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Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1 (EC 4.3.2.5) (Peptidylamidoglycolate lyase 1) (dPAL1)

 PAL1_DROME              Reviewed;         541 AA.
Q9V5E1; Q960U4;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 123.
RecName: Full=Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1;
EC=4.3.2.5;
AltName: Full=Peptidylamidoglycolate lyase 1;
AltName: Full=dPAL1;
Flags: Precursor;
Name=Pal1; ORFNames=CG12130;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=15198673; DOI=10.1111/j.1471-4159.2004.02464.x;
Han M., Park D., Vanderzalm P.J., Mains R.E., Eipper B.A.,
Taghert P.H.;
"Drosophila uses two distinct neuropeptide amidating enzymes, dPAL1
and dPAL2.";
J. Neurochem. 90:129-141(2004).
-!- FUNCTION: Probable lyase that catalyzes an essential reaction in
C-terminal alpha-amidation of peptides. Mediates the dismutation
of the unstable peptidyl(2-hydroxyglycine) intermediate to
glyoxylate and the corresponding desglycine peptide amide. C-
terminal amidation of peptides such as neuropeptides is essential
for full biological activity. {ECO:0000269|PubMed:15198673}.
-!- CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide +
glyoxylate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=45 uM for peptidyl-alpha-hydroxyglycine
{ECO:0000269|PubMed:15198673};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Note=Confined to cell
bodies. {ECO:0000269|PubMed:15198673}.
-!- TISSUE SPECIFICITY: Widely expressed. In mature larvae, it is
ubiquitously expressed with a low expression in all cells and a
stronger expression in a subset of neurons. Colocalizes with
neuropeptide proctolin. In adults, weak expression is observed in
most neuronal cell bodies and in scattered large cells throughout
the protocerebrum and also in the subesophageal neuromeres (at
protein level). {ECO:0000269|PubMed:15198673}.
-!- PTM: N-glycosylated. {ECO:0000305|PubMed:15198673}.
-!- SIMILARITY: Belongs to the peptidyl-alpha-hydroxyglycine alpha-
amidating lyase family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AE013599; AAF58870.1; -; Genomic_DNA.
EMBL; AY051842; AAK93266.1; -; mRNA.
RefSeq; NP_001137630.2; NM_001144158.3.
RefSeq; NP_610537.2; NM_136693.3.
UniGene; Dm.548; -.
ProteinModelPortal; Q9V5E1; -.
SMR; Q9V5E1; -.
STRING; 7227.FBpp0271777; -.
PaxDb; Q9V5E1; -.
PRIDE; Q9V5E1; -.
EnsemblMetazoa; FBtr0088385; FBpp0087473; FBgn0283510.
EnsemblMetazoa; FBtr0339423; FBpp0308510; FBgn0283510.
GeneID; 36033; -.
KEGG; dme:Dmel_CG12130; -.
UCSC; CG12130-RA; d. melanogaster.
CTD; 36033; -.
FlyBase; FBgn0283510; Pal1.
eggNOG; KOG3567; Eukaryota.
eggNOG; ENOG410XS0X; LUCA.
GeneTree; ENSGT00530000063085; -.
InParanoid; Q9V5E1; -.
KO; K18200; -.
OrthoDB; EOG091G067T; -.
BRENDA; 4.3.2.5; 1994.
ChiTaRS; sdt; fly.
GenomeRNAi; 36033; -.
PRO; PR:Q9V5E1; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0033466; Expressed in 10 organ(s), highest expression level in head.
ExpressionAtlas; Q9V5E1; differential.
Genevisible; Q9V5E1; DM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004598; F:peptidylamidoglycolate lyase activity; IDA:UniProtKB.
GO; GO:0007619; P:courtship behavior; NAS:FlyBase.
GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
GO; GO:0044719; P:regulation of imaginal disc-derived wing size; IMP:FlyBase.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001258; NHL_repeat.
InterPro; IPR013017; NHL_repeat_subgr.
InterPro; IPR000720; PHM/PAL.
Pfam; PF01436; NHL; 3.
PRINTS; PR00790; PAMONOXGNASE.
PROSITE; PS51125; NHL; 4.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Lyase;
Membrane; Metal-binding; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Zinc.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 541 Peptidyl-alpha-hydroxyglycine alpha-
amidating lyase 1.
/FTId=PRO_0000248573.
TOPO_DOM 34 458 Extracellular. {ECO:0000255}.
TRANSMEM 459 479 Helical. {ECO:0000255}.
TOPO_DOM 480 541 Cytoplasmic. {ECO:0000255}.
REPEAT 164 205 NHL 1.
REPEAT 215 258 NHL 2.
REPEAT 272 314 NHL 3.
REPEAT 374 418 NHL 4.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 228 248 {ECO:0000250}.
DISULFID 299 310 {ECO:0000250}.
CONFLICT 253 253 L -> F (in Ref. 3; AAK93266).
{ECO:0000305}.
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


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