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UniProtKB/Swiss-Prot entry Q9W1L5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PAL2_DROME
Primary accession number Q9W1L5
Secondary accession numbers Q7KVI0 Q9GPF3
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on October 1, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 46)
Name and origin of the protein
Protein name Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 2 [Precursor]
Synonyms EC 4.3.2.5
Peptidylamidoglycolate lyase 2
dPAL2
Gene name
Name: Pal
Synonyms: PAL2
ORFNames: CG5472
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Williamson M., Grimmelikhuijzen C.J.P.;
"Molecular cloning of a peptidyl-alpha-hydroxyglycine alpha-amidating lyase from Drosophila melanogaster.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
DOI=10.1111/j.1471-4159.2004.02464.x; PubMed=15198673 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY007228; AAG01895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF47043.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAS64762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY119165; AAM51025.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_525118.2; -.
NP_995930.1; -.
UniGene Dm.1661
3D structure databases
ModBase Q9W1L5.
Organism-specific databases
FlyBase FBgn0020623; Pal.
Gene expression databases
ArrayExpress Q9W1L5; -.
GermOnline CG5472; Drosophila melanogaster.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from direct assay from UniProtKB).
GO:0004598; Molecular function: peptidylamidoglycolate lyase activity (inferred from mutant phenotype from UniProtKB).
GO:0044237; Biological process: cellular metabolic process (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011042; 6-blade_b-propeller_TolB-like.
IPR001258; NHL_repeat.
IPR013017; NHL_repeat_subgr.
Graphical view of domain structure.
Gene3D G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
Pfam PF01436; NHL; 4.
Pfam graphical view of domain structure.
PROSITE PS51125; NHL; 4.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9W1L5.
Genome annotation databases
Ensembl CG5472; Drosophila melanogaster. [Contig view]
GeneID 37746; -.
KEGG dme:Dmel_CG5472; -.
Other
ProtoNet Q9W1L5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Glycoprotein; Lyase; Metal-binding; Repeat; Secreted; Signal; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   406  387     Peptidyl-alpha-hydroxyglycine alpha-amidating lyase 2. PRO_0000248574
REPEAT   168   209  42     NHL 1. 
REPEAT   218   261  44     NHL 2. 
REPEAT   264   308  45     NHL 3. 
REPEAT   358   402  45     NHL 4. 
DISULFID   231   251        By similarity. 
DISULFID   293   304        By similarity. 
VAR_SEQ   204   205        Missing (in isoform 2). VSP_020314
CONFLICT   13    13        S -> T (in Ref. 1; AAG01895). 
CONFLICT   16    16        Y -> C (in Ref. 1; AAG01895). 
CONFLICT   40    40        N -> S (in Ref. 1; AAG01895). 
CONFLICT   382   382        N -> S (in Ref. 1; AAG01895). 
Sequence information
Length: 406 AA [This is the length of the unprocessed precursor] Molecular weight: 44712 Da [This is the MW of the unprocessed precursor] CRC64: 47E6037A41071DF9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRLLFVALL AISLGYVASS SSNHLPAGLA MDLGPGVNLN ERFFDQVRAL IKRRLQEKGL 

        70         80         90        100        110        120 
AKPEQPELAM PLTDDDAVAL QNQRSYDNVP LPAASVPTPV LVENWPTEQH SFGQVTAVAV 

       130        140        150        160        170        180 
DPQGSPVVFH RAERYWDVNT FNESNIYYLI EYGPIKENTI YVLDAKTGAI KSGWGSNMFY 

       190        200        210        220        230        240 
MPHGLTIDLH GNYWITDVAM HQAFKFKPFS NKPLLTIGKR FRPGSSVKHL CKPTSIAVAT 

       250        260        270        280        290        300 
TGEFFIADGY CNSRILKFNA AGKLLRTIPQ PPEFLSLQVP HAITLLEHLD LLCIADRENM 

       310        320        330        340        350        360 
RVVCPKAGLI SSHGEGEPAA TIQEPDLGRV FGVASFGDIV FAVNGPTSML PVRGFTIDPR 

       370        380        390        400 
SETIIGHWGE FKNPHSMAVS VNGSALYVTE IGTNHQTNRV WKYVLA 

Q9W1L5 in FASTA format

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View entry in raw text format (no links)
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