YCF2E_CAEEL
ID YCF2E_CAEEL Reviewed; 452 AA.
AC P90850;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Uncharacterized peptidase C1-like protein F26E4.3;
DE Flags: Precursor;
GN ORFNames=F26E4.3;
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-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- CAUTION: Although strongly related to peptidase C1 family, it lacks the
CC conserved active Cys in position 210, which is replaced by a Ser
CC residue, suggesting that it has no protease activity. {ECO:0000305}.
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DR EMBL; Z81070; CAB03007.2; -; Genomic_DNA.
DR PIR; T21421; T21421.
DR RefSeq; NP_492593.2; NM_060192.6.
DR AlphaFoldDB; P90850; -.
DR SMR; P90850; -.
DR STRING; 6239.F26E4.3.1; -.
DR iPTMnet; P90850; -.
DR EPD; P90850; -.
DR PaxDb; P90850; -.
DR PeptideAtlas; P90850; -.
DR EnsemblMetazoa; F26E4.3.1; F26E4.3.1; WBGene00009158.
DR EnsemblMetazoa; F26E4.3.2; F26E4.3.2; WBGene00009158.
DR GeneID; 172827; -.
DR KEGG; cel:CELE_F26E4.3; -.
DR UCSC; F26E4.3.1; c. elegans.
DR CTD; 172827; -.
DR WormBase; F26E4.3; CE42101; WBGene00009158; -.
DR eggNOG; KOG1544; Eukaryota.
DR GeneTree; ENSGT00940000170013; -.
DR HOGENOM; CLU_012184_3_2_1; -.
DR InParanoid; P90850; -.
DR OMA; EVPDQGW; -.
DR OrthoDB; 1436535at2759; -.
DR PhylomeDB; P90850; -.
DR PRO; PR:P90850; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009158; Expressed in larva and 3 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50958; SMB_2; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..452
FT /note="Uncharacterized peptidase C1-like protein F26E4.3"
FT /id="PRO_0000250555"
FT DOMAIN 34..85
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT DISULFID 38..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..46
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 46..80
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 56..73
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 56..58
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 62..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 73..80
FT /note="Alternate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
SQ SEQUENCE 452 AA; 51121 MW; 9B6710E2E43E3EEE CRC64;
MPPNSVFLLP VLCLIVPIYS RGFFGIPGDY CSVRTHTCCE NRDDDCTVPI LGDHLCYCDM
FCDRGPDGGN DCCPDFEATC RGKDIQNDQR IDGESCSMDG DTKEKNCEKC TCHNGFWKCD
GTACLIQPDI LEKIHTGRYS WSARNYSAFW GRSLSDGIKY RLGTLFPERS VQNMNEILIK
PRELPEHFDA RDKWGPLIHP VADQGDCGSS WSVSTTAISS DRLAIISEGR INSTLSSQQL
LSCNQHRQKG CEGGYLDRAW WYIRKLGVVG DHCYPYVSGQ SREPGHCLIP KRDYTNRQGL
RCPSGSQDST AFKMTPPYKV SSREEDIQTE LMTNGPVQAT FVVHEDFFMY AGGVYQHSDL
AAQKGASSVA EGYHSVRVLG WGVDHSTGKP IKYWLCANSW GTQWGEDGYF KVLRGENHCE
IESFVIGAWG KGSKRRRRFK MRKLRRFRKM FK
