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FI21236p1 (Rumpelstiltskin, isoform A)

 Q9VHC7_DROME            Unreviewed;       632 AA.
Q9VHC7;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-MAY-2000, sequence version 1.
13-FEB-2019, entry version 159.
SubName: Full=FI21236p1 {ECO:0000313|EMBL:AGW25605.1};
SubName: Full=Rumpelstiltskin, isoform A {ECO:0000313|EMBL:AAF54387.1};
Name=rump {ECO:0000313|EMBL:AAF54387.1,
ECO:0000313|FlyBase:FBgn0267790};
Synonyms=cg9373 {ECO:0000313|EMBL:AAF54387.1},
Dmel\CG9373 {ECO:0000313|EMBL:AAF54387.1},
hnRNP M {ECO:0000313|EMBL:AAF54387.1},
HnRNP-S5 {ECO:0000313|EMBL:AAF54387.1},
Hrp59 {ECO:0000313|EMBL:AAF54387.1},
hrp59 {ECO:0000313|EMBL:AAF54387.1},
p70 {ECO:0000313|EMBL:AAF54387.1}, p75 {ECO:0000313|EMBL:AAF54387.1},
rump-RA {ECO:0000313|EMBL:AGW25605.1},
S5 {ECO:0000313|EMBL:AAF54387.1};
ORFNames=CG9373 {ECO:0000313|FlyBase:FBgn0267790},
Dmel_CG9373 {ECO:0000313|EMBL:AAF54387.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[3] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[5] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[6] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[7] {ECO:0000313|EMBL:AAF54387.1}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:AAF54387.1}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[10] {ECO:0000313|EMBL:AAF54387.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[11] {ECO:0000313|EMBL:AGW25605.1}
NUCLEOTIDE SEQUENCE.
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
[12] {ECO:0000313|EMBL:AAF54387.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109357; DOI=.1534/g3.115.018929;
FlyBase Consortium;
Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B.,
St Pierre S.E., Gramates L.S., Zhou P., Schroeder A.J., Falls K.,
Strelets V., Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: Impact of High-
Throughput Data.";
G3 (Bethesda) 5:1721-1736(2015).
[13] {ECO:0000313|EMBL:AAF54387.1}
NUCLEOTIDE SEQUENCE.
PubMed=26109356; DOI=.1534/g3.115.018937;
FlyBase Consortium;
Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B.,
St Pierre S.E., Zhou P., Schroeder A.J., Falls K., Emmert D.B.,
Russo S.M., Gelbart W.M.;
"Gene Model Annotations for Drosophila melanogaster: The Rule-
Benders.";
G3 (Bethesda) 5:1737-1749(2015).
[14] {ECO:0000313|EMBL:AAF54387.1}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE014297; AAF54387.1; -; Genomic_DNA.
EMBL; BT150323; AGW25605.1; -; mRNA.
RefSeq; NP_649899.1; NM_141642.3.
UniGene; Dm.7304; -.
SMR; Q9VHC7; -.
IntAct; Q9VHC7; 5.
STRING; 7227.FBpp0081601; -.
EnsemblMetazoa; FBtr0082123; FBpp0081601; FBgn0267790.
GeneID; 41138; -.
UCSC; CG9373-RA; d. melanogaster.
CTD; 41138; -.
FlyBase; FBgn0267790; rump.
eggNOG; KOG4212; Eukaryota.
eggNOG; ENOG4110PAX; LUCA.
GeneTree; ENSGT00940000168568; -.
OMA; MFGNHAA; -.
OrthoDB; 1174365at2759; -.
Reactome; R-DME-6803529; FGFR2 alternative splicing.
Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; rump; fly.
GenomeRNAi; 41138; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0267790; Expressed in 78 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9VHC7; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0000790; C:nuclear chromatin; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0035062; C:omega speckle; IDA:FlyBase.
GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:FlyBase.
GO; GO:0009952; P:anterior/posterior pattern specification; IGI:FlyBase.
GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
GO; GO:0007277; P:pole cell development; IGI:FlyBase.
GO; GO:0045451; P:pole plasm oskar mRNA localization; IGI:FlyBase.
GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
GO; GO:0035282; P:segmentation; IGI:FlyBase.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Proteomics identification {ECO:0000213|PeptideAtlas:Q9VHC7};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
DOMAIN 57 135 RRM. {ECO:0000259|PROSITE:PS50102}.
DOMAIN 232 309 RRM. {ECO:0000259|PROSITE:PS50102}.
DOMAIN 563 632 RRM. {ECO:0000259|PROSITE:PS50102}.
SEQUENCE 632 AA; 66731 MW; 5ED46DB41797CD23 CRC64;
MSMDASNSVE SREKERDRRG RGARGSRFTD ADGNGNGAGS QGGGVAARDR SRERRNCRVY
ISNIPYDYRW QDLKDLFRRI VGSIEYVQLF FDESGKARGC GIVEFKDPEN VQKALEKMNR
YEVNGRELVV KEDHGEQRDQ YGRIVRDGGG GGGGGGGVQG GNGGNNGGGG GGGRDHMDDR
DRGFSRRDDD RLSGRNNFNM MSNDYNNSSN YNLYGLSASF LESLGISGPL HNKVFVANLD
YKVDNKKLKQ VFKLAGKVQS VDLSLDKEGN SRGFAVIEYD HPVEAVQAIS MLDRQMLFDR
RMTVRLDRIP DKNEGIKLPE GLGGVGIGLG PNGEPLRDVA HNLPNGGQSQ GQLLGNAQQG
SQLGSVGSQP NSSAVSNATT NLLNNLTGVM FGNHAAVQPS PVAPVQKPSL GNNTGSGGLN
LNNLNPSILA AVVGNLGNQG GNLSNPLLSS SLSNLGLNLG NSGNDDNLPP SNVGLSNNYS
SGGTGGGNSY SSGNNYSGGG GSSNLGYNAY SSSGGMGGGN GGVGVDGNDY NTGNPLDVYG
GGSNVGNSNV GSANAVGASR KSDTIIIKNV PITCTWQTLR DKFREIGDVK FAEIRGNDVG
VVRFFKERDA ELAIALMDGS RLDGRNIKVT YF


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[Or22b AN12 DOR22A.2 dor67 Or22A.2 CG4231] Odorant receptor 22b
[Cryba1] Beta-crystallin A3 [Cleaved into: Beta-crystallin A3, isoform A1, Delta4 form; Beta-crystallin A3, isoform A1, Delta7 form; Beta-crystallin A3, isoform A1, Delta8 form]
[PPP2R2A] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)
[TCIRG1 ATP6N1C ATP6V0A3] V-type proton ATPase 116 kDa subunit a isoform 3 (V-ATPase 116 kDa isoform a3) (Osteoclastic proton pump 116 kDa subunit) (OC-116 kDa) (OC116) (T-cell immune regulator 1) (T-cell immune response cDNA7 protein) (TIRC7) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3)
[PPP2R5E] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon)
[PPP2R5B] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform (PP2A B subunit isoform B'-beta) (PP2A B subunit isoform B56-beta) (PP2A B subunit isoform PR61-beta) (PP2A B subunit isoform R5-beta)
[PPP2R1B] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta)
[PPP2R5A] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha) (PP2A B subunit isoform B56-alpha) (PP2A B subunit isoform PR61-alpha) (PR61alpha) (PP2A B subunit isoform R5-alpha)
[Atp6v0a2 Atp6n1b Tj6] V-type proton ATPase 116 kDa subunit a isoform 2 (V-ATPase 116 kDa isoform a2) (Immune suppressor factor J6B7) (ISF) (Lysosomal H(+)-transporting ATPase V0 subunit a2) (ShIF) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2)
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[ATP6V0A1 ATP6N1 ATP6N1A VPP1] V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
[ST8SIA1 SIAT8 SIAT8A] Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.99.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (Ganglioside GT3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI)
[Atp6v0a4 Atp6n1b] V-type proton ATPase 116 kDa subunit a isoform 4 (V-ATPase 116 kDa isoform a4) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4) (Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform)
[Atp6v0a1 Atp6n1] V-type proton ATPase 116 kDa subunit a isoform 1 (V-ATPase 116 kDa isoform a1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
[st8sia1 siat8a] Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase (EC 2.4.99.8) (Alpha-2,8-sialyltransferase 8A) (Ganglioside GD3 synthase) (XlGD3 synthase) (Sialyltransferase 8A) (SIAT8-A) (Sialyltransferase St8Sia I) (ST8SiaI)
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[CPT1A CPT1] Carnitine O-palmitoyltransferase 1, liver isoform (CPT1-L) (EC 2.3.1.21) (Carnitine O-palmitoyltransferase I, liver isoform) (CPT I) (CPTI-L) (Carnitine palmitoyltransferase 1A)
[] Sarafotoxin [Cleaved into: Sarafotoxin-A, Ser-isoform (SRTX-A) (Sarafotoxin-A) (S6A); Sarafotoxin-C (SRTX-C) (S6C); Sarafotoxin-B (SRTX-B) (S6B); Sarafotoxin-E (SRTX-E) (S6E); Sarafotoxin-A, Thr-isoform]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)

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