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Q5U483

- G251B_XENLA

UniProt

Q5U483 - G251B_XENLA

Protein

Procollagen galactosyltransferase 1-B

Gene

colgalt1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Protein family/group databases

    CAZyiGT25. Glycosyltransferase Family 25.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Procollagen galactosyltransferase 1-B (EC:2.4.1.50)
    Alternative name(s):
    Collagen beta(1-O)galactosyltransferase 1-B
    Glycosyltransferase 25 family member 1-B
    Hydroxylysine galactosyltransferase 1-B
    Gene namesi
    Name:colgalt1-b
    Synonyms:glt25d1-b
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6253736. colgalt1.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 611587Procollagen galactosyltransferase 1-BPRO_0000309540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5U483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi608 – 6114Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the glycosyltransferase 25 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG058097.
    KOiK11703.

    Family and domain databases

    Gene3Di3.90.550.10. 2 hits.
    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.

    Q5U483-1 [UniParc]FASTAAdd to Basket

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    MSQAGVERLL KGLQILVLVL RLSAGYFPEE RWNPESPFRS PTVLIAVLAR    50
    NSEGSLPEVL GALDRLHYPK ERISLWVATD HNFDNTSQIL REWLINVQNQ 100
    YHHVEWRPQE HPRWFRDEES PKHWSHSRYE YVMKLRQAAL TSAREMWADY 150
    IFFLDADNLL TNSETLNLLI AENKTVVAPM LESRAAYSNF WCGMTTQGYY 200
    RRTPAYMPIR RRERQGCFPV PMVHSTFLID LRKEASQQLD FYPPHADYTW 250
    AFDDIIVFAF SCRQAEVQMF LCNKEIYGYL PVPLRSHSTL LDETDNFLHT 300
    KLEAMVKGPQ VHPSSFVTIP KKVPDKMSFD EVFLINLKHR QDRRERMKRT 350
    LYELQIDFKL VDAVYGKMLN QSNVTEMGIK MLPGYKDPYH GRPLTRGEMG 400
    CFLSHYNIWK EISERNLEVS AVLEDDLRFE IFFKRRLQTL LHDLEIAKLD 450
    WDLIYLGRKR MQVDEPEEPV PGVRNLVVSD YSYWTLGYLI SLRGARKLLN 500
    AEPLGKMLPV DEFLPVMYDK HPISDYSSHF STRDLRAFSV EPLLLYPTHY 550
    TGDKGYISDT ETSVLWDNVT QPTDWDRAKS RKTHQQEKLR SEALNTPSMG 600
    SPFDNTARDE L 611
    Length:611
    Mass (Da):71,607
    Last modified:December 7, 2004 - v1
    Checksum:i63AED42791D52B08
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC085226 mRNA. Translation: AAH85226.1.
    RefSeqiNP_001088623.1. NM_001095154.1.
    UniGeneiXl.13613.

    Genome annotation databases

    GeneIDi495521.
    KEGGixla:495521.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC085226 mRNA. Translation: AAH85226.1 .
    RefSeqi NP_001088623.1. NM_001095154.1.
    UniGenei Xl.13613.

    3D structure databases

    ProteinModelPortali Q5U483.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT25. Glycosyltransferase Family 25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 495521.
    KEGGi xla:495521.

    Organism-specific databases

    CTDi 495521.
    Xenbasei XB-GENE-6253736. colgalt1.

    Phylogenomic databases

    HOVERGENi HBG058097.
    KOi K11703.

    Family and domain databases

    Gene3Di 3.90.550.10. 2 hits.
    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. NIH - Xenopus Gene Collection (XGC) project
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiG251B_XENLA
    AccessioniPrimary (citable) accession number: Q5U483
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3