PCMT1

Protein-L-izoaspartat (D-aspartat) O-metiltransferaza jest enzim koji je kod ljudi kodiran genom PCMT1.

PCMT1
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 1I1N, 1KR5
Identifikatori
Aliasi	PCMT1
Vanjski ID-jevi	OMIM: 176851 MGI: 97502 HomoloGene: 55895 GeneCards: PCMT1
Lokacija gena (čovjek) Hrom. Hromosom 6 (čovjek) Bend 6q25.1 Početak 149,749,443 bp Kraj 149,811,420 bp
Lokacija gena (miš) Hrom. Hromosom 10 (miš) Bend 10 A1|10 2.26 cM Početak 7,629,373 bp Kraj 7,681,136 bp
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • GO:0102674, GO:0102675 methyltransferase activity • aktivnost sa transferazom • GO:0001948, GO:0016582 vezivanje za proteine • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity • cadherin binding Ćelijska komponenta • extracellular vesicle • Egzosom • citoplazma • citosol Biološki proces • Metilacija • protein repair • protein methylation Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	5110	18537
Ensembl	ENSG00000120265	ENSMUSG00000019795
UniProt	P22061	P23506
RefSeq (mRNK)	NM_001252049 NM_001252050 NM_001252051 NM_001252052 NM_001252053 NM_005389 NM_001360452 NM_001360456	NM_008786 NM_001347228 NM_001358647 NM_001358649 NM_001358651 NM_001358652 NM_001358653 NM_001358654 NM_001358657
RefSeq (bjelančevina)	NP_001238978 NP_001238979 NP_001238980 NP_001238981 NP_001238982 NP_005380 NP_001347381 NP_001347385	n/a
Lokacija (UCSC)	Chr 6: 149.75 – 149.81 Mb	Chr 10: 7.63 – 7.68 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 227 aminokiselina, а molekulska težina 24.636 Da.

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MAWKSGGASH		SELIHNLRKN		GIIKTDKVFE		VMLATDRSHY		AKCNPYMDSP
QSIGFQATIS		APHMHAYALE		LLFDQLHEGA		KALDVGSGSG		ILTACFARMV
GCTGKVIGID		HIKELVDDSV		NNVRKDDPTL		LSSGRVQLVV		GDGRMGYAEE
APYDAIHVGA		AAPVVPQALI		DQLKPGGRLI		LPVGPAGGNQ		MLEQYDKLQD
GSIKMKPLMG		VIYVPLTDKE		KQWSRWK

Funkcija

Tri klase proteinskih karboksil metiltransferaza, koje se razlikuju po specifičnosti supstrata metil-akceptora, pronađene su u prokariotskim i eukariotskim ćelijama. Enzim tipa II katalizira prijenos metilne grupe iz S-adenozil-L-metionina u slobodne karboksilne grupe ostataka D-aspartila i L-izoaspartila. Ovi ostaci koji prihvataju metil, rezultat su spontane deamidacije, izomerizacije i racemizacije normalnih L-asparatilnih i L-asparaginilnih ostataka i predstavljaju mjesta kovalentnog oštećenja proteina koji stare. PCMT1 (EC 2.1.1.77) je enzim za obnovu proteina koji započinje pretvorbu abnormalnih D-aspartyl i L-izoaspartil ostataka u normalni L-aspartil oblik (prema OMIMu).

Dopunska literatura

• MacLaren DC, Kagan RM, Clarke S (1992). "Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II". Biochem. Biophys. Res. Commun. 185 (1): 277–83. doi:10.1016/S0006-291X(05)80987-8. PMID 1339271.
• Ingrosso D, Kagan RM, Clarke S (1991). "Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase". Biochem. Biophys. Res. Commun. 175 (1): 351–8. doi:10.1016/S0006-291X(05)81242-2. PMID 1998518.
• Ingrosso D, Fowler AV, Bleibaum J, Clarke S (1989). "Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases". J. Biol. Chem. 264 (33): 20131–9. doi:10.1016/S0021-9258(19)47228-1. PMID 2684970.
• Gilbert JM, Fowler A, Bleibaum J, Clarke S (1988). "Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes". Biochemistry. 27 (14): 5227–33. doi:10.1021/bi00414a042. PMID 3167043.
• Ota IM, Gilbert JM, Clarke S (1988). "Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes". Biochem. Biophys. Res. Commun. 151 (3): 1136–43. doi:10.1016/S0006-291X(88)80484-4. PMID 3355545.
• Takeda R, Mizobuchi M, Murao K, et al. (1995). "Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells". J. Biochem. 117 (4): 683–5. doi:10.1093/jb/117.2.267. PMID 7592526.
• Tsai W, Clarke S (1994). "Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair". Biochem. Biophys. Res. Commun. 203 (1): 491–7. doi:10.1006/bbrc.1994.2209. PMID 8074695.
• DeVry CG, Tsai W, Clarke S (1997). "Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase". Arch. Biochem. Biophys. 335 (2): 321–32. CiteSeerX 10.1.1.630.8527. doi:10.1006/abbi.1996.0513. PMID 8914929.
• DeVry CG, Clarke S (1999). "Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins". J. Hum. Genet. 44 (5): 275–88. doi:10.1007/s100380050161. PMID 10496068.
• Ryttersgaard C, Griffith SC, Sawaya MR, et al. (2002). "Crystal structure of human L-isoaspartyl methyltransferase". J. Biol. Chem. 277 (12): 10642–6. doi:10.1074/jbc.M200229200. PMID 11792715.
• Smith CD, Carson M, Friedman AM, et al. (2002). "Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-Å resolution and modeling of an isoaspartyl-containing peptide at the active site". Protein Sci. 11 (3): 625–35. doi:10.1110/ps.37802. PMC 2373461. PMID 11847284.
• Misra P, Qi C, Yu S, et al. (2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Enünlü I, Pápai G, Cserpán I, et al. (2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/S0006-291X(03)01514-6. PMID 12943661.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Zhu H, Yang W, Lu W, et al. (2006). "A known functional polymorphism (Ile120Val) of the human PCMT1 gene and risk of spina bifida". Mol. Genet. Metab. 87 (1): 66–70. doi:10.1016/j.ymgme.2005.09.008. PMC 2947858. PMID 16256389.
• Lanthier J, Desrosiers RR (2007). "Regulation of protein L-isoaspartyl methyltransferase by cell-matrix interactions: involvement of integrin alphavbeta3, PI 3-kinase, and the proteasome". Biochem. Cell Biol. 84 (5): 684–94. doi:10.1139/o06-055. PMID 17167531.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.