Gene_locus Report for: ratno-BCHE Rattus norvegicus (Rat) Butyrylcholinesterase
Relationship
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Glires: N E > Rodentia: N E > Myomorpha: N E > Muroidea: N E > Muridae: N E > Murinae: N E > Rattus: N E > Rattus norvegicus: N E A85-EsteraseD-FGH :
rat-estd Rattus norvegicus (Rat) Esterase D .
ABHD6-Lip :
rat-abhd6 Rattus norvegicus (Rat) Abhydrolase domain-containing protein 6 .
ABHD8 :
rat-b5den3 Rattus norvegicus (Rat). Abhydrolase domain-containing 8 .
ABHD10 :
rat-abhda Rattus norvegicus (Rat) Abhydrolase domain-containing protein 10, mitochondrial .
ABHD11-Acetyl_transferase :
rat-d3zxk4 Rattus norvegicus (Rat). Abhydrolase domain-containing 11 .
ABHD12-PHARC :
ratno-q6ayt7 Rattus norvegicus (Rat) ABD12 Lysophosphatidylserine lipase ABHD12 .
ABHD13-BEM46 :
rat-d4a1b6 Rattus norvegicus (Rat). Similar to 1110065L07Rik protein (Predicted), isoform CRA_b .
ABHD16 :
ratno-q5xil6 Rattus norvegicus (Rat) rgd1309726_predicted protein ,
ratno-q6mg55 Rattus norvegicus (Rat) hla-b associated transcript 5, rat orthologue .
ABHD17-depalmitoylase :
ratno-q5xij5 Rattus norvegicus (Rat) similar to cdna sequence bc005632 AB17A ,
ratno-q6ay17 Rattus norvegicus (Rat) AB17B hypothetical protein ,
rat-ab17c Rattus norvegicus (Rat). Alpha/beta hydrolase domain-containing protein 17C .
ABHD18 :
rat-cd029 Rattus norvegicus (Rat) Uncharacterized protein ABHD18 C4orf29 homolog .
abh_upf0017 :
rat-d4a7w1 Rattus norvegicus (Rat) Protein Abhd2 ,
ratno-ABH15 Rattus norvegicus (Rat) Abhydrolase domain-containing 15 ,
ratno-abhd1 Rattus norvegicus (Rat) abhydrolase domain containing 1 (predicted) ,
ratno-d4a3d4 Rattus norvegicus (Rat) lung alpha/beta hydrolase fold protein 3 .
ACHE :
ratno-ACHE Rattus norvegicus (Rat) Acetylcholinesterase .
Acidic_Lipase :
rat-d3zuq1 Rattus norvegicus (Rat) Lipase ,
rat-d4a9l7 Rattus norvegicus (Rat) Lipase ,
rat-d4aa33 Rattus norvegicus (Rat) Lipase ,
rat-d4aa61 Rattus norvegicus (Rat) Lipase ,
ratno-1lipg Rattus norvegicus (Rat) Lingual lipase ,
ratno-1llip Rattus norvegicus (Rat) lysosomal acid lipase, intracellular hydrolase rats, Wolman, liver mRNA .
ACPH_Peptidase_S9 :
ratno-acph Rattus norvegicus (Rat) Acyl-peptide hydrolase; Acylamino-acid-releasing enzyme .
Acyl-CoA_Thioesterase :
ratno-acot1 Rattus norvegicus (Rat) hydrolase) (cte-I) (lach2) (ach2) ,
ratno-acot2 Rattus norvegicus (Rat) (EC 3.1.2.2) ACOT2 mitochondrial Acyl-CoA thioesterase 1 very-long-chain Acyl-CoA thioesterase (MTE-I) ,
ratno-BAAT Rattus norvegicus (Rat) bile acid CoA: amino acid n-acyltransferase kan-1 (EC 3.1.2.2) ,
ratno-q5fvr5 Rattus norvegicus (Rat) hypothetical loc313220 .
Arylacetamide_deacetylase :
rat-nceh1 Rattus norvegicus (Rat) Arylacetamide deacetylase-like 1 ,
ratno-aryla Rattus norvegicus (Rat) Arylacetamide deacetylase gene (aadac) ,
rat-d3zba8 Rattus norvegicus (Rat). Similar to arylacetamide deacetylase (Predicted) ,
rat-d3zbj1 Rattus norvegicus (Rat). Similar to novel protein similar to esterases ,
rat-d3zcr8 Rattus norvegicus (Rat). Arylacetamide deacetylase-like 3 ,
rat-d3zxw5 Rattus norvegicus (Rat). Similar to hypothetical protein C130079G13 ,
rat-d4a340 Rattus norvegicus (Rat). Similar to arylacetamide deacetylase ,
rat-f1lvg7 Rattus norvegicus (Rat). Similar to hypothetical protein C130079G13 ,
rat-m0r509 Rattus norvegicus (Rat). Similar to hypothetical protein C130079G13 ,
rat-m0r5d4 Rattus norvegicus (Rat). Arylacetamide deacetylase-like 2 .
Carboxypeptidase_S10 :
ratno-CPVL Rattus norvegicus (Rat) hypothetical protein loc502774 ,
ratno-Ppgb Rattus norvegicus (Rat) Lysosomal protective protein, Cathepsin A Ctsa, Protective protein for beta-galactosidase Ppgb ,
ratno-RISC Rattus norvegicus (Rat) retinoid-inducible serine carboxypeptidase precursor .
Carb_B_Chordata :
ratno-cauxin Rattus norvegicus (Rat) Carboxylesterase 5A (old est7) Epididymis-specific carboxylesterase 615 protein Carboxylesterase-like urinary excreted protein homolog ,
ratno-Ces1c Rattus norvegicus (Rat) Neutral retinyl ester hydrolase ,
ratno-Ces1d Rattus norvegicus (Rat) Carboxylesterase (ES-HVEL) pI 6.1 esterase (ES-10) CES1D Ces1d ,
ratno-Ces1e Rattus norvegicus (Rat) Liver carboxylesterase Carboxylesterase 1E ES-3 (egasyn) ,
ratno-Ces2f Rattus norvegicus (Rat) Protein Ces2f ,
ratno-CESRRL1 Rattus norvegicus (Rat) carboxylesterase rl1 ,
ratno-d3ze31 Rattus norvegicus (Rat) Putative uncharacterized protein RGD1565045 ,
ratno-d3zp14 Rattus norvegicus (Rat) Putative uncharacterized protein LOC685645 ,
ratno-d3zxq0 Rattus norvegicus (Rat) Similar to 2210023G05Rik protein (Predicted) ,
ratno-d3zxq1 Rattus norvegicus (Rat) Putative uncharacterized protein ENSRNOP00000044470 ,
ratno-d4aa05 Rattus norvegicus (Rat) Putative uncharacterized protein LOC679817 ,
ratno-est8 Rattus norvegicus (Rat) RCG51618 ,
ratno-kmcxe Rattus norvegicus (Rat) Liver carboxylesterase 4, kydney microsomal carboxylesterase Liver carboxylesterase 4 ES-4 ,
ratno-lmcxe Rattus norvegicus (Rat) Liver microsomal carboxylesterase Ces1f ,
ratno-LOC246252 Rattus norvegicus carboxylesterase isoenzyme gene (LOC246252) Ces1h EST2A Ces2a ,
ratno-pbcxe Rattus norvegicus (Rat) Phenobarbital-inducible carboxylesterase Ces2c ,
ratno-phebest Rattus norvegicus (Rat) Carboxylesterase, partial cds ,
ratno-q4qr68 Rattus norvegicus (Rat) hypothetical protein Ces2b ,
ratno-q32q55 Rattus norvegicus (Rat) hypothetical protein ,
ratno-q68g49 Rattus norvegicus (Rat) loc291863 protein ,
ratno-sicxe Rattus norvegicus (Rat) small intestinal carboxylesterase precursor ,
rat-a0a0g2k9y7 Rattus norvegicus (Rat). Carboxylic ester hydrolase ,
rat-a0a0g2kb83 Rattus norvegicus (Rat). Carboxylic ester hydrolase .
CGI-58_ABHD5_ABHD4 :
rat-d3zaw4 Rattus norvegicus (Rat) Uncharacterized protein ,
ratno-abhd5 Rattus norvegicus (Rat) cgi-58-like protein .
Cholesterol_esterase :
ratno-balip Rattus norvegicus (Rat) Cholesterol esterase .
CIB-CCG1-interacting-factor-B :
rat-abhea Rattus norvegicus (Rat) Abhydrolase domain-containing protein 14A ,
rat-abheb Rattus norvegicus (Rat) Abhydrolase domain-containing protein 14B .
CMBL :
ratno-CMBL Rattus norvegicus (Rat) ab2-225 (2310016a09rik protein) .
DPP4N_Peptidase_S9 :
rat-dpp9 ,
rat-d3zhq1 Rattus norvegicus (Rat) DPP8 ,
ratno-dpp4 ,
ratno-dpp6 Rattus norvegicus (Rat) Dipeptidyl aminopeptidase-like protein 6 (dipeptidylpeptidase VI) (dppx) ,
ratno-FAP Rattus norvegicus (Rat) fibroblast activation protein alpha subunit ,
ratno-q6q629 Rattus norvegicus (Rat) DPP-10 Dipeptidyl peptidase IV-related , kv4 potassium channel auxiliary subunit .
Duf_676 :
rat-d3zxw8 Rattus norvegicus (Rat) Protein Fam135a Similar to KIAA1411 protein ,
rat-f1lz91 Rattus norvegicus (Rat) Protein RGD1308133 .
Duf_726 :
rat-tmco4 Rattus norvegicus (Rat) Transmembrane and coiled-coil domain-containing protein 4 .
Epoxide_hydrolase :
rat-d3zkp8 Rattus norvegicus (Rat) Uncharacterized protein ,
rat-d4a4w4 Rattus norvegicus (Rat) Uncharacterized protein ,
ratno-hyep Rattus norvegicus (Rat) Epoxide hydrolase 1, Epoxide hydratase ,
ratno-hyes Rattus norvegicus (Rat) Bifunctional epoxide hydrolase 2, cytosolic epoxide hydrolase, Lipid-phosphate phosphatase .
Hepatic_Lipase :
ratno-1hlip Rattus norvegicus (Rat) Triacylglycerol lipase hepatic .
Hormone-sensitive_lipase_like :
ratno-hslip Rattus norvegicus (Rat) Hormone sensitive lipase .
Hydrolase_RBBP9_YdeN :
ratno-rbbp9 Rattus norvegicus (Rat) Retinoblastoma-binding protein 9 B5T overexpressed gene protein (bog protein) .
Kynurenine-formamidase :
rat-m0rc77 Rattus norvegicus (Rat). N-formylkynurenine formamidase .
LIDHydrolase :
rat-Ldah Rattus norvegicus (Rat) UPF0554 protein LDAH C2orf43 homolog .
Lipase_3 :
rat-dglb Rattus norvegicus (Rat) Sn1-specific diacylglycerol lipase beta ,
ratno-q5ylm1 Rattus norvegicus (Rat) neural stem cell-derived dendrite regulator Diacylglycerol lipase-alpha Dagla .
Lipoprotein_Lipase :
ratno-lipli Rattus norvegicus (Rat) Lipoprotein lipase ,
ratno-q5d216 Rattus norvegicus (Rat) endothelial lipase Lipg .
LYsophospholipase_carboxylesterase :
ratno-lypla1a Rattus norvegicus (Rat) Lysophospholipase (Pla1a) ,
ratno-lypla2 Rattus norvegicus (Rat) Lysophospholipase II .
Maspardin-ACP33-SPG21_like :
ratno-SPG21 Rattus norvegicus (Rat) acid cluster protein 33 (Spg21) Maspardin .
MEST-like :
ratno-q6p5p5 Rattus norvegicus (Rat) Mesoderm-specific transcript homolog protein .
Monoglyceridelipase_lysophospholip :
ratno-MGLL Rattus norvegicus (rat) monoglyceride lipase (Mgl2) .
Ndr_family :
ratno-ndr4 Rattus norvegicus (Rat) ndrg4 protein (brain development-related molecule 1) ndrg4-b1 ndrg4-a2 ,
ratno-NDRG2 Rattus norvegicus (Rat) ndrg1 related protein ndrg2b1 (ndrg1 related protein ndrg2a1) ,
ratno-q6ayr2 Rattus norvegicus (Rat) hypothetical protein ,
ratno-q6je36 Rattus norvegicus (Rat) n-myc downstream regulated 1 (hypothetical protein) .
Neuroligin :
ratno-1neur ,
ratno-2neur ,
ratno-3neur Rattus norvegicus (Rat) Neuroligin 3 Nlgn3 .
NLS3-Tex30 :
rat-Kansl3 Rattus norvegicus (Rat) Non-specific lethal 3 homologue Uncharacterized protein KIAA1310 homolog ,
rat-Tex30 Rattus norvegicus (Rat) Putative uncharacterized protein RGD1309095_predicted .
PAF-Acetylhydrolase :
ratno-paf2 Rattus norvegicus (Rat) PAFAHII platelet-activating factor acetylhydrolase II ,
ratno-q5m7t7 Rattus norvegicus (Rat) acetylhydrolase, plasma) (predicted) .
Palmitoyl-protein_thioesterase :
ratno-ppt Rattus norvegicus (Rat) Palmitoyl-protein thioesterase 1 ,
ratno-PPT2 Rattus norvegicus (Rat) palmitoyl-protein thioesterase 2, EC 3.1.2.22 .
Pancreatic_lipase :
ratno-1plip Rattus norvegicus (Rat) Pancreatic lipase ,
ratno-3plip Rattus norvegicus (Rat) Pancreatic lipase-related protein 1 precursor (EC 3.1.1.3) ,
ratno-4plip .
PC-sterol_acyltransferase :
ratno-lcat Rattus norvegicus (Rat) Phosphatidylcholine-sterol acyltransfer ,
ratno-q675a5 Rattus norvegicus (Rat) lysosomal phospholipase a2 .
Pectinacetylesterase-Notum :
ratno-d3zxi3 Rattus norvegicus (Rat) Notum .
PGAP1 :
ratno-q765a7 Rattus norvegicus (Rat) gpi deacylase .
Phospholipase :
ratno-P97535 Rattus norvegicus (Rat) ps-pla1 precursor ,
ratno-q6p6s8 Rattus norvegicus (Rat) hypothetical protein (fragment) ,
rat-d3zmg4 Rattus norvegicus (Rat). Lipase, member H (Predicted) .
Prolylcarboxypeptidase :
rat-d4aa31 Rattus norvegicus (Rat) Protein Prcp ,
ratno-dpp2 Rattus norvegicus (Rat) Dipeptidyl aminopeptidase II (quiescent cell proline dipeptidase) ,
ratno-q3mhs0 Rattus norvegicus (Rat) protease, serine, 16 (thymus) .
S9N_PPCE_Peptidase_S9 :
ratno-RPOP Rattus norvegicus (Rat) Prolyl endopeptidase rPop .
S9N_PREPL_Peptidase_S9 :
ratno-q5hza6 Rattus norvegicus (Rat) similar to riken cdna d030028o16 (predicted) .
SERHL :
rat-d4a071 Rattus norvegicus (Rat) Similar to serine hydolase like protein, isoforms Serhl-2 (Predicted) .
Thioesterase :
ratno-fas Rattus norvegicus (Rat) fatty acid synthase FAS Thioesterase domain ,
ratno-sast Rattus norvegicus (Rat) (thioesterase II) .
Thyroglobulin :
ratno-thyro Rattus norvegicus (Rat) Thyroglobulin .
Valacyclovir-hydrolase :
ratno-q3b8n9 Rattus norvegicus (Rat) biphenyl hydrolase-like , breast epithelial mucin-assoc AG BPHL Molecular evidence
Database
1 mutation :
ratno-BCHE No structure No kinetic No Substrate No inhibitor
Sequence
Graphical view for this peptide sequence: ratno-BCHE Colored MSA for BCHE (raw)
MVTEIHFLLWILLLCMLFGKSHTEEDVIITTKTGRVRGLSMPILGGTVTA
FLGIPYAQPPLGSLRFKKPQPLNKWPDVYNATKYANSCYQNIDQAFPGFQ
GSEMWNPNTNLSEDCLYLNVWIPVPKPKNATVMVWVYGGGFQTGTSSLPV
YDGKFLTRVERVIVVSMNYRVGALGFLAFPGNSEAPGNMGLFDQQLALQW
IQRNIAAFGGNPKSVTLFGESAGAASVSLHLLCPQSYPLFTRAILESGSS
NAPWAVKHPEEARNRTLTLAKFIGCSKENEKEIITCLRSKDPQEILLNEK
LVLPSDSIRSINFGPTVDGDFLTDMPHTLLQLGKVKTAQILVGVNKDEGT
AFLVYGAPGFSKDNDSLITRREFQEGLNMYFPGVSSLGKEAILFYYVDWL
GDQTPEVYREAFDDIIGDYNIICPALEFTKKFAELEINAFFYYFEHRSSK
LPWPEWMGVMHGYEIEFVFGLPLERRVNYTRAEEIFSRSIMKTWANFAKY
GHPNGTQGNSTVWPVFTSTEQKYLTLNTEKSKINSKLRAPQCQFWRLFFP
KVLEITGDIDEREQEWKAGFHRWSNYMMDWKNQFNDYTSKKETCTDL
Legend
This sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA
M V T E I H F L L W I L L L C M L F G K S H T E E D V I I T T K T G R V R G L S M P I L G G T V T A F L G I P Y A Q P P L G S L R F K K P Q P L N K W P D V Y N A T K Y A N S C Y Q N I D Q A F P G F Q G S E M W N P N T N L S E D C L Y L N V W I P V P K P K N A T V M V W V Y G G G F Q T G T S S L P V Y D G K F L T R V E R V I V V S M N Y R V G A L G F L A F P G N S E A P G N M G L F D Q Q L A L Q W I Q R N I A A F G G N P K S V T L F G E S A G A A S V S L H L L C P Q S Y P L F T R A I L E S G S S N A P W A V K H P E E A R N R T L T L A K F I G C S K E N E K E I I T C L R S K D P Q E I L L N E K L V L P S D S I R S I N F G P T V D G D F L T D M P H T L L Q L G K V K T A Q I L V G V N K D E G T A F L V Y G A P G F S K D N D S L I T R R E F Q E G L N M Y F P G V S S L G K E A I L F Y Y V D W L G D Q T P E V Y R E A F D D I I G D Y N I I C P A L E F T K K F A E L E I N A F F Y Y F E H R S S K L P W P E W M G V M H G Y E I E F V F G L P L E R R V N Y T R A E E I F S R S I M K T W A N F A K Y G H P N G T Q G N S T V W P V F T S T E Q K Y L T L N T E K S K I N S K L R A P Q C Q F W R L F F P K V L E I T G D I D E R E Q E W K A G F H R W S N Y M M D W K N Q F N D Y T S K K E T C T D L
References
Title: Genome sequence of the Brown Norway rat yields insights into mammalian evolutionGibbs RA , Weinstock GM , Metzker ML , Muzny DM , Sodergren EJ , Scherer S , Scott G , Steffen D , Worley KC and Collins F <218 more author(s)> Gibbs RA , Weinstock GM , Metzker ML , Muzny DM , Sodergren EJ , Scherer S , Scott G , Steffen D , Worley KC , Burch PE , Okwuonu G , Hines S , Lewis L , DeRamo C , Delgado O , Dugan-Rocha S , Miner G , Morgan M , Hawes A , Gill R , Celera , Holt RA , Adams MD , Amanatides PG , Baden-Tillson H , Barnstead M , Chin S , Evans CA , Ferriera S , Fosler C , Glodek A , Gu Z , Jennings D , Kraft CL , Nguyen T , Pfannkoch CM , Sitter C , Sutton GG , Venter JC , Woodage T , Smith D , Lee HM , Gustafson E , Cahill P , Kana A , Doucette-Stamm L , Weinstock K , Fechtel K , Weiss RB , Dunn DM , Green ED , Blakesley RW , Bouffard GG , de Jong PJ , Osoegawa K , Zhu B , Marra M , Schein J , Bosdet I , Fjell C , Jones S , Krzywinski M , Mathewson C , Siddiqui A , Wye N , McPherson J , Zhao S , Fraser CM , Shetty J , Shatsman S , Geer K , Chen Y , Abramzon S , Nierman WC , Havlak PH , Chen R , Durbin KJ , Egan A , Ren Y , Song XZ , Li B , Liu Y , Qin X , Cawley S , Cooney AJ , D'Souza LM , Martin K , Wu JQ , Gonzalez-Garay ML , Jackson AR , Kalafus KJ , McLeod MP , Milosavljevic A , Virk D , Volkov A , Wheeler DA , Zhang Z , Bailey JA , Eichler EE , Tuzun E , Birney E , Mongin E , Ureta-Vidal A , Woodwark C , Zdobnov E , Bork P , Suyama M , Torrents D , Alexandersson M , Trask BJ , Young JM , Huang H , Wang H , Xing H , Daniels S , Gietzen D , Schmidt J , Stevens K , Vitt U , Wingrove J , Camara F , Mar Alba M , Abril JF , Guigo R , Smit A , Dubchak I , Rubin EM , Couronne O , Poliakov A , Hubner N , Ganten D , Goesele C , Hummel O , Kreitler T , Lee YA , Monti J , Schulz H , Zimdahl H , Himmelbauer H , Lehrach H , Jacob HJ , Bromberg S , Gullings-Handley J , Jensen-Seaman MI , Kwitek AE , Lazar J , Pasko D , Tonellato PJ , Twigger S , Ponting CP , Duarte JM , Rice S , Goodstadt L , Beatson SA , Emes RD , Winter EE , Webber C , Brandt P , Nyakatura G , Adetobi M , Chiaromonte F , Elnitski L , Eswara P , Hardison RC , Hou M , Kolbe D , Makova K , Miller W , Nekrutenko A , Riemer C , Schwartz S , Taylor J , Yang S , Zhang Y , Lindpaintner K , Andrews TD , Caccamo M , Clamp M , Clarke L , Curwen V , Durbin R , Eyras E , Searle SM , Cooper GM , Batzoglou S , Brudno M , Sidow A , Stone EA , Payseur BA , Bourque G , Lopez-Otin C , Puente XS , Chakrabarti K , Chatterji S , Dewey C , Pachter L , Bray N , Yap VB , Caspi A , Tesler G , Pevzner PA , Haussler D , Roskin KM , Baertsch R , Clawson H , Furey TS , Hinrichs AS , Karolchik D , Kent WJ , Rosenbloom KR , Trumbower H , Weirauch M , Cooper DN , Stenson PD , Ma B , Brent M , Arumugam M , Shteynberg D , Copley RR , Taylor MS , Riethman H , Mudunuri U , Peterson J , Guyer M , Felsenfeld A , Old S , Mockrin S , Collins F (- 218) Ref: Nature, 428 :493, 2004 : PubMed Abstract ESTHER: Gibbs_2004_Nature_428_493 PubMedSearch: Gibbs 2004 Nature 428 493 PubMedID: 15057822 Gene_locus related to this paper: rat-abhea ,
rat-abheb ,
rat-cd029 ,
rat-d3zaw4 ,
rat-dpp9 ,
rat-d3zhq1 ,
rat-d3zkp8 ,
rat-d3zuq1 ,
rat-d3zxw8 ,
rat-d4a4w4 ,
rat-d4a7w1 ,
rat-d4a9l7 ,
rat-d4a071 ,
rat-d4aa31 ,
rat-d4aa33 ,
rat-d4aa61 ,
rat-dglb ,
rat-f1lz91 ,
rat-Kansl3 ,
rat-nceh1 ,
rat-Tex30 ,
ratno-1hlip ,
ratno-1neur ,
ratno-1plip ,
ratno-2neur ,
ratno-3neur ,
ratno-3plip ,
ratno-ABH15 ,
ratno-ACHE ,
ratno-balip ,
ratno-BCHE ,
ratno-cauxin ,
ratno-Ces1d ,
ratno-Ces1e ,
ratno-Ces2f ,
ratno-d3ze31 ,
ratno-d3zp14 ,
ratno-d3zxi3 ,
ratno-d3zxq0 ,
ratno-d3zxq1 ,
ratno-d4a3d4 ,
ratno-d4aa05 ,
ratno-dpp4 ,
ratno-dpp6 ,
ratno-est8 ,
ratno-FAP ,
ratno-hyep ,
ratno-hyes ,
ratno-kmcxe ,
ratno-lmcxe ,
ratno-LOC246252 ,
ratno-MGLL ,
ratno-pbcxe ,
ratno-phebest ,
ratno-Ppgb ,
ratno-q4qr68 ,
ratno-q6ayr2 ,
ratno-q6q629 ,
ratno-SPG21 ,
ratno-thyro ,
rat-m0rc77 ,
rat-a0a0g2k9y7 ,
rat-a0a0g2kb83 ,
rat-d3zba8 ,
rat-d3zbj1 ,
rat-d3zcr8 ,
rat-d3zxw5 ,
rat-d4a340 ,
rat-f1lvg7 ,
rat-m0r509 ,
rat-m0r5d4 ,
rat-b5den3 ,
rat-d3zxk4 ,
rat-d4a1b6 ,
rat-d3zmg4 ,
rat-ab17c Abstract
The laboratory rat (Rattus norvegicus) is an indispensable tool in experimental medicine and drug development, having made inestimable contributions to human health. We report here the genome sequence of the Brown Norway (BN) rat strain. The sequence represents a high-quality 'draft' covering over 90% of the genome. The BN rat sequence is the third complete mammalian genome to be deciphered, and three-way comparisons with the human and mouse genomes resolve details of mammalian evolution. This first comprehensive analysis includes genes and proteins and their relation to human disease, repeated sequences, comparative genome-wide studies of mammalian orthologous chromosomal regions and rearrangement breakpoints, reconstruction of ancestral karyotypes and the events leading to existing species, rates of variation, and lineage-specific and lineage-independent evolutionary events such as expansion of gene families, orthology relations and protein evolution.
Title: DNA sequence of butyrylcholinesterase from the rat: expression of the protein and characterization of the properties of rat butyrylcholinesteraseBoeck AT , Schopfer LM , Lockridge O Ref: Biochemical Pharmacology, 63 :2101, 2002 : PubMed Abstract ESTHER: Boeck_2002_Biochem.Pharmacol_63_2101 PubMedSearch: Boeck 2002 Biochem.Pharmacol 63 2101 PubMedID: 12110369 Gene_locus related to this paper: ratno-BCHE Abstract
The rat is the model animal for toxicity studies. Butyrylcholinesterase (BChE), being sensitive to inhibition by some organophosphorus and carbamate pesticides, is a biomarker of toxic exposure. The goal of this work was to characterize the purified rat BChE enzyme. The cDNA sequence showed eight amino acid differences between the active site gorge of rat and human BChE, six clustered around the acyl binding pocket and two below the active site serine. A prominent difference in rat was the substitution of arginine for leucine at position 286 in the acyl pocket. Wild-type rat BChE, the mutant R286L, wild-type human BChE, and the mutant L286R were expressed in CHO cells and purified. Arg286 was found responsible for the resistance of rat BChE to inhibition by Triton X-100. Replacement of Arg286 with leucine caused the affinity for Triton X-100 to increase 20-fold, making it as sensitive as human BChE to inhibition by Triton X-100. Wild-type rat BChE had an 8- to 9-fold higher K(m) for the positively charged substrates butyrylthiocholine, acetylthiocholine, propionylthiocholine, benzoylcholine, and cocaine compared with wild-type human BChE. Wild-type rat BChE catalyzed turnover 2- to 7-fold more rapidly than human BChE, showing the highest turnover with propionylthiocholine (201,000 min(-1)). Human BChE does not reactivate spontaneously after inhibition by echothiophate, but rat BChE reactivates with a half-life of 4.3hr. Human serum contains 5mg/L of BChE and 0.01mg/L of AChE. Male rat serum contains 0.2mg/L of BChE and approximately 0.2mg/L of AChE.
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