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Reviewed, UniProtKB/Swiss-Prot Q8MT80 (PIGZ_DROME)

Last modified November 4, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
    GPI mannosyltransferase 4
    EC=2.4.1.-
Alternative name(s):
    GPI mannosyltransferase IV
      Short name=GPI-MT-IV
Gene names
ORF Names: CG3419
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 length696 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane proteinBy similarity.

Sequence similarities

Belongs to the glycosyltransferase 22 family. PIGZ subfamily.

Sequence caution

The sequence AAF47201.1 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords

   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processGPI anchor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionalpha-1,2-mannosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 696696GPI mannosyltransferase 4
PRO_0000246270

Regions

Transmembrane100 – 12021 Potential
Transmembrane125 – 14218 Potential
Transmembrane149 – 16921 Potential
Transmembrane185 – 20521 Potential
Transmembrane227 – 24721 Potential
Transmembrane338 – 35821 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8MT80-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: DCB78A0FEE0E5799

FASTA69680,217
        10         20         30         40         50         60 
MRLTTLWQNR SPGDRHLSTY FCFAAVRLLL VFVPQLGYVH PDEFFQSVEV MTGDHFRLEH 

        70         80         90        100        110        120 
TRTWEFNNSL PVRSIVLPFA LLRIPWSFYE FVAECLKAWW QLELLGTYAY VVFPRLIYTL 

       130        140        150        160        170        180 
ISFSNDYCLF RICRLYGLRF EIRLLAMGSS WILLVFGTRT FSNSLEMAMC SWLLCLVSEC 

       190        200        210        220        230        240 
MLRTNTVVYK KEFLEEKYDK AESISERVRI WKLKNSLPAH NLQHLMAMST ICVAGVFNRP 

       250        260        270        280        290        300 
TFLLFGAPMV FFWLLRGMGT RSITFRDFNL RIALFCLCAL PALVLFIFCD SLYYQHLTLG 

       310        320        330        340        350        360 
ELHMMHLSID NFVFTPWNFI KANLDSAQTA SHGVHPCYVH LMVNMPMLFN VLALASLGAF 

       370        380        390        400        410        420 
AQLLLRFFRA EYQVLPRFQS IVSLMSGAIF VPLFFLSLIN HQEPRFLLPV TFPLILLHAP 

       430        440        450        460        470        480 
KLITGFSAKY PFQKDHPLLR LFYDKLLSSK ASGPYLLKIW YVSNVALTLF FGFIHQAGVY 

       490        500        510        520        530        540 
PLAADISHVI ATKPAATHVH LITSHIYSLP LHLINIPSSR VLHFNRLTHQ RYRRPRDFYM 

       550        560        570        580        590        600 
YEYGGLPLDS LLQKVKLISG SCEVKKSGPS RRRYKLYLAI PASLSADLHE ALVHSNASSY 

       610        620        630        640        650        660 
LNFELLKVFY PHLSTEAFPH LQGRHPCDVD APHWAHDDLR GTCSAEQLPA FSFAYLNKQF 

       670        680        690 
SSFVHQLGLA LYEIDVTRNK PRSVVIKKAS MTETAA

« Hide

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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.

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Cross-references

Sequence databases

AE013599 Genomic DNA. Translation: AAF47201.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAS64768.1.
AY118320 mRNA. Translation: AAM48349.1.
RefSeqNP_611909.1.
NP_995937.1.
UniGeneDm.13579

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8MT80.

Genome annotation databases

EnsemblCG3419. Drosophila melanogaster. [Contig view]
GeneID37896.
KEGGdme:Dmel_CG3419.

Organism-specific databases

FlyBaseFBgn0035002. CG3419.

Gene expression databases

ArrayExpressQ8MT80.
GermOnlineCG3419. Drosophila melanogaster.

Family and domain databases

InterProIPR005599. Alg9_trans.
[Graphical view]
PANTHERPTHR22760. Alg9_trans. 1 hit.
PfamPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio805927.

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Entry information

Entry namePIGZ_DROME
AccessionPrimary (citable) accession number: Q8MT80
Secondary accession number(s): Q9W176
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2002
Last modified: November 4, 2008
This is version 48 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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