA:WormBase.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; HEP:WormBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.980; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008758; Peptidase_S28.
DR   InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR   Pfam; PF05577; Peptidase_S28; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..540
FT                   /note="Putative serine protease F56F10.1"
FT                   /id="PRO_0000027325"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        453
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        479
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   540 AA;  60568 MW;  9C389EF45CF68C4E CRC64;
     MLRNLLLLLL PLLIEAKLPP FFLGRLNGKT LLNHHLDRLT ASDGASIQET YPNLQVHNFT
     QKLDHFDPYN TKTWNQKYFY NPVFSRNNSI IFLMIGGEGP ENGKWAANPN VQYLQWAKEF
     GADVFDLEHR FFGDSWPIPD MQTSSLRYLT TQQALADLAF FIEFMNQQYG FKNPRWVTFG
     GSYPGSLAAW FRQKYPQLTV GSVASSAPVN LKLDFYEYAM VVEDDLRITD PKCAQATKDA
     FVQMQKLALT AEGRNSLNNH FNLQPPFDAN TTKLDINNFF GNIFNTYQGM TQYTYDGQSN
     STHSDKTVRK MCDIMTNATE TDVVMRVENL FLWFNQMEPA SANLTVMPNS YWDVISQVGS
     GDLNVLGPDG AAARGWMWLC CNEIGFLQTT NQGNNVFGTG VPLNLFIDMC TDMFGDSMKM
     SQIMGGNKKS QNYYGGADFY NATNVVLPNG SLDPWHALGT YGTIKSQSLL PYLINGTAHC
     GDMYPSYDGE PGSLLAARAF VKENVRQFIR YDPNVDGPGG SSSSASLFVV AYIVCGFLFV