Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Procollagen galactosyltransferase 1

Gene

Colgalt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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_198984. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1924348. Colgalt1.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation
Note: Colocalized with PLOD3 and mannose binding lectin.By similarity

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
  2. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 617586Procollagen galactosyltransferase 1PRO_0000309537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)1 Publication
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8K297.
PaxDbiQ8K297.
PRIDEiQ8K297.

PTM databases

PhosphoSiteiQ8K297.

Expressioni

Gene expression databases

BgeeiQ8K297.
CleanExiMM_GLT25D1.
GenevestigatoriQ8K297.

Interactioni

Protein-protein interaction databases

BioGridi231529. 2 interactions.
IntActiQ8K297. 1 interaction.
MINTiMINT-1866727.

Structurei

3D structure databases

ProteinModelPortaliQ8K297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi614 – 6174Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyltransferase 25 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
InParanoidiQ8K297.
KOiK11703.
OMAiMWADYIL.
OrthoDBiEOG7060RC.
PhylomeDBiQ8K297.
TreeFamiTF313826.

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.

Q8K297-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALPRGSRG LPLLPLLLLL PPLGGPRGAD GYFPEERWSP ESPLQAPRVL
60 70 80 90 100
IALLARNAAP ALPATLGALE QLRHPRERTA LWVATDHNTD NTSAILREWL
110 120 130 140 150
VAVKGLYHSV EWRPAEEPSS YPDEEGPKHW SDSRYEHVMK LRQAALKSAR
160 170 180 190 200
DMWADYILFM DIDNLITNPD TLSLLIAENK TVVAPMLDSR AAYSNFWCGM
210 220 230 240 250
TSQGYYKRTP AYIPIRKRDR RGCFAVPMVH STFLIDLRKA ASRNLAFYPT
260 270 280 290 300
HPDYTWSFDD IIVFAFSCKQ AEVQMYVCNK EVYGFLPVPL RAHSSLQDEA
310 320 330 340 350
ESFMHVQLEV MVKHPPVQLS RFISAPRKTS DKMGFDEVFM INLKRRRDRR
360 370 380 390 400
ERMLRALHEQ EIDCQLVEAV DGKAMNTSQV EAMGIQMLPG YRDPYHGRPL
410 420 430 440 450
TKGELGCFLS HYNIWKEVVD RGLQKSLVFE DDLRFEIFFK RRLMNLMRDV
460 470 480 490 500
EREGLDWDLI YVGRKRMQVE HPEKAVPHVR NLVEADYSYW TLAYVISLQG
510 520 530 540 550
AQKLLAAKPL AKMLPVDEFL PVMFDKHPMS EYKSHFSPRN LRAFSVEPLL
560 570 580 590 600
IYPTHYTGDD GYVSDTETSV VWNNEQVKTD WDRAKSQKMR EQQALSREAK
610
NSDVLQSPLD STARDEL
Length:617
Mass (Da):71,061
Last modified:November 13, 2007 - v2
Checksum:i828D28E3300D9CC6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81S → L in BAE43293. (PubMed:16141072)Curated
Sequence conflicti30 – 301D → A in BAE43293. (PubMed:16141072)Curated
Sequence conflicti250 – 2501T → P in AAH32165. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035788 mRNA. Translation: BAE43293.1.
BC032165 mRNA. Translation: AAH32165.1.
BC056951 mRNA. Translation: AAH56951.1.
CCDSiCCDS22401.1.
RefSeqiNP_666323.2. NM_146211.3.
UniGeneiMm.273836.
Mm.334606.

Genome annotation databases

EnsembliENSMUST00000047903; ENSMUSP00000047923; ENSMUSG00000034807.
GeneIDi234407.
KEGGimmu:234407.
UCSCiuc009mee.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035788 mRNA. Translation: BAE43293.1.
BC032165 mRNA. Translation: AAH32165.1.
BC056951 mRNA. Translation: AAH56951.1.
CCDSiCCDS22401.1.
RefSeqiNP_666323.2. NM_146211.3.
UniGeneiMm.273836.
Mm.334606.

3D structure databases

ProteinModelPortaliQ8K297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231529. 2 interactions.
IntActiQ8K297. 1 interaction.
MINTiMINT-1866727.

Protein family/group databases

CAZyiGT25. Glycosyltransferase Family 25.

PTM databases

PhosphoSiteiQ8K297.

Proteomic databases

MaxQBiQ8K297.
PaxDbiQ8K297.
PRIDEiQ8K297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047903; ENSMUSP00000047923; ENSMUSG00000034807.
GeneIDi234407.
KEGGimmu:234407.
UCSCiuc009mee.2. mouse.

Organism-specific databases

CTDi234407.
MGIiMGI:1924348. Colgalt1.

Phylogenomic databases

eggNOGiNOG293154.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000007198.
HOVERGENiHBG058097.
InParanoidiQ8K297.
KOiK11703.
OMAiMWADYIL.
OrthoDBiEOG7060RC.
PhylomeDBiQ8K297.
TreeFamiTF313826.

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi382175.
PROiQ8K297.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K297.
CleanExiMM_GLT25D1.
GenevestigatoriQ8K297.

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]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiGT251_MOUSE
AccessioniPrimary (citable) accession number: Q8K297
Secondary accession number(s): Q3V3R5, Q6PGL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: February 4, 2015
This is version 95 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.