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Protein

Glycosyltransferase 25 family member

Gene

CG31915

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

GO - Biological processi

  1. lipopolysaccharide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_180755. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosyltransferase 25 family member (EC:2.-.-.-)
Gene namesi
ORF Names:CG31915
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0051915. CG31915.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 612592Glycosyltransferase 25 family memberPRO_0000309549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi263 – 2631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8IPK4.
PRIDEiQ8IPK4.

Expressioni

Gene expression databases

BgeeiQ8IPK4.

Structurei

3D structure databases

ProteinModelPortaliQ8IPK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi609 – 6124Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase 25 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
InParanoidiQ8IPK4.
KOiK11703.
OMAiPEESKMQ.
OrthoDBiEOG7060RC.
PhylomeDBiQ8IPK4.

Family and domain databases

InterProiIPR002654. Glyco_trans_25.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01755. Glyco_transf_25. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IPK4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKQVIFGLL LACILVCISG QDEEDYQESP TVLIALLVRN KAHILPMFLS
60 70 80 90 100
YLEQQDYPKE RIAIWLRCDH SNDDSIELLR QWLDNSGDLY HSVSYEFKPE
110 120 130 140 150
EQSFVNGTSP YEWPASRFKH LIALKEEAFQ YGRDIWADYV FFLDADVLLT
160 170 180 190 200
SKDSLKVLTR LQLPIVAPML ISESLYSNFW CGMTEDYYYR RTDEYKEIYH
210 220 230 240 250
VKKQGSFPVP MVHTAVLVNM NHRAVRNLTF DRNKLVELQK SRQQEPLYDG
260 270 280 290 300
PADDIIVFAI SANSSGIPLH ICNDITFGYI LQPLEPGDTL DHDVQQLVNL
310 320 330 340 350
KSIMVNELGA VPPLLDYYKH LEKKPEKSKL SLDRIFMINL KRRPERREKM
360 370 380 390 400
ERLFDEIGIE AEHFPAVDGK ELSTERLLEM GVRFLPGYED PYHHRAMTMG
410 420 430 440 450
EIGCFLSHYN IWVMMVRKQL KEVLILEDDI RFEPYFRQNA VRILNQARNA
460 470 480 490 500
AQYDLIYFGR KRLKEESEPA VENADNLVHA GYSYWTLGYV ISLQGALKLL
510 520 530 540 550
AAKPLDKLIP VDEFLPLMFD RHPNKTWTEA FPKRNLVAFS ASPLLLYPIY
560 570 580 590 600
YTGESGYISD TEDSQQISVE TSEEGEARLK SDREQVFDHE QEFKLNPELK
610
LGESLSKSHQ EL
Length:612
Mass (Da):71,149
Last modified:March 1, 2003 - v1
Checksum:i5719BCE07C7698B6
GO

Sequence cautioni

The sequence ABY21735.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAN10543.1.
BT031322 mRNA. Translation: ABY21735.1. Different initiation.
RefSeqiNP_723087.1. NM_164645.3.

Genome annotation databases

EnsemblMetazoaiFBtr0079099; FBpp0078732; FBgn0051915.
GeneIDi319025.
KEGGidme:Dmel_CG31915.
UCSCiCG31915-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAN10543.1.
BT031322 mRNA. Translation: ABY21735.1. Different initiation.
RefSeqiNP_723087.1. NM_164645.3.

3D structure databases

ProteinModelPortaliQ8IPK4.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

Proteomic databases

PaxDbiQ8IPK4.
PRIDEiQ8IPK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079099; FBpp0078732; FBgn0051915.
GeneIDi319025.
KEGGidme:Dmel_CG31915.
UCSCiCG31915-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0051915. CG31915.

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
InParanoidiQ8IPK4.
KOiK11703.
OMAiPEESKMQ.
OrthoDBiEOG7060RC.
PhylomeDBiQ8IPK4.

Enzyme and pathway databases

ReactomeiREACT_180755. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

GenomeRNAii319025.
NextBioi847004.

Gene expression databases

BgeeiQ8IPK4.

Family and domain databases

InterProiIPR002654. Glyco_trans_25.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01755. Glyco_transf_25. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiGLT25_DROME
AccessioniPrimary (citable) accession number: Q8IPK4
Secondary accession number(s): A9UNF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.