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A5PMF6

- GT251_DANRE

UniProt

A5PMF6 - GT251_DANRE

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Protein
Procollagen galactosyltransferase 1
Gene
colgalt1, glt25d1, si:ch211-114l13.7, zgc:110667
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - 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

  1. procollagen galactosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_222767. 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: Chromosome 1

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 604586Procollagen galactosyltransferase 1
PRO_0000309538Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Expressioni

Gene expression databases

BgeeiA5PMF6.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000075565.

Structurei

3D structure databases

ProteinModelPortaliA5PMF6.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi601 – 6044Prevents secretion from ER By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
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

MHLLCFFFLL LWTGPARSYF PEERWSPESA LLAPRVLVAL VCRNSAHSLP    50
HVLGAIDRLN YPKDRMAVWV ATDHNSDNTT EILREWLVNV QNFYHYVEWR 100
PQDEPSVYEG ESGPKHWTNL RYEHVMKLRQ AALETAREMW ADYFMLVDCD 150
NLLTNRDVLW KLMRENKTIV APMLESRAAY SNFWCGMTSQ GYYKRTPAYM 200
PIRRQERKGC FAVPMVHSTL LLDLRKEASR QLAFFPPHPD YTWAFDDIII 250
FAFSARMAEV QMYICNRETY GYFPVPLRSQ NSLQDEAESF LHSQLEVMVR 300
NPPIEPSVYL SLMPKQTDKM GFDEVFMINL LRRSDRRERM LRTLYEQEIA 350
CKIITAVDGK ALNASQVEAL GIKMLPGYSD PYHGRPLTKG ELGCFLSHYN 400
IWNEIVDRGL QSSLVIEDDL RFEVFFKRRL QNLMQEVQSQ QLDWDLIYIG 450
RKRMQVERPE KSVPRIHSLV EADYSYWTLG YVISLRGAQK LLRAEPLKKM 500
LPVDEFLPVM YNKHPIEEYM SHFPQRDLRA FSAEPLLIYP THYTGDQGYI 550
SDTETSSVWD NESVLTDWDR ARSRKSREQE ELSSEAQNTD VLQSPLDSTA 600
RDEL 604
Length:604
Mass (Da):70,832
Last modified:July 10, 2007 - v1
Checksum:i7D9556D629E4BF7D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BX469930 Genomic DNA. Translation: CAN87888.1 .
RefSeqi NP_001103992.1. NM_001110522.1.
UniGenei Dr.135672.

3D structure databases

ProteinModelPortali A5PMF6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000075565.

Protein family/group databases

CAZyi GT25. Glycosyltransferase Family 25.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000081122 ; ENSDARP00000075565 ; ENSDARG00000058270 .
GeneIDi 567859.
KEGGi dre:567859.

Phylogenomic databases

eggNOGi NOG293154.
GeneTreei ENSGT00550000074427.
HOGENOMi HOG000007198.
HOVERGENi HBG058097.
KOi K11703.
OMAi MWADYIL.
OrthoDBi EOG7060RC.
PhylomeDBi A5PMF6.
TreeFami TF313826.

Enzyme and pathway databases

Reactomei REACT_222767. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi 20888883.

Gene expression databases

Bgeei A5PMF6.

Family and domain databases

InterProi IPR002654. Glyco_trans_25.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF01755. Glyco_transf_25. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 59 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

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