GLT25_DROME
ID GLT25_DROME Reviewed; 612 AA.
AC Q8IPK4; A9UNF8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glycosyltransferase 25 family member;
DE EC=2.-.-.-;
DE Flags: Precursor;
GN ORFNames=CG31915;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABY21735.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAN10543.1; -; Genomic_DNA.
DR EMBL; BT031322; ABY21735.1; ALT_INIT; mRNA.
DR RefSeq; NP_723087.1; NM_164645.3.
DR AlphaFoldDB; Q8IPK4; -.
DR SMR; Q8IPK4; -.
DR STRING; 7227.FBpp0078732; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyGen; Q8IPK4; 4 sites.
DR PaxDb; Q8IPK4; -.
DR PRIDE; Q8IPK4; -.
DR DNASU; 319025; -.
DR EnsemblMetazoa; FBtr0079099; FBpp0078732; FBgn0051915.
DR GeneID; 319025; -.
DR KEGG; dme:Dmel_CG31915; -.
DR UCSC; CG31915-RA; d. melanogaster.
DR FlyBase; FBgn0051915; CG31915.
DR VEuPathDB; VectorBase:FBgn0051915; -.
DR eggNOG; KOG2540; Eukaryota.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q8IPK4; -.
DR OMA; KRTGCFA; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q8IPK4; -.
DR Reactome; R-DME-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 319025; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 319025; -.
DR PRO; PR:Q8IPK4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051915; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR Genevisible; Q8IPK4; DM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:FlyBase.
DR GO; GO:0050211; F:procollagen galactosyltransferase activity; ISS:FlyBase.
DR GO; GO:1904028; P:positive regulation of collagen fibril organization; ISS:FlyBase.
DR CDD; cd06532; Glyco_transf_25; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002654; Glyco_trans_25.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01755; Glyco_transf_25; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..612
FT /note="Glycosyltransferase 25 family member"
FT /id="PRO_0000309549"
FT MOTIF 609..612
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 612 AA; 71149 MW; 5719BCE07C7698B6 CRC64;
MNKQVIFGLL LACILVCISG QDEEDYQESP TVLIALLVRN KAHILPMFLS YLEQQDYPKE
RIAIWLRCDH SNDDSIELLR QWLDNSGDLY HSVSYEFKPE EQSFVNGTSP YEWPASRFKH
LIALKEEAFQ YGRDIWADYV FFLDADVLLT SKDSLKVLTR LQLPIVAPML ISESLYSNFW
CGMTEDYYYR RTDEYKEIYH VKKQGSFPVP MVHTAVLVNM NHRAVRNLTF DRNKLVELQK
SRQQEPLYDG PADDIIVFAI SANSSGIPLH ICNDITFGYI LQPLEPGDTL DHDVQQLVNL
KSIMVNELGA VPPLLDYYKH LEKKPEKSKL SLDRIFMINL KRRPERREKM ERLFDEIGIE
AEHFPAVDGK ELSTERLLEM GVRFLPGYED PYHHRAMTMG EIGCFLSHYN IWVMMVRKQL
KEVLILEDDI RFEPYFRQNA VRILNQARNA AQYDLIYFGR KRLKEESEPA VENADNLVHA
GYSYWTLGYV ISLQGALKLL AAKPLDKLIP VDEFLPLMFD RHPNKTWTEA FPKRNLVAFS
ASPLLLYPIY YTGESGYISD TEDSQQISVE TSEEGEARLK SDREQVFDHE QEFKLNPELK
LGESLSKSHQ EL