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Reviewed, UniProtKB/Swiss-Prot Q04499 (PROD_DROME)

Last modified November 3, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proline dehydrogenase, mitochondrial
    EC=1.5.99.8
Alternative name(s):
    Proline oxidase
    Protein sluggish-A
Gene names
Name: slgA
Synonyms: slg
ORF Names: CG1417
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length681 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts proline to delta-1-pyrroline-5-carboxylate. Ref.1

Catalytic activity

L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.

Cofactor

FAD.

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.

Subcellular location

Mitochondrion matrix. Ref.1

Tissue specificity

Most abundant in developing nervous system. Ref.1

Developmental stage

Expressed in developing embryo as well as in adult. Ref.1

Disruption phenotype

Flies exhibit reduced proline oxidase activity which produces sluggish behavior. Ref.1

Sequence similarities

Belongs to the proline oxidase family.

Ontologies

Keywords
   Biological processProline metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamate biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

phototaxis

Inferred from mutant phenotype. Source: FlyBase

proline catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionproline dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: Q04499-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform A (identifier: Q04499-2)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     158-192: LARNLLGQKLFVLLMKSSFYGHFVAGENRHTIVPA → WSKNVLGQRLFTLLMKATFYGHFVAGEDQIKIIPT
     285-296: Missing.
Isoform B (identifier: Q04499-3)

The sequence of this isoform differs from the canonical sequence as follows:
     285-296: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: Q04499-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-325: Missing.
Note: No experimental confirmation available.
Isoform E (identifier: Q04499-5)

The sequence of this isoform differs from the canonical sequence as follows:
     158-192: LARNLLGQKLFVLLMKSSFYGHFVAGENRHTIVPA → WSKNVLGQRLFTLLMKATFYGHFVAGEDQIKIIPT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Potential
Chain31 – 681651Proline dehydrogenase, mitochondrial
PRO_0000025803

Natural variations

Alternative sequence1 – 325325Missing in isoform C.
VSP_015400
Alternative sequence158 – 19235LARNL…TIVPA → WSKNVLGQRLFTLLMKATFY GHFVAGEDQIKIIPT in isoform A and isoform E.
VSP_015401
Alternative sequence285 – 29612Missing in isoform A and isoform B.
VSP_015402

Experimental info

Sequence conflict421S → N in AAA02748. Ref.1
Sequence conflict1471K → N in AAA02748. Ref.1
Sequence conflict1491V → F in AAC28410. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform D [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 2AB69ABB67D83FF8

FASTA68177,153
        10         20         30         40         50         60 
MALLRSLSAQ RTAISLVYGR NSSKSSNSVA VAACRSFHQR GSGSTSIAGE GAASESTRGV 

        70         80         90        100        110        120 
NGARFLHSGD RPLQASTLVQ PEVVSSETVK RSMKQESSQE KNPSPAGSPQ RDPLDVSFND 

       130        140        150        160        170        180 
PIAAFKSKTT GELIRAYLVY MICSSEKLVE HNMTLMKLAR NLLGQKLFVL LMKSSFYGHF 

       190        200        210        220        230        240 
VAGENRHTIV PALERLRSFG VKPILDYSVE EDITQEEAEK REVESSVSSA GDKKEEGSMP 

       250        260        270        280        290        300 
QYHVDKSFAD RRYKVSSART YFYLNEATCE RNMEIFIKCL EAVSDDDRKA PRAVATGATF 

       310        320        330        340        350        360 
GTGITAIKLT ALGRPQLLLQ LSEVIMRTRK YMEDMVGGQG NVLTHHKTIK DLEKYYATLG 

       370        380        390        400        410        420 
DNKDVKEFLN NVTSDKEGIL HLFPWSGIVD EDSQLSDTFR VPDPQTGQMR RLISQIPPKE 

       430        440        450        460        470        480 
EEMFRNMIRR LNTIVKAAAD LDVRIMVDAE QTYFQPAISR ITLEMMRKYN KDKAIVFNTY 

       490        500        510        520        530        540 
QCYLRETFRE VNTDLEQAKR QNFYFGAKLV RGAYMDQERD RAKSLGYPDP VNPTFEATTD 

       550        560        570        580        590        600 
MYHRTLSECL RRIKLMKDCD DDARKIGIMV ASHNEDTVRF AIQQMKEIGI SPEDKVICFG 

       610        620        630        640        650        660 
QLLGMCDYIT FPLGQAGYSA YKYIPYGPVE EVLPYLSRRA QENKGVLKKI KKEKRLLLSE 

       670        680 
IRRRLMRGQL FYKPKGNYVP I 

« Hide

Isoform A (F).

Checksum: 89C68093DF0D82EE
Show »

FASTA66975,952
Isoform B.

Checksum: 976800739C0839CC
Show »

FASTA66975,857
Isoform C.

Checksum: F1A5FF82FD03142C
Show »

FASTA35641,558
Isoform E.

Checksum: 783D5C065E1EC77A
Show »

FASTA68177,248

References

« Hide 'large scale' references
[1]"The sluggish-A gene of Drosophila melanogaster is expressed in the nervous system and encodes proline oxidase, a mitochondrial enzyme involved in glutamate biosynthesis."
Hayward D.C., Delaney S.J., Campbell H.D., Ghysen A., Benzer S., Kasprzak A.B., Cotsell J.N., Young I.G., Miklos G.L.G.
Proc. Natl. Acad. Sci. U.S.A. 90:2979-2983(1993) [PubMed: 8096642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: Canton-S.
[2]"Data transferability from model organisms to human beings: insights from the functional genomics of the flightless region of Drosophila."
Maleszka R., de Couet H.G., Miklos G.L.G.
Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998) [PubMed: 9520435] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
Strain: Canton-S.
[3]"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.
[4]"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, ALTERNATIVE SPLICING.
[5]"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] (ISOFORM A).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

L07330 mRNA. Translation: AAA02748.1.
AF017777 Genomic DNA. Translation: AAC28410.1.
AE014298 Genomic DNA. Translation: AAF50814.2.
AE014298 Genomic DNA. Translation: AAF50819.2.
AE014298 Genomic DNA. Translation: AAF50820.2.
AE014298 Genomic DNA. Translation: AAF50821.1.
AE014298 Genomic DNA. Translation: AAF50822.3.
AY069407 mRNA. Translation: AAL39552.1.
PIRA47302.
RefSeqNP_523433.2.
NP_728422.1.
NP_728423.1.
NP_728424.1.
NP_728425.1.
NP_996526.1.
NP_996527.1.
NP_996528.1.
UniGeneDm.6612

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ04499. 20 interactions.
STRINGQ04499.

Genome annotation databases

EnsemblFBtr0077204; FBpp0076903; FBgn0003423; Drosophila melanogaster. [Genome view]
GeneID33117.
KEGGdme:Dmel_CG1417.

Organism-specific databases

CTD33117.
FlyBaseFBgn0003423. slgA.

Phylogenomic databases

OMAMESCTSA.

Enzyme and pathway databases

BRENDA1.5.99.8. 48.

Gene expression databases

BgeeQ04499.
GermOnlineCG1417. Drosophila melanogaster.

Family and domain databases

InterProIPR002872. Proline_DH.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERPTHR13914. Proline_oxidase. 1 hit.
PfamPF01619. Pro_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio781979.

Entry information

Entry namePROD_DROME
AccessionPrimary (citable) accession number: Q04499
Secondary accession number(s): O61349 expand/collapse secondary AC list , Q8IQ45, Q8IQ46, Q8T0C7, Q9VRH7, Q9VRH8, Q9VRH9, Q9VRI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: August 30, 2005
Last modified: November 3, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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