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Reviewed, UniProtKB/Swiss-Prot Q9V5E1 (PAL1_DROME)

Last modified February 9, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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. Ref.4

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. Ref.4

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 541508Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 1
PRO_0000248573

Regions

Topological domain34 – 458425Extracellular Potential
Transmembrane459 – 47921 Potential
Topological domain480 – 54162Cytoplasmic Potential
Repeat164 – 20542NHL 1
Repeat215 – 25844NHL 2
Repeat272 – 31443NHL 3
Repeat374 – 41845NHL 4

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Disulfide bond228 ↔ 248 By similarity
Disulfide bond299 ↔ 310 By similarity

Experimental info

Sequence conflict2531L → F in AAK93266. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q9V5E1-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A3C6E43F5AE5B148

FASTA54159,642
        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

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References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAF58870.1.
AY051842 mRNA. Translation: AAK93266.1.
RefSeqNP_610537.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9V5E1.

Proteomic databases

PRIDEQ9V5E1.

Genome annotation databases

EnsemblFBtr0088385; FBpp0087473; FBgn0033466; Drosophila melanogaster. [Genome view]
FBtr0273269; FBpp0271777; FBgn0033466; Drosophila melanogaster. [Genome view]
GeneID36033.
NMPDRfig|7227.3.peg.4344.
UCSCCG12130-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0033466. CG12130.

Phylogenomic databases

eggNOGinNOG07787.
InParanoidQ9V5E1.
OMARGPIRES.
PhylomeDBQ9V5E1.

Enzyme and pathway databases

BRENDA4.3.2.5. 48.

Gene expression databases

GermOnlineCG12130. Drosophila melanogaster.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR013017. NHL_repeat_subgr.
IPR000720. Pep_amidat_mOase.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
PRINTSPR00790. PAMONOXGNASE.
PROSITEPS51125. NHL. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio796470.

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Entry information

Entry namePAL1_DROME
AccessionPrimary (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: February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents