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Protein

Procollagen galactosyltransferase 1

Gene

colgalt1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_298707. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:colgalt1
Synonyms:glt25d1
ORF Names:si:ch211-114l13.7, zgc:110667
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 1

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 604586Procollagen galactosyltransferase 1PRO_0000309538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Gene expression databases

BgeeiA5PMF6.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000075565.

Structurei

3D structure databases

ProteinModelPortaliA5PMF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi601 – 6044Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase 25 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
InParanoidiA5PMF6.
KOiK11703.
OMAiMWADYIL.
OrthoDBiEOG7060RC.
PhylomeDBiA5PMF6.
TreeFamiTF313826.

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.

A5PMF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLCFFFLL LWTGPARSYF PEERWSPESA LLAPRVLVAL VCRNSAHSLP
60 70 80 90 100
HVLGAIDRLN YPKDRMAVWV ATDHNSDNTT EILREWLVNV QNFYHYVEWR
110 120 130 140 150
PQDEPSVYEG ESGPKHWTNL RYEHVMKLRQ AALETAREMW ADYFMLVDCD
160 170 180 190 200
NLLTNRDVLW KLMRENKTIV APMLESRAAY SNFWCGMTSQ GYYKRTPAYM
210 220 230 240 250
PIRRQERKGC FAVPMVHSTL LLDLRKEASR QLAFFPPHPD YTWAFDDIII
260 270 280 290 300
FAFSARMAEV QMYICNRETY GYFPVPLRSQ NSLQDEAESF LHSQLEVMVR
310 320 330 340 350
NPPIEPSVYL SLMPKQTDKM GFDEVFMINL LRRSDRRERM LRTLYEQEIA
360 370 380 390 400
CKIITAVDGK ALNASQVEAL GIKMLPGYSD PYHGRPLTKG ELGCFLSHYN
410 420 430 440 450
IWNEIVDRGL QSSLVIEDDL RFEVFFKRRL QNLMQEVQSQ QLDWDLIYIG
460 470 480 490 500
RKRMQVERPE KSVPRIHSLV EADYSYWTLG YVISLRGAQK LLRAEPLKKM
510 520 530 540 550
LPVDEFLPVM YNKHPIEEYM SHFPQRDLRA FSAEPLLIYP THYTGDQGYI
560 570 580 590 600
SDTETSSVWD NESVLTDWDR ARSRKSREQE ELSSEAQNTD VLQSPLDSTA

RDEL
Length:604
Mass (Da):70,832
Last modified:July 10, 2007 - v1
Checksum:i7D9556D629E4BF7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX469930 Genomic DNA. Translation: CAN87888.1.
RefSeqiNP_001103992.1. NM_001110522.1.
UniGeneiDr.135672.

Genome annotation databases

EnsembliENSDART00000081122; ENSDARP00000075565; ENSDARG00000058270.
GeneIDi567859.
KEGGidre:567859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX469930 Genomic DNA. Translation: CAN87888.1.
RefSeqiNP_001103992.1. NM_001110522.1.
UniGeneiDr.135672.

3D structure databases

ProteinModelPortaliA5PMF6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000075565.

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000081122; ENSDARP00000075565; ENSDARG00000058270.
GeneIDi567859.
KEGGidre:567859.

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
InParanoidiA5PMF6.
KOiK11703.
OMAiMWADYIL.
OrthoDBiEOG7060RC.
PhylomeDBiA5PMF6.
TreeFamiTF313826.

Enzyme and pathway databases

ReactomeiREACT_298707. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi20888883.
PROiA5PMF6.

Gene expression databases

BgeeiA5PMF6.

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

  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.
    , 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.

Entry informationi

Entry nameiGT251_DANRE
AccessioniPrimary (citable) accession number: A5PMF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 10, 2007
Last modified: April 29, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.