Reviewed, UniProtKB/Swiss-Prot Q9V5E1 (PAL1_DROME)

Names and origin

Protein names

Recommended name:
    Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1
    EC=4.3.2.5
Alternative name(s):
    Peptidylamidoglycolate lyase 1
    dPAL1

Gene names

Name:	PAL1
ORF Names:	CG12130

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.4
Catalytic activity	Peptidylamidoglycolate = peptidyl amide + glyoxylate.
Cofactor	Zinc By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein Potential. Note: Confined to cell bodies.
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 suboesophageal neuromeres (at protein level). Ref.4
Post-translational modification	N-glycosylated Probable.
Sequence similarities	Belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family. Contains 4 NHL repeats.
Biophysicochemical properties	Kinetic parameters: KM=45 µM for peptidyl-alpha-hydroxyglycine

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	peptide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cell soma Ref.4 Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro peptidylamidoglycolate lyase activity Ref.4 Inferred from direct assay. Source: UniProtKB peptidylglycine monooxygenase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 33	33	Potential
	Chain	34 – 541	508	Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1		PRO_0000248573
Regions
	Topological domain	34 – 458	425	Extracellular Potential
	Transmembrane	459 – 479	21	Potential
	Topological domain	480 – 541	62	Cytoplasmic Potential
	Repeat	164 – 205	42	NHL 1
	Repeat	215 – 258	44	NHL 2
	Repeat	272 – 314	43	NHL 3
	Repeat	374 – 418	45	NHL 4
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	315	1	N-linked (GlcNAc...) Potential
	Disulfide bond	228 ↔ 248		By similarity
	Disulfide bond	299 ↔ 310		By similarity
Experimental info
	Sequence conflict	253	1	L → F in AAK93266. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9V5E1-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: A3C6E43F5AE5B148	FASTA	541	59,642
	10 20 30 40 50 60 MKSTDSAKCL GSKSLAICCL LLHLLLCIRP AVSQTQSPQR YLHNVDSNSN NNERLHQILK 70 80 90 100 110 120 GSGAGSGATQ LNWPQPPKQT VPNVKTELAK LNNTYVYQNA WPANNVKLGA VTAVSFDKAG 130 140 150 160 170 180 NVVIFHRVNR VWGQTTFDNR NQYQEKYRGP IRESTILALE PATGKVQYDW GKNFFYMPHG 190 200 210 220 230 240 LTVDPEDNVW LTDVAMHQVF KFPPRGGDGK PALTLGDAFQ PGSGRKFCKP TSVAVLDNGD 250 260 270 280 290 300 FFVADGYCNA RILKYSRKGE LILFWGQNTF SGISYDVAPQ NFFAIPHALT LVPELQLLCA 310 320 330 340 350 360 ADRENGRVQC FLSSNGTFHS QYHNQLIGDR LFSMAYTPAA GGQLVIVNGP TAELGIHPEH 370 380 390 400 410 420 YNEVHGFVLS MRSKQLVSKF GPNNLQFQNP HDVAVTADGN EIYVAELNPM RIHKFVHRSL 430 440 450 460 470 480 AKPMSLSASK DSRDSAISQA VGGDQVPAVA VHHPSGKAIL VASLMLLFAG STFALALIFA 490 500 510 520 530 540 RRRKRGCLPF GARGRRHAWE KSDGFKLGGL LDRDRNGFEK LDQQASDEEQ ETKTLASAQY A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Drosophila uses two distinct neuropeptide amidating enzymes, dPAL1 and dPAL2." Han M., Park D., Vanderzalm P.J., Mains R.E., Eipper B.A., Taghert P.H. J. Neurochem. 90:129-141(2004) [PubMed: 15198673] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF58870.1. AY051842 mRNA. Translation: AAK93266.1.
RefSeq	NP_610537.2.
UniGene	Dm.548
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9V5E1.
Proteomic databases
PRIDE	Q9V5E1.
Genome annotation databases
Ensembl	FBtr0088385; FBpp0087473; FBgn0033466; Drosophila melanogaster. [Genome view]
GeneID	36033.
NMPDR	fig|7227.3.peg.4344.
UCSC	CG12130-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0033466. CG12130.
Phylogenomic databases
OMA	RGPIRES.
Enzyme and pathway databases
BRENDA	4.3.2.5. 48.
Gene expression databases
GermOnline	CG12130. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR001258. NHL_repeat. IPR013017. NHL_repeat_subgr. IPR000720. Pep_amidat_mOase. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
Pfam	PF01436. NHL. 4 hits. [Graphical view]
PRINTS	PR00790. PAMONOXGNASE.
PROSITE	PS51125. NHL. 4 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	796470.

Entry information

Entry name

PAL1_DROME

Accession

Primary (citable) accession number: Q9V5E1
Secondary accession number(s): Q960U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project