NOCT_DROME
ID NOCT_DROME Reviewed; 642 AA.
AC A8JQX3; A0A0B4KH43; A0A0C4DHA6; C0PPK5; Q3ZAP4; Q6AWF6; Q8MTZ6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nocturnin {ECO:0000303|PubMed:19581445, ECO:0000312|FlyBase:FBgn0261808};
DE EC=3.1.3.- {ECO:0000269|PubMed:31147539};
DE AltName: Full=Curled {ECO:0000303|PubMed:19581445, ECO:0000312|FlyBase:FBgn0261808};
GN Name=cu {ECO:0000303|PubMed:19581445, ECO:0000312|FlyBase:FBgn0261808};
GN ORFNames=CG31299 {ECO:0000312|FlyBase:FBgn0261808};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAK85704.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX PubMed=11747467; DOI=10.1186/1471-2164-2-9;
RA Dupressoir A., Morel A.-P., Barbot W., Loireau M.-P., Corbo L.,
RA Heidmann T.;
RT "Identification of four families of yCCR4- and Mg2+-dependent endonuclease-
RT related proteins in higher eukaryotes, and characterization of orthologs of
RT yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2
RT binding.";
RL BMC Genomics 2:9-9(2001).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAZ86746.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAZ86746.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAZ86746.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:AAZ86746.1, ECO:0000312|EMBL:ACN38810.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAZ86746.1, ECO:0000312|EMBL:ACN38810.1};
RA Stapleton M., Booth B., Carlson J., Chavez C., Frise E., George R.,
RA Pacleb J., Park S., Wan K., Yu C., Celniker S., Sandler J., Wan K.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:AAT94521.1}
RP NNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-642.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAT94521.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX DOI=10.1266/jjg.31.321;
RA Nozawa K.;
RT "The Effects Of The Environmental Conditions On Curled Expressivity And The
RT Interaction Between Two Mimic Genes, Curled And Curly, In Drosophila
RT Melanogaster.";
RL Jpn. J. Genet. 31:321-326(1956).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY FOOD DEPRIVATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19581445; DOI=10.1534/genetics.109.105601;
RA Groenke S., Bickmeyer I., Wunderlich R., Jaeckle H., Kuehnlein R.P.;
RT "Curled encodes the Drosophila homolog of the vertebrate circadian
RT deadenylase Nocturnin.";
RL Genetics 183:219-232(2009).
RN [9] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19966839; DOI=10.1038/nn.2451;
RA Nagoshi E., Sugino K., Kula E., Okazaki E., Tachibana T., Nelson S.,
RA Rosbash M.;
RT "Dissecting differential gene expression within the circadian neuronal
RT circuit of Drosophila.";
RL Nat. Neurosci. 13:60-68(2010).
RN [10] {ECO:0000305}
RP FUNCTION, ASSOCIATION WITH THE CCR4-NOT COMPLEX, AND MUTAGENESIS OF ASP-491
RP AND ASN-493.
RX PubMed=20504953; DOI=10.1261/rna.2145110;
RA Temme C., Zhang L., Kremmer E., Ihling C., Chartier A., Sinz A.,
RA Simonelig M., Wahle E.;
RT "Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA
RT deadenylation.";
RL RNA 16:1356-1370(2010).
RN [11] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, LACK OF ADENYLASE ACTIVITY, AND MUTAGENESIS
RP OF GLU-363.
RX PubMed=31147539; DOI=10.1038/s41467-019-10125-z;
RA Estrella M.A., Du J., Chen L., Rath S., Prangley E., Chitrakar A., Aoki T.,
RA Schedl P., Rabinowitz J., Korennykh A.;
RT "The metabolites NADP+ and NADPH are the targets of the circadian protein
RT Nocturnin (Curled).";
RL Nat. Commun. 10:2367-2367(2019).
CC -!- FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to
CC NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference
CC for NADPH over NADP(+) (PubMed:31147539). Because of its association
CC with the CCR4-NOT complex, has a role in mRNA deadenylation and decay
CC (PubMed:20504953). Required at the pupal stage for proper wing
CC morphogenesis after eclosion (PubMed:19581445).
CC {ECO:0000269|PubMed:19581445, ECO:0000269|PubMed:20504953,
CC ECO:0000269|PubMed:31147539}.
CC -!- FUNCTION: [Isoform C]: Doesn't have a role in light-mediated behavioral
CC response. {ECO:0000269|PubMed:19966839}.
CC -!- FUNCTION: [Isoform D]: In dorsal neurons, contributes to the light-
CC mediated behavioral response. {ECO:0000269|PubMed:19966839}.
CC -!- FUNCTION: [Isoform E]: Doesn't have a role in light-mediated behavioral
CC response. {ECO:0000269|PubMed:19966839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31147539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051;
CC Evidence={ECO:0000269|PubMed:31147539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:31147539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665;
CC Evidence={ECO:0000269|PubMed:31147539};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC Note=Binds 2 magnesium ions, but the ions are only loosely bound to the
CC protein. {ECO:0000250|UniProtKB:Q9UK39};
CC -!- SUBUNIT: Associates to the CCR4-NOT complex composed of at least
CC Pop2/Caf1-55, Ccr4, Not1, Rga/Not2, and Not3.
CC {ECO:0000269|PubMed:20504953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19581445}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=D {ECO:0000303|PubMed:19581445, ECO:0000303|PubMed:19966839,
CC ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-1; Sequence=Displayed;
CC Name=F {ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-2; Sequence=VSP_060324;
CC Name=E {ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-3; Sequence=VSP_060328;
CC Name=C {ECO:0000303|PubMed:19581445, ECO:0000303|PubMed:19966839,
CC ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-4; Sequence=VSP_060327;
CC Name=H {ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-5; Sequence=VSP_060326;
CC Name=G {ECO:0000312|FlyBase:FBgn0261808};
CC IsoId=A8JQX3-6; Sequence=VSP_060325;
CC -!- TISSUE SPECIFICITY: Expressed in the head, in the dorsal neurons DN3, a
CC subgroup of clock neurons (at protein level) (PubMed:19966839).
CC Ubiquitously expressed in both males and females (PubMed:19581445).
CC {ECO:0000269|PubMed:19581445, ECO:0000269|PubMed:19966839}.
CC -!- DEVELOPMENTAL STAGE: Expressed at every stage (PubMed:19581445).
CC Expressed in the embryonic salivary glands, the distal part of the
CC proventriculus and the ring gland as well as weak expression in the
CC midgut (PubMed:19581445). At third instar larval stage, expressed at
CC the proventricular and ring gland (PubMed:19581445). No transcript
CC detected in the larval central brain, in the imaginal disks, the
CC salivary glands, or in the fat body (PubMed:19581445).
CC {ECO:0000269|PubMed:19581445}.
CC -!- INDUCTION: Nutritional conditions, such as food deprivation, and higher
CC temperature during the larval stage increase protein expression in the
CC adult flies (Ref.7, PubMed:19581445). Levels of expression at the pupal
CC stage are phenocritical for the cu-dependent wing phenotype
CC (PubMed:19581445). In the dorsal neurons DN3, a subgroup of clock
CC neurons, accumulates rhythmically with a peak around ZT12
CC (PubMed:19966839). {ECO:0000269|PubMed:19581445,
CC ECO:0000269|PubMed:19966839, ECO:0000269|Ref.7}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile with upward bent (curled)
CC wings and proximally crossed posterior scutellar bristles
CC (PubMed:19581445). RNAi-mediated knockdown has a similar phenotype
CC (PubMed:19581445). RNAi-mediated knockdown in the wing, nervous system,
CC ring gland, muscles, fat body, tracheal system, salivary gland, or gut
CC has no impact on wing morphogenesis (PubMed:19581445).
CC {ECO:0000269|PubMed:19581445}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC -!- CAUTION: The purified protein lacks deadenylase activity.
CC {ECO:0000269|PubMed:31147539}.
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DR EMBL; AY043266; AAK85704.1; -; mRNA.
DR EMBL; AE014297; AAF54600.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF54601.3; -; Genomic_DNA.
DR EMBL; AE014297; ABW08639.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08640.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08641.1; -; Genomic_DNA.
DR EMBL; AE014297; AGB95853.1; -; Genomic_DNA.
DR EMBL; BT023825; AAZ86746.1; -; mRNA.
DR EMBL; BT015292; AAT94521.1; -; mRNA.
DR EMBL; BT025859; ABF85759.1; -; mRNA.
DR EMBL; BT070224; ACN38810.1; -; mRNA.
DR RefSeq; NP_001097745.1; NM_001104275.3. [A8JQX3-4]
DR RefSeq; NP_001097746.1; NM_001104276.2. [A8JQX3-1]
DR RefSeq; NP_001097747.1; NM_001104277.2. [A8JQX3-3]
DR RefSeq; NP_001262471.1; NM_001275542.1. [A8JQX3-5]
DR RefSeq; NP_731539.2; NM_169374.2. [A8JQX3-6]
DR RefSeq; NP_731540.2; NM_169375.2. [A8JQX3-2]
DR AlphaFoldDB; A8JQX3; -.
DR SMR; A8JQX3; -.
DR IntAct; A8JQX3; 1.
DR STRING; 7227.FBpp0112131; -.
DR PaxDb; A8JQX3; -.
DR PRIDE; A8JQX3; -.
DR DNASU; 41339; -.
DR EnsemblMetazoa; FBtr0113218; FBpp0112130; FBgn0261808. [A8JQX3-4]
DR EnsemblMetazoa; FBtr0113219; FBpp0112131; FBgn0261808. [A8JQX3-1]
DR EnsemblMetazoa; FBtr0113220; FBpp0112132; FBgn0261808. [A8JQX3-3]
DR EnsemblMetazoa; FBtr0335218; FBpp0307205; FBgn0261808. [A8JQX3-2]
DR EnsemblMetazoa; FBtr0335219; FBpp0307206; FBgn0261808. [A8JQX3-6]
DR EnsemblMetazoa; FBtr0335220; FBpp0307207; FBgn0261808. [A8JQX3-5]
DR GeneID; 41339; -.
DR KEGG; dme:Dmel_CG31299; -.
DR UCSC; CG31299-RC; d. melanogaster.
DR UCSC; CG31299-RD; d. melanogaster. [A8JQX3-1]
DR UCSC; CG31299-RE; d. melanogaster.
DR CTD; 41339; -.
DR FlyBase; FBgn0261808; cu.
DR VEuPathDB; VectorBase:FBgn0261808; -.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000155249; -.
DR HOGENOM; CLU_411195_0_0_1; -.
DR InParanoid; A8JQX3; -.
DR OMA; PTGECCS; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; A8JQX3; -.
DR BRENDA; 3.1.3.108; 1994.
DR BioGRID-ORCS; 41339; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41339; -.
DR PRO; PR:A8JQX3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261808; Expressed in embryonic/larval hemocyte (Drosophila) and 30 other tissues.
DR ExpressionAtlas; A8JQX3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019178; F:NADP phosphatase activity; IDA:UniProtKB.
DR GO; GO:0102757; F:NADPH phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:InterPro.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:InterPro.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040109; Nocturnin.
DR PANTHER; PTHR12121:SF45; PTHR12121:SF45; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..642
FT /note="Nocturnin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000448000"
FT REGION 50..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 453..456
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 491..493
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 600
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT VAR_SEQ 1..223
FT /note="MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLED
FT DDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQ
FT SAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAAR
FT KLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR -> MK
FT LISTVVYLLVAFYKFAKKLL (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_060324"
FT VAR_SEQ 1..223
FT /note="MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLED
FT DDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQ
FT SAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAAR
FT KLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVR -> ME
FT FLMKTSRLIVTSKTFARRVAVPIPSKVKMGQFYTSQRHSHSLFIFSIILRKILYRKPNA
FT L (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_060325"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_060326"
FT VAR_SEQ 1..222
FT /note="MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLED
FT DDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQ
FT SAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAAR
FT KLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV -> MEP
FT AVPIKRANKAPCKNDRKAYLQKVMLT (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_060327"
FT VAR_SEQ 1..222
FT /note="MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLED
FT DDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQ
FT SAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAAR
FT KLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLV -> MEF
FT LMKTSRLIVTSKTFARRVAVPIP (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_060328"
FT MUTAGEN 363
FT /note="E->A: Disrupts catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 491
FT /note="D->A: Decreases mRNA deadelynation and decay; when
FT associated with A-493."
FT /evidence="ECO:0000269|PubMed:20504953"
FT MUTAGEN 493
FT /note="N->A: Decreases mRNA deadelynation and decay; when
FT associated with A-491."
FT /evidence="ECO:0000269|PubMed:20504953"
FT CONFLICT 579
FT /note="D -> Y (in Ref. 5; AAT94521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 71880 MW; 4AF5B5856E82C41B CRC64;
MDQKTTGLRE NYGHRRQPAL GKAMPVTALL LNLESNPLDY SRNDIGAELL EDDDKPPQLF
SVTDEPPSPN EEDYKPPNHH EDDGKLAGER HREIPCSNCL KTAPGHLIDR QSAINEMCQR
LCGPECRRPQ GLTLDGVRQD FLRQYEIAEA VAKTSAMTST VQMKQRLAAR KLEFEKEMEM
DEQLGVASPR NDINLGQSST VAATGMGEFE FEPPRDLLLY LVRMGSFNSA PKINNVDSQD
DGLVLPSGLS TPALLQHVQQ LRGGGIEQPS LLTRGFLKPL LADEDVADGL RCLKLNSVSR
VCSAPVEGDD IRLLQWNILS QTLGQHNDGF VRCPEEALTW EHRKYLIVQE ILQNQPDVIC
LQEVDHFKFL QTVLGSQNYA GIFFPKPDSP CLYIEQNNGP DGCAIFYKRD KLQLQGYDTR
ILEVWRVQSN QVAIAARLRM RSSGREFCVA TTHLKARHGA LLAKLRNEQG RDLIRFVKQF
AGDTPLLLCG DFNAEPVEPI YATILGCDLL RLGSAYADVK LDREEILHPN ADVGEFVAKS
MKREPPYTTW KIREEGEECH TIDYVFYTPD RLKIKNCLDF PAGEQIGKNR TPSFQYPSDH
FSLVCDFELL PPTENGKESG SGSGSDGENE TEVEGSKHGS IQ
