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Q8K297 (GT251_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Note: Colocalized with PLOD3 and mannose binding lectin By similarity.

Post-translational modification

N-glycosylated 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 – 3131 Potential
Chain32 – 617586Procollagen galactosyltransferase 1
PRO_0000309537

Regions

Motif614 – 6174Prevents secretion from ER By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Ref.3
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict81S → L in BAE43293. Ref.1
Sequence conflict301D → A in BAE43293. Ref.1
Sequence conflict2501T → P in AAH32165. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8K297 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 828D28E3300D9CC6

FASTA61771,061
        10         20         30         40         50         60 
MAALPRGSRG LPLLPLLLLL PPLGGPRGAD GYFPEERWSP ESPLQAPRVL IALLARNAAP 

        70         80         90        100        110        120 
ALPATLGALE QLRHPRERTA LWVATDHNTD NTSAILREWL VAVKGLYHSV EWRPAEEPSS 

       130        140        150        160        170        180 
YPDEEGPKHW SDSRYEHVMK LRQAALKSAR DMWADYILFM DIDNLITNPD TLSLLIAENK 

       190        200        210        220        230        240 
TVVAPMLDSR AAYSNFWCGM TSQGYYKRTP AYIPIRKRDR RGCFAVPMVH STFLIDLRKA 

       250        260        270        280        290        300 
ASRNLAFYPT HPDYTWSFDD IIVFAFSCKQ AEVQMYVCNK EVYGFLPVPL RAHSSLQDEA 

       310        320        330        340        350        360 
ESFMHVQLEV MVKHPPVQLS RFISAPRKTS DKMGFDEVFM INLKRRRDRR ERMLRALHEQ 

       370        380        390        400        410        420 
EIDCQLVEAV DGKAMNTSQV EAMGIQMLPG YRDPYHGRPL TKGELGCFLS HYNIWKEVVD 

       430        440        450        460        470        480 
RGLQKSLVFE DDLRFEIFFK RRLMNLMRDV EREGLDWDLI YVGRKRMQVE HPEKAVPHVR 

       490        500        510        520        530        540 
NLVEADYSYW TLAYVISLQG AQKLLAAKPL AKMLPVDEFL PVMFDKHPMS EYKSHFSPRN 

       550        560        570        580        590        600 
LRAFSVEPLL IYPTHYTGDD GYVSDTETSV VWNNEQVKTD WDRAKSQKMR EQQALSREAK 

       610 
NSDVLQSPLD STARDEL 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary tumor.
[3]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK035788 mRNA. Translation: BAE43293.1.
BC032165 mRNA. Translation: AAH32165.1.
BC056951 mRNA. Translation: AAH56951.1.
RefSeqNP_666323.2. NM_146211.3.
UniGeneMm.273836.
Mm.334606.

3D structure databases

ProteinModelPortalQ8K297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231529. 1 interaction.
IntActQ8K297. 1 interaction.
MINTMINT-1866727.

Protein family/group databases

CAZyGT25. Glycosyltransferase Family 25.

PTM databases

PhosphoSiteQ8K297.

Proteomic databases

PaxDbQ8K297.
PRIDEQ8K297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047903; ENSMUSP00000047923; ENSMUSG00000034807.
GeneID234407.
KEGGmmu:234407.
UCSCuc009mee.2. mouse.

Organism-specific databases

CTD234407.
MGIMGI:1924348. Colgalt1.

Phylogenomic databases

eggNOGNOG293154.
GeneTreeENSGT00550000074427.
HOGENOMHOG000007198.
HOVERGENHBG058097.
InParanoidQ8K297.
KOK11703.
OMAMWADYIL.
OrthoDBEOG7060RC.
PhylomeDBQ8K297.
TreeFamTF313826.

Gene expression databases

BgeeQ8K297.
CleanExMM_GLT25D1.
GenevestigatorQ8K297.

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

ChiTaRSGLT25D1. mouse.
NextBio382175.
PROQ8K297.
SOURCESearch...

Entry information

Entry nameGT251_MOUSE
AccessionPrimary (citable) accession number: Q8K297
Secondary accession number(s): Q3V3R5, Q6PGL1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 87 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot