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A5PMF6 (GT251_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Procollagen galactosyltransferase 1

EC=2.4.1.50
Alternative name(s):
Collagen beta(1-O)galactosyltransferase 1
Glycosyltransferase 25 family member 1
Hydroxylysine galactosyltransferase 1
Gene names
Name:colgalt1
Synonyms:glt25d1
ORF Names:si:ch211-114l13.7, zgc:110667
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen By similarity.

Catalytic activity

UDP-alpha-D-galactose + 5-hydroxy-L-lysine-[procollagen] = UDP + 5-(D-galactosyloxy)-L-lysine-[procollagen].

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the glycosyltransferase 25 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprocollagen galactosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 604586Procollagen galactosyltransferase 1
PRO_0000309538

Regions

Motif601 – 6044Prevents secretion from ER By similarity

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A5PMF6 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 7D9556D629E4BF7D

FASTA60470,832
        10         20         30         40         50         60 
MHLLCFFFLL LWTGPARSYF PEERWSPESA LLAPRVLVAL VCRNSAHSLP HVLGAIDRLN 

        70         80         90        100        110        120 
YPKDRMAVWV ATDHNSDNTT EILREWLVNV QNFYHYVEWR PQDEPSVYEG ESGPKHWTNL 

       130        140        150        160        170        180 
RYEHVMKLRQ AALETAREMW ADYFMLVDCD NLLTNRDVLW KLMRENKTIV APMLESRAAY 

       190        200        210        220        230        240 
SNFWCGMTSQ GYYKRTPAYM PIRRQERKGC FAVPMVHSTL LLDLRKEASR QLAFFPPHPD 

       250        260        270        280        290        300 
YTWAFDDIII FAFSARMAEV QMYICNRETY GYFPVPLRSQ NSLQDEAESF LHSQLEVMVR 

       310        320        330        340        350        360 
NPPIEPSVYL SLMPKQTDKM GFDEVFMINL LRRSDRRERM LRTLYEQEIA CKIITAVDGK 

       370        380        390        400        410        420 
ALNASQVEAL GIKMLPGYSD PYHGRPLTKG ELGCFLSHYN IWNEIVDRGL QSSLVIEDDL 

       430        440        450        460        470        480 
RFEVFFKRRL QNLMQEVQSQ QLDWDLIYIG RKRMQVERPE KSVPRIHSLV EADYSYWTLG 

       490        500        510        520        530        540 
YVISLRGAQK LLRAEPLKKM LPVDEFLPVM YNKHPIEEYM SHFPQRDLRA FSAEPLLIYP 

       550        560        570        580        590        600 
THYTGDQGYI SDTETSSVWD NESVLTDWDR ARSRKSREQE ELSSEAQNTD VLQSPLDSTA 


RDEL 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX469930 Genomic DNA. Translation: CAN87888.1.
RefSeqNP_001103992.1. NM_001110522.1.
UniGeneDr.135672.

3D structure databases

ProteinModelPortalA5PMF6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000075565.

Protein family/group databases

CAZyGT25. Glycosyltransferase Family 25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000081122; ENSDARP00000075565; ENSDARG00000058270.
GeneID567859.
KEGGdre:567859.

Phylogenomic databases

eggNOGNOG293154.
GeneTreeENSGT00550000074427.
HOGENOMHOG000007198.
HOVERGENHBG058097.
KOK11703.
OMAMWADYIL.
OrthoDBEOG7060RC.
PhylomeDBA5PMF6.
TreeFamTF313826.

Gene expression databases

BgeeA5PMF6.

Family and domain databases

InterProIPR002654. Glyco_trans_25.
[Graphical view]
PfamPF01755. Glyco_transf_25. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20888883.

Entry information

Entry nameGT251_DANRE
AccessionPrimary (citable) accession number: A5PMF6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families