PGAL_CAEEL
ID PGAL_CAEEL Reviewed; 350 AA.
AC P91268;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase pgal-1 {ECO:0000305};
DE EC=4.3.2.5;
DE AltName: Full=Probable peptidylamidoglycolate lyase;
DE Short=PAL;
DE Flags: Precursor;
GN Name=pgal-1 {ECO:0000312|WormBase:F21F3.1};
GN ORFNames=F21F3.1 {ECO:0000312|WormBase:F21F3.1};
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-103, 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 -!- FUNCTION: Probable lyase that catalyzes an essential reaction in C-
CC terminal alpha-amidation of peptides. Mediates the dismutation of the
CC unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the
CC corresponding desglycine peptide amide. C-terminal amidation of
CC peptides such as neuropeptides is essential for full biological
CC activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a [peptide]-C-terminal (2S)-2-hydroxyglycine = a [peptide]-C-
CC terminal amide + glyoxylate; Xref=Rhea:RHEA:20924, Rhea:RHEA-
CC COMP:13485, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:137001, ChEBI:CHEBI:142768; EC=4.3.2.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidyl-alpha-hydroxyglycine alpha-
CC amidating lyase family. {ECO:0000305}.
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DR EMBL; FO081197; CCD69816.1; -; Genomic_DNA.
DR PIR; T25723; T25723.
DR RefSeq; NP_491475.2; NM_059074.6.
DR AlphaFoldDB; P91268; -.
DR SMR; P91268; -.
DR BioGRID; 37570; 1.
DR STRING; 6239.F21F3.1.1; -.
DR iPTMnet; P91268; -.
DR EPD; P91268; -.
DR PaxDb; P91268; -.
DR PeptideAtlas; P91268; -.
DR EnsemblMetazoa; F21F3.1.1; F21F3.1.1; WBGene00017671.
DR GeneID; 172108; -.
DR KEGG; cel:CELE_F21F3.1; -.
DR UCSC; F21F3.1.1; c. elegans.
DR CTD; 172108; -.
DR WormBase; F21F3.1; CE32870; WBGene00017671; pgal-1.
DR eggNOG; KOG3567; Eukaryota.
DR GeneTree; ENSGT00940000156369; -.
DR HOGENOM; CLU_037899_1_0_1; -.
DR InParanoid; P91268; -.
DR OMA; NERFFDQ; -.
DR OrthoDB; 476471at2759; -.
DR PhylomeDB; P91268; -.
DR PRO; PR:P91268; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00017671; Expressed in larva and 4 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000720; PHM/PAL.
DR Pfam; PF01436; NHL; 3.
DR PRINTS; PR00790; PAMONOXGNASE.
DR PROSITE; PS51125; NHL; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Lyase; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..350
FT /note="Probable peptidyl-alpha-hydroxyglycine alpha-
FT amidating lyase pgal-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000248572"
FT REPEAT 46..90
FT /note="NHL 1"
FT REPEAT 113..154
FT /note="NHL 2"
FT REPEAT 162..206
FT /note="NHL 3"
FT REPEAT 212..256
FT /note="NHL 4"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 176..196
FT /evidence="ECO:0000250"
FT DISULFID 241..252
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 38593 MW; A1892DDAAF0756DB CRC64;
MRASTACLVA LLAPFYISAL PVEYFYGDEQ QPIEEGAENS AVFEQDRELI GLFNPSKEIG
QVSGLAVNKN GHIVAFHRSG RVWDEKSFND HETFNKDLGV INNKTIAIIS REKKVIDEFG
AGLFYMPHGL TIDNNGDYWV TDVGSHQVHK IDAKTQKIVM SLGEKMVPGE DQAHFCKPTD
VAVAKNGHIF VADGYCNSRI LKFDAKGNLM AQINAATEEN QPSEFVVPHS LSLIEDMNIV
CVADRENQRV QCFSAGLSEG DRTLPTGIPI TSATDIGRVF AIREREHYLI GVTGNSEDVE
AQMFSIDMQT GKTETFAKGV RNTHALAIAA DGVMFVSQLE PSRILEIRLL
