| Identification |
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| Name | Dolichyl-phosphate-mannose--protein mannosyltransferase 4 |
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| Synonyms | Not Available |
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| Gene Name | PMT4 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in mannosyltransferase activity |
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| Specific Function | Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to be active on GAS1 |
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| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | | O-Mannosyl glycan biosynthesis | ec00514 |  |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00937 | dolichyl D-mannosyl phosphate | Show |
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| GO Classification | | Component |
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| cell part | | membrane | | Function |
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| catalytic activity | | transferase activity | | transferase activity, transferring glycosyl groups | | transferase activity, transferring hexosyl groups | | mannosyltransferase activity | | Process |
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| protein modification process | | protein amino acid glycosylation | | protein amino acid O-linked glycosylation | | metabolic process | | macromolecule metabolic process | | macromolecule modification |
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| Gene Properties |
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| Chromosome Location | chromosome 10 |
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| Locus | YJR143C |
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| Gene Sequence | >2289 bp
ATGTCTGTGCCCAAAAAACGTAACCATGGGAAGTTACCACCTTCCACTAAGGACGTAGAC
GATCCTTCGTTGAAGTACACGAAGGCCGCGCCTAAATGTGAACAAGTTGCTGAACATTGG
CTCTTGCAGCCACTACCGGAACCGGAATCACGTTATAGCTTTTGGGTAACAATTGTTACC
TTATTAGCGTTTGCTGCTAGATTTTATAAGATCTGGTATCCAAAAGAAGTTGTTTTTGAT
GAGGTACATTTCGGGAAATTTGCATCGTATTACTTAGAAAGGTCTTATTTCTTTGACGTT
CATCCCCCTTTTGCTAAGATGATGATTGCCTTCATTGGTTGGTTATGTGGCTATGATGGT
TCCTTTAAGTTTGATGAGATTGGGTATTCTTATGAAACTCATCCAGCTCCATATATCGCG
TACCGTTCTTTCAACGCGATATTGGGCACATTGACTGTACCAATTATGTTCAACACTTTG
AAGGAACTGAATTTCAGGGCTATTACATGTGCGTTTGCATCTCTCTTGGTTGCAATCGAT
ACTGCGCATGTTACAGAAACTAGGCTGATTTTACTGGATGCCATCTTGATTATTTCTATT
GCTGCTACTATGTATTGTTACGTTCGTTTCTACAAGTGCCAATTGCGTCAACCTTTTACA
TGGAGTTGGTATATTTGGTTACACGCTACTGGTTTGTCTTTATCCTTCGTGATTTCCACA
AAATATGTTGGTGTTATGACATATTCCGCTATTGGTTTTGCTGCTGTGGTCAACTTATGG
CAATTACTGGACATCAAGGCGGGTTTGTCCTTGAGGCAGTTCATGAGACATTTTAGTAAA
AGGCTGAATGGTTTAGTTTTGATTCCATTTGTGATTTACTTGTTTTGGTTCTGGGTTCAT
TTCACCGTTTTGAATACTTCAGGTCCTGGCGACGCATTTATGTCTGCTGAATTTCAAGAA
ACACTTAAGGACTCTCCCTTAAGTGTTGACTCTAAAACCGTCAATTATTTTGATATTATC
ACTATCAAACATCAAGATACTGACGCATTCTTACATTCTCACTTGGCACGTTACCCACAA
CGGTATGAAGATGGTCGTATCTCATCCGCTGGTCAACAAGTTACTGGTTACACGCATCCT
GACTTCAACAATCAATGGGAAGTGTTACCACCCCATGGCAGTGATGTCGGTAAAGGACAA
GCTGTTCTATTGAACCAGCATATAAGATTGAGACATGTAGCCACCGATACCTACTTGTTA
GCCCATGATGTCGCCTCCCCATTTTACCCTACCAATGAAGAAATCACTACAGTAACTTTA
GAAGAAGGTGATGGGGAATTATATCCTGAAACACTTTTTGCATTCCAACCACTGAAAAAA
TCAGATGAAGGTCACGTTTTAAAGAGTAAAACGGTTTCTTTCCGTCTTTTCCACGTTGAT
ACCTCCGTAGCTTTGTGGACTCACAACGACGAGTTGTTACCGGATTGGGGGTTCCAACAA
CAAGAAATTAATGGTAACAAAAAAGTTATTGATCCTTCAAATAACTGGGTTGTTGATGAA
ATTGTTAACCTGGACGAGGTTCGGAAGGTATATATTCCGAAGGTTGTTAAGCCATTACCA
TTCTTGAAGAAATGGATTGAAACTCAAAAATCTATGTTCGAACATAACAATAAACTATCA
TCAGAGCATCCATTTGCCTCTGAACCTTACAGTTGGCCCGGTAGTTTAAGTGGTGTTTCG
TTCTGGACCAACGGTGACGAAAAGAAGCAAATATATTTCATTGGTAACATCATTGGGTGG
TGGTTCCAAGTCATATCATTGGCTGTTTTTGTTGGCATTATCGTGGCCGATTTAATTACT
AGACATCGTGGCTATTATGCCCTAAACAAGATGACCAGAGAAAAGCTGTATGGCCCATTG
ATGTTTTTCTTCGTCTCCTGGTGCTGTCATTATTTTCCATTCTTTTTAATGGCGCGTCAA
AAGTTTTTGCATCATTACTTACCAGCTCATTTAATCGCGTGCTTATTCTCAGGAGCACTA
TGGGAAGTAATTTTCAGTGATTGCAAATCATTGGATTTGGAGAAAGACGAGGATATTTCA
GGTGCATCATATGAACGGAACCCTAAGGTCTACGTTAAACCCTATACCGTCTTCTTGGTG
TGTGTCTCCTGTGCTGTTGCGTGGTTTTTTGTATACTTTTCACCACTAGTGTATGGAGAT
GTCAGCTTGTCACCATCGGAAGTTGTTTCTAGAGAGTGGTTTGACATAGAATTAAATTTC
TCCAAGTAA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 762 |
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| Protein Molecular Weight | 87965.5 |
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| Protein Theoretical pI | 6.93 |
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| Signalling Regions | |
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| Transmembrane Regions | - 54-74
- 137-157
- 167-187
- 190-210
- 218-238
- 243-263
- 284-304
- 594-614
- 636-656
- 717-737
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| Protein Sequence | >Dolichyl-phosphate-mannose--protein mannosyltransferase 4
MSVPKKRNHGKLPPSTKDVDDPSLKYTKAAPKCEQVAEHWLLQPLPEPESRYSFWVTIVT
LLAFAARFYKIWYPKEVVFDEVHFGKFASYYLERSYFFDVHPPFAKMMIAFIGWLCGYDG
SFKFDEIGYSYETHPAPYIAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAID
TAHVTETRLILLDAILIISIAATMYCYVRFYKCQLRQPFTWSWYIWLHATGLSLSFVIST
KYVGVMTYSAIGFAAVVNLWQLLDIKAGLSLRQFMRHFSKRLNGLVLIPFVIYLFWFWVH
FTVLNTSGPGDAFMSAEFQETLKDSPLSVDSKTVNYFDIITIKHQDTDAFLHSHLARYPQ
RYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSDVGKGQAVLLNQHIRLRHVATDTYLL
AHDVASPFYPTNEEITTVTLEEGDGELYPETLFAFQPLKKSDEGHVLKSKTVSFRLFHVD
TSVALWTHNDELLPDWGFQQQEINGNKKVIDPSNNWVVDEIVNLDEVRKVYIPKVVKPLP
FLKKWIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEKKQIYFIGNIIGW
WFQVISLAVFVGIIVADLITRHRGYYALNKMTREKLYGPLMFFFVSWCCHYFPFFLMARQ
KFLHHYLPAHLIACLFSGALWEVIFSDCKSLDLEKDEDISGASYERNPKVYVKPYTVFLV
CVSCAVAWFFVYFSPLVYGDVSLSPSEVVSREWFDIELNFSK |
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| References |
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| External Links | |
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| General Reference | - Immervoll, T., Gentzsch, M., Tanner, W. (1995). "PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene family of Saccharomyces cerevisiae." Yeast 11:1345-1351.8585318
- Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
- Gentzsch, M., Tanner, W. (1996). "The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital." EMBO J 15:5752-5759.8918452
- Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
- Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
- Imai, K., Noda, Y., Adachi, H., Yoda, K. (2007). "Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5." Biosci Biotechnol Biochem 71:249-252.17213653
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