PAL1_DROME
ID PAL1_DROME Reviewed; 541 AA.
AC Q9V5E1; Q960U4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1;
DE EC=4.3.2.5 {ECO:0000269|PubMed:15198673};
DE AltName: Full=Peptidylamidoglycolate lyase 1;
DE AltName: Full=dPAL1 {ECO:0000303|PubMed:15198673};
DE Flags: Precursor;
GN Name=Pal1; ORFNames=CG12130;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=15198673; DOI=10.1111/j.1471-4159.2004.02464.x;
RA Han M., Park D., Vanderzalm P.J., Mains R.E., Eipper B.A., Taghert P.H.;
RT "Drosophila uses two distinct neuropeptide amidating enzymes, dPAL1 and
RT dPAL2.";
RL J. Neurochem. 90:129-141(2004).
CC -!- FUNCTION: Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that
CC catalyzes an essential reaction in C-terminal alpha-amidation of
CC peptides. Mediates the dismutation of the unstable peptidyl(2-
CC hydroxyglycine) intermediate to glyoxylate and the corresponding
CC desglycine peptide amide. C-terminal amidation of peptides such as
CC neuropeptides is essential for full biological activity.
CC {ECO:0000269|PubMed:15198673}.
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 Evidence={ECO:0000269|PubMed:15198673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20925;
CC Evidence={ECO:0000269|PubMed:15198673};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for peptidyl-alpha-hydroxyglycine
CC {ECO:0000269|PubMed:15198673};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Confined to cell bodies.
CC {ECO:0000269|PubMed:15198673}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In mature larvae, it is
CC ubiquitously expressed with a low expression in all cells and a
CC stronger expression in a subset of neurons. Colocalizes with
CC neuropeptide proctolin. In adults, weak expression is observed in most
CC neuronal cell bodies and in scattered large cells throughout the
CC protocerebrum and also in the subesophageal neuromeres (at protein
CC level). {ECO:0000269|PubMed:15198673}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:15198673}.
CC -!- SIMILARITY: Belongs to the peptidyl-alpha-hydroxyglycine alpha-
CC amidating lyase family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58870.1; -; Genomic_DNA.
DR EMBL; AY051842; AAK93266.1; -; mRNA.
DR RefSeq; NP_001137630.2; NM_001144158.3.
DR RefSeq; NP_610537.2; NM_136693.3.
DR AlphaFoldDB; Q9V5E1; -.
DR SMR; Q9V5E1; -.
DR STRING; 7227.FBpp0271777; -.
DR GlyGen; Q9V5E1; 2 sites.
DR PaxDb; Q9V5E1; -.
DR PRIDE; Q9V5E1; -.
DR DNASU; 36033; -.
DR EnsemblMetazoa; FBtr0088385; FBpp0087473; FBgn0283510.
DR EnsemblMetazoa; FBtr0339423; FBpp0308510; FBgn0283510.
DR GeneID; 36033; -.
DR KEGG; dme:Dmel_CG12130; -.
DR UCSC; CG12130-RA; d. melanogaster.
DR CTD; 36033; -.
DR FlyBase; FBgn0283510; Pal1.
DR VEuPathDB; VectorBase:FBgn0283510; -.
DR eggNOG; KOG3567; Eukaryota.
DR GeneTree; ENSGT00940000156369; -.
DR HOGENOM; CLU_037899_4_0_1; -.
DR InParanoid; Q9V5E1; -.
DR OrthoDB; 476471at2759; -.
DR PhylomeDB; Q9V5E1; -.
DR BRENDA; 4.3.2.5; 1994.
DR SABIO-RK; Q9V5E1; -.
DR BioGRID-ORCS; 36033; 0 hits in 3 CRISPR screens.
DR ChiTaRS; sdt; fly.
DR GenomeRNAi; 36033; -.
DR PRO; PR:Q9V5E1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0283510; Expressed in saliva-secreting gland and 36 other tissues.
DR ExpressionAtlas; Q9V5E1; baseline and differential.
DR Genevisible; Q9V5E1; DM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IDA:UniProtKB.
DR GO; GO:0004504; F:peptidylglycine monooxygenase activity; ISS:FlyBase.
DR GO; GO:0007619; P:courtship behavior; NAS:FlyBase.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0044719; P:regulation of imaginal disc-derived wing size; IMP:FlyBase.
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 Cell membrane; Disulfide bond; Glycoprotein; Lyase; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..541
FT /note="Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
FT 1"
FT /id="PRO_0000248573"
FT TOPO_DOM 34..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 164..205
FT /note="NHL 1"
FT REPEAT 215..258
FT /note="NHL 2"
FT REPEAT 272..314
FT /note="NHL 3"
FT REPEAT 374..418
FT /note="NHL 4"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..248
FT /evidence="ECO:0000250"
FT DISULFID 299..310
FT /evidence="ECO:0000250"
FT CONFLICT 253
FT /note="L -> F (in Ref. 3; AAK93266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59642 MW; A3C6E43F5AE5B148 CRC64;
MKSTDSAKCL GSKSLAICCL LLHLLLCIRP AVSQTQSPQR YLHNVDSNSN NNERLHQILK
GSGAGSGATQ LNWPQPPKQT VPNVKTELAK LNNTYVYQNA WPANNVKLGA VTAVSFDKAG
NVVIFHRVNR VWGQTTFDNR NQYQEKYRGP IRESTILALE PATGKVQYDW GKNFFYMPHG
LTVDPEDNVW LTDVAMHQVF KFPPRGGDGK PALTLGDAFQ PGSGRKFCKP TSVAVLDNGD
FFVADGYCNA RILKYSRKGE LILFWGQNTF SGISYDVAPQ NFFAIPHALT LVPELQLLCA
ADRENGRVQC FLSSNGTFHS QYHNQLIGDR LFSMAYTPAA GGQLVIVNGP TAELGIHPEH
YNEVHGFVLS MRSKQLVSKF GPNNLQFQNP HDVAVTADGN EIYVAELNPM RIHKFVHRSL
AKPMSLSASK DSRDSAISQA VGGDQVPAVA VHHPSGKAIL VASLMLLFAG STFALALIFA
RRRKRGCLPF GARGRRHAWE KSDGFKLGGL LDRDRNGFEK LDQQASDEEQ ETKTLASAQY
A
