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Sequence of PLOD3_MOUSE

EC Number:2.4.1.66

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
procollagen glucosyltransferase
Q9R0E1
Mus musculus
741
84922
Reaction
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine
Other sequences found for EC No. 2.4.1.66

General information:

Sequence
show sequence in fasta format
  0 MAAAGPEPRL LLLLLLLLPP LPPVTSASDR PRGANAVNPD KLLVITVATA ETEGYRRFLQ
 60 SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM EKYADQKDMI IMFVDSYDVI
120 LASSPTELLK KFVQSGSHLL FSAESFCWPE WGLAEQYPEV GMGKRFLNSG GFIGFAPTIH
180 QIVRQWNYKD DDDDQLFYTQ LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVILKFDQNR
240 VRIRNVAYDT LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNQTLR TLPGGQPPPR
300 VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNSEV YHEPHIADAW PQLQDHFSAV
360 KLVGPEEALS AGEARDMAMD SCRQNPECEF YFSLDADAVL TNPETLRVLI EQNRKVIAPM
420 LSRHGKLWSN FWGALSPNEY YARSEDYVEL VQRKRVGVWN VPYISQAYVI RGETLRTELP
480 QKEVFSSSDT DPDMAFCKSV RDKGIFLHLS NQHEFGRLLA TSRYDTDHLH PDLWQIFDNP
540 VDWREQYIHE NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED
600 SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEY LFPGYHTKTR AVMNFVVRYR
660 PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD CRISSPRKGW ALLHPGRLTH
720 YHEGLPTTRG TRYIMVSFVD P
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
75975
Ruotsalainen H.,Sipila L.,Kerkela E.,Pospiech H.,Myllylae R.
Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse.
Matrix Biol.
18
325-329
1999
75976
Ruotsalainen H.,Vanhatupa S.,Tampio M.,Sipila L.,Valtavaara M.,Myllylae R.
Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase.
Matrix Biol.
20
137-146
2001
75977
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.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
75978
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
75979
Rautavuoma K.,Takaluoma K.,Sormunen R.,Myllyharju J.,Kivirikko K.I.,Soininen R.
Premature aggregation of type IV collagen and early lethality in lysyl hydroxylase 3 null mice.
Proc. Natl. Acad. Sci. U.S.A.
101
14120-14125
2004
75980
Salo A.M.,Wang C.,Sipilae L.,Sormunen R.,Vapola M.,Kervinen P.,Ruotsalainen H.,Heikkinen J.,Myllylae R.
Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling.
J. Cell. Physiol.
207
644-653
2006
75981
Ruotsalainen H.,Sipilae L.,Vapola M.,Sormunen R.,Salo A.M.,Uitto L.,Mercer D.K.,Robins S.P.,Risteli M.,Aszodi A.,Faessler R.,Myllylae R.
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes.
J. Cell Sci.
119
625-635
2006
75982
Sipilae L.,Ruotsalainen H.,Sormunen R.,Baker N.L.,Lamande S.R.,Vapola M.,Wang C.,Sado Y.,Aszodi A.,Myllylae R.
Secretion and assembly of type IV and VI collagens depend on glycosylation of hydroxylysines.
J. Biol. Chem.
282
33381-33388
2007
75983
Wollscheid B.,Bausch-Fluck D.,Henderson C.,O'Brien R.,Bibel M.,Schiess R.,Aebersold R.,Watts J.D.
Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
Nat. Biotechnol.
27
378-386
2009
75984
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
75985
Sricholpech M.,Perdivara I.,Nagaoka H.,Yokoyama M.,Tomer K.B.,Yamauchi M.
Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture.
J. Biol. Chem.
286
8846-8856
2011
75986
Wang C.,Ristiluoma M.M.,Salo A.M.,Eskelinen S.,Myllylae R.
Lysyl hydroxylase 3 is secreted from cells by two pathways.
J. Cell. Physiol.
227
668-675
2012
75987
Ruotsalainen H.,Risteli M.,Wang C.,Wang Y.,Karppinen M.,Bergmann U.,Kvist A.P.,Pospiech H.,Herzig K.H.,Myllylae R.
The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin.
PLoS ONE
7
0-0
2012
75988
Risteli M.,Ruotsalainen H.,Bergmann U.,Venkatraman Girija U.,Wallis R.,Myllylae R.
Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin.
PLoS ONE
9
0-0
2014