CNOT1_MOUSE
ID CNOT1_MOUSE Reviewed; 2375 AA.
AC Q6ZQ08; B2RY28; Q3UPB7; Q8BSB4; Q8BXB2; Q8C0H2; Q8K3D8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=CCR4-NOT transcription complex subunit 1;
DE AltName: Full=CCR4-associated factor 1;
GN Name=Cnot1; Synonyms=Kiaa1007;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-2305 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 203-847 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 533-1302 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1819-2375 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Spleen, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1247-2375 (ISOFORM 1/2).
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 918-2375 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS2.
RX PubMed=20133598; DOI=10.1073/pnas.0908664107;
RA Suzuki A., Igarashi K., Aisaki K., Kanno J., Saga Y.;
RT "NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to
RT suppression of specific RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3594-3599(2010).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22367759; DOI=10.1002/stem.1070;
RA Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P.,
RA Archer T.K., Jothi R., Hu G.;
RT "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit
RT extraembryonic differentiation.";
RL Stem Cells 30:910-922(2012).
RN [9]
RP MUTAGENESIS OF ARG-535.
RX PubMed=31006513; DOI=10.1016/j.ajhg.2019.03.018;
RA De Franco E., Watson R.A., Weninger W.J., Wong C.C., Flanagan S.E.,
RA Caswell R., Green A., Tudor C., Lelliott C.J., Geyer S.H., Maurer-Gesek B.,
RA Reissig L.F., Lango Allen H., Caliebe A., Siebert R., Holterhus P.M.,
RA Deeb A., Prin F., Hilbrands R., Heimberg H., Ellard S., Hattersley A.T.,
RA Barroso I.;
RT "A specific CNOT1 mutation results in a novel syndrome of pancreatic
RT agenesis and holoprosencephaly through impaired pancreatic and neurological
RT development.";
RL Am. J. Hum. Genet. 104:985-989(2019).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=31006510; DOI=10.1016/j.ajhg.2019.03.017;
RA Kruszka P., Berger S.I., Weiss K., Everson J.L., Martinez A.F., Hong S.,
RA Anyane-Yeboa K., Lipinski R.J., Muenke M.;
RT "A CCR4-NOT transcription complex, subunit 1, CNOT1, variant associated
RT with holoprosencephaly.";
RL Am. J. Hum. Genet. 104:990-993(2019).
RN [11]
RP INTERACTION WITH YTHDF2.
RX PubMed=32905781; DOI=10.1016/j.celrep.2020.108120;
RA Liu J., Gao M., Xu S., Chen Y., Wu K., Liu H., Wang J., Yang X., Wang J.,
RA Liu W., Bao X., Chen J.;
RT "YTHDF2/3 are required for somatic reprogramming through different RNA
RT deadenylation pathways.";
RL Cell Rep. 32:108120-108120(2020).
CC -!- FUNCTION: Scaffolding component of the CCR4-NOT complex which is one of
CC the major cellular mRNA deadenylases and is linked to various cellular
CC processes including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. Its scaffolding
CC function implies its interaction with the catalytic complex module and
CC diverse RNA-binding proteins mediating the complex recruitment to
CC selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-
CC containing mRNAs probably via association with ZFP36. Mediates the
CC recruitment of the CCR4-NOT complex to miRNA targets and to the RISC
CC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a
CC transcriptional repressor. Represses the ligand-dependent
CC transcriptional activation by nuclear receptors. Involved in the
CC maintenance of embryonic stem (ES) cell identity; prevents their
CC differentiation towards extraembryonic trophectoderm lineages.
CC {ECO:0000269|PubMed:22367759}.
CC -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to
CC exist that differ in the participation of probably mutually exclusive
CC catalytic subunits (By similarity). In the complex, interacts directly
CC with CNOT6, CNOT6L, CNOT7 or CNOT8 (By similarity). Interacts in a
CC ligand-dependent fashion with ESR1 and RXRA (By similarity). Interacts
CC with NANOS2, TOB1 and ZFP36 (PubMed:20133598). Interacts with TNRC6A,
CC TNRC6B or TNRC6C; the interactions are direct (By similarity).
CC Interacts with YTHDF2; the interaction is direct and promotes
CC recruitment of the CCR4-NOT complex to N6-methyladenosine (m6A)-
CC containing mRNAs, leading to their deadenylation and subsequent
CC degradation (PubMed:32905781). Interacts with EIF4ENIF1/4E-T (By
CC similarity). {ECO:0000250|UniProtKB:A5YKK6,
CC ECO:0000269|PubMed:20133598, ECO:0000269|PubMed:32905781}.
CC -!- INTERACTION:
CC Q6ZQ08; P60322: Nanos2; NbExp=3; IntAct=EBI-682479, EBI-6507212;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:20133598}.
CC Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=NANOS2 promotes
CC its localization to P-body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZQ08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQ08-2; Sequence=VSP_030565, VSP_030566;
CC Name=3;
CC IsoId=Q6ZQ08-3; Sequence=VSP_030564;
CC Name=4;
CC IsoId=Q6ZQ08-4; Sequence=VSP_030565;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells and in
CC inner cell mass (ICM) of the blastocyst. At 8.25 dpc it is expressed in
CC both the neuroectoderm and mesenchyme of the neural folds but not in
CC extra-embryonic membranes (PubMed:31006510).
CC {ECO:0000269|PubMed:22367759, ECO:0000269|PubMed:31006510}.
CC -!- DOMAIN: Contains Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, a motif known to
CC be important for the association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CNOT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27364.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28830.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE25479.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC113951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031357; BAC27364.1; ALT_INIT; mRNA.
DR EMBL; AK034776; BAC28830.1; ALT_INIT; mRNA.
DR EMBL; AK048177; BAC33267.1; -; mRNA.
DR EMBL; AK143651; BAE25479.1; ALT_INIT; mRNA.
DR EMBL; BC018281; AAH18281.2; -; mRNA.
DR EMBL; BC158073; AAI58074.1; -; mRNA.
DR EMBL; AK129258; BAC98068.2; -; Transcribed_RNA.
DR CCDS; CCDS90442.1; -. [Q6ZQ08-4]
DR RefSeq; NP_835179.1; NM_178078.2. [Q6ZQ08-2]
DR RefSeq; XP_006530937.1; XM_006530874.2.
DR AlphaFoldDB; Q6ZQ08; -.
DR SMR; Q6ZQ08; -.
DR BioGRID; 231545; 15.
DR DIP; DIP-46845N; -.
DR ELM; Q6ZQ08; -.
DR IntAct; Q6ZQ08; 18.
DR MINT; Q6ZQ08; -.
DR STRING; 10090.ENSMUSP00000096073; -.
DR CarbonylDB; Q6ZQ08; -.
DR iPTMnet; Q6ZQ08; -.
DR PhosphoSitePlus; Q6ZQ08; -.
DR EPD; Q6ZQ08; -.
DR MaxQB; Q6ZQ08; -.
DR PaxDb; Q6ZQ08; -.
DR PeptideAtlas; Q6ZQ08; -.
DR PRIDE; Q6ZQ08; -.
DR ProteomicsDB; 283460; -. [Q6ZQ08-1]
DR ProteomicsDB; 283461; -. [Q6ZQ08-2]
DR ProteomicsDB; 283462; -. [Q6ZQ08-3]
DR ProteomicsDB; 283463; -. [Q6ZQ08-4]
DR Antibodypedia; 29121; 99 antibodies from 21 providers.
DR Ensembl; ENSMUST00000098473; ENSMUSP00000096073; ENSMUSG00000036550. [Q6ZQ08-4]
DR GeneID; 234594; -.
DR KEGG; mmu:234594; -.
DR UCSC; uc009myy.1; mouse. [Q6ZQ08-3]
DR UCSC; uc009myz.3; mouse. [Q6ZQ08-2]
DR CTD; 23019; -.
DR MGI; MGI:2442402; Cnot1.
DR VEuPathDB; HostDB:ENSMUSG00000036550; -.
DR eggNOG; KOG1831; Eukaryota.
DR GeneTree; ENSGT00390000014869; -.
DR HOGENOM; CLU_000286_3_0_1; -.
DR InParanoid; Q6ZQ08; -.
DR OMA; IDEYHCY; -.
DR OrthoDB; 42530at2759; -.
DR PhylomeDB; Q6ZQ08; -.
DR TreeFam; TF105630; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR BioGRID-ORCS; 234594; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Cnot1; mouse.
DR PRO; PR:Q6ZQ08; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6ZQ08; protein.
DR Bgee; ENSMUSG00000036550; Expressed in embryonic post-anal tail and 122 other tissues.
DR ExpressionAtlas; Q6ZQ08; baseline and differential.
DR Genevisible; Q6ZQ08; MM.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISS:UniProtKB.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IBA:GO_Central.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISO:MGI.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:UniProtKB.
DR Gene3D; 1.25.40.840; -; 1.
DR InterPro; IPR007196; CCR4-Not_Not1_C.
DR InterPro; IPR032191; CNOT1_CAF1_bind.
DR InterPro; IPR024557; CNOT1_dom_4.
DR InterPro; IPR032194; CNOT1_HEAT.
DR InterPro; IPR032193; CNOT1_TTP_bind.
DR InterPro; IPR038535; CNOT1_TTP_bind_sf.
DR InterPro; IPR040398; Not1.
DR PANTHER; PTHR13162; PTHR13162; 1.
DR Pfam; PF16415; CNOT1_CAF1_bind; 1.
DR Pfam; PF16418; CNOT1_HEAT; 1.
DR Pfam; PF16417; CNOT1_TTP_bind; 1.
DR Pfam; PF12842; DUF3819; 1.
DR Pfam; PF04054; Not1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Translation regulation.
FT CHAIN 1..2375
FT /note="CCR4-NOT transcription complex subunit 1"
FT /id="PRO_0000315542"
FT REGION 725..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..1014
FT /note="Interaction with ZFP36"
FT /evidence="ECO:0000250"
FT REGION 1089..1604
FT /note="Interaction with CNOT6, CNOT6L, CNOT7 and CNOT8"
FT /evidence="ECO:0000250"
FT REGION 1314..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 153..157
FT /note="LXXLL"
FT MOTIF 181..185
FT /note="LXXLL"
FT MOTIF 223..227
FT /note="LXXLL"
FT MOTIF 570..574
FT /note="LXXLL"
FT MOTIF 1638..1642
FT /note="LXXLL"
FT MOTIF 1941..1945
FT /note="LXXLL"
FT MOTIF 2095..2099
FT /note="LXXLL"
FT COMPBIAS 1328..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A5YKK6"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A5YKK6"
FT VAR_SEQ 1..1881
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030564"
FT VAR_SEQ 777
FT /note="P -> PV (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030565"
FT VAR_SEQ 821..826
FT /note="SKMKPS -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030566"
FT MUTAGEN 535
FT /note="R->C: Homozygous mutant embryos show a small
FT pancreas, exencephaly, eye defects and edema."
FT /evidence="ECO:0000269|PubMed:31006513"
FT CONFLICT 2089
FT /note="I -> F (in Ref. 3; AAH18281)"
FT /evidence="ECO:0000305"
FT CONFLICT 2203
FT /note="N -> S (in Ref. 2; BAC33267)"
FT /evidence="ECO:0000305"
FT CONFLICT 2233
FT /note="G -> D (in Ref. 2; BAC27364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2375 AA; 266808 MW; 7771515027BA4B60 CRC64;
MNLDSLSLAL SQISYLVDNL TKKNYRASQQ EIQHIVNRHG PEADRHLLRC LFSHVDFSGD
GKSSGKDFHQ TQFLIQECAS LITKPNFIST LSYAIDNPLH YQKSLKPAPH LFAQLSKVLK
LSKVQEVIFG LALLNSSSPD LRGFAAQFIK QKLPDLLRSY IDADVSGNQE GGFQDIAIEV
LHLLLSHLLF GQKGAFGVGQ EQIDAFLKTL RRDFPQERCP VVLAPLLYPE KRDILMDRIL
PDSGGVAKTM MESSLADFMQ EVGYGFCASI EECRNIIMQF GVREVTAAQV ARVLGMMART
HSGLTDGIPL QSISAPGSGI WSDGKDKSEG AQAHTWNVEV LIDVLKELNP SLNFKEVTYE
LDHPGFQIRD SKGLHNVVYG IQRGLGMEVF PVDFIYRPWK HAEGQLSFIQ HSLINPEVFC
FADYPCHTVA TDILKAPPED DNREIATWKS LDLIESLLRL AEVGQYEQVK QLFSFPIKHC
PDMLVLALLQ INTSWHTLRH ELISTLMPIF LGNHPNSAII LHYAWHGQGQ SPSIRQLIMH
AMAEWYMRGE QYDQAKLSRI LDVAQDLKAL SMLLNGTPFA FVIDLAALAS RREYLKLDKW
LTDKIREHGE PFIQACMTFL KRRCPSILGG LAPEKDQPKS AQLPAETLAT MLACLQACAG
SVSQELSETI LTMVANCSNV MNKARQPPPG VMPKGRPPSA SSLDAISPVQ IDPLAGMASL
SIGGSAAPHT QSMQGFPPNL GSAFSTPQSP AKAFPPLSTP NQTTAFSGIG GLSSQLPGGL
GTGSLTGIGT GALGLPAVNN DPFVQRKLGT SGLNQPTFQQ SKMKPSDLSQ VWPEANQHFS
KEIDDEANSY FQRIYNHPPH PTMSVDEVLE MLQRFKDSTI KREREVFNCM LRNLFEEYRF
FPQYPDKELH ITACLFGGII EKGLVTYMAL GLALRYVLEA LRKPFGSKMY YFGIAALDRF
KNRLKDYPQY CQHLASISHF MQFPHHLQEY IEYGQQSRDP PVKMQGSITT PGSIALAQAQ
AQAQVPAKAP LAGQVNTMVT TSTTTTVAKT VTVTKPTGVS FKKDVPPSIN TTNIDTLLVA
TDQTERIVEP PENIQEKIAF IFNNLSQSNM TQKVEELKET VKEEFMPWVS QYLVMKRVSI
EPNFHSLYSN FLDTLKNPEF NKMVLNETYR NIKVLLTSDK AAANFSDRSL LKNLGHWLGM
ITLAKNKPIL HTDLDVKSLL LEAYVKGQQE LLYVVPFVAK VLESSIRSLV FRPPNPWTMA
IMNVLAELHQ EHDLKLNLKF EIEVLCKNLA LDINELKPGN LLKDKDRLKN LDEQLSAPKK
DVKQPEELPA ITTTTTSTTP ATSTTCTATV PPQPQYSYHD INVYSLAGLA PHITLNPTIP
LFQAHPQLKQ CVRQAIERAV QELVHPVVDR SIKIAMTTCE QIVRKDFALD SEESRMRIAA
HHMMRNLTAG MAMITCREPL LMSISTNLKN SFASALRTAS PQQREMMDQA AAQLAQDNCE
LACCFIQKTA VEKAGPEMDK RLATEFELRK HARQEGRRYC DPVVLTYQAE RMPEQIRLKV
GGVDPKQLAV YEEFARNVPG FLPTNDLSQP TGFLAQPMKQ AWATDDVAQI YDKCITELEQ
HLHAIPPTLA MNPQAQALRS LLEVVVLSRN SRDAIAALGL LQKAVEGLLD ATSGADADLL
LRYRECHLLV LKALQDGRAY GSPWCNKQIT RCLIECRDEY KYNVEAVELL IRNHLVNMQQ
YDLHLAQSME NGLNYMAVAF AMQLVKILLV DERSVAHITE ADLFHTIETL MRINAHSRGN
APEGLPQLME VVRSNYEAMI DRAHGGPNFM MHSGISQASE YDDPPGLREK AEYLLREWVN
LYHSAAAGRD STKAFSAFVG QMHQQGILKT DDLITRFFRL CTEMCVEISY RAQAEQQHNP
AANPTMIRAK CYHNLDAFVR LIALLVKHSG EATNTVTKIN LLNKVLGIVV GVLLQDHDVR
QSEFQQLPYH RIFIMLLLEL NAPEHVLETI NFQTLTAFCN TFHILRPTKA PGFVYAWLEL
ISHRIFIARM LAHTPQQKGW PMYAQLLIDL FKYLAPFLRN VELTKPMQIL YKGTLRVLLV
LLHDFPEFLC DYHYGFCDVI PPNCIQLRNL ILSAFPRNMR LPDPFTPNLK VDMLSEINIA
PRILTNFTGV MPPQFKKDLD SYLKTRSPVT FLSDLRSNLQ VSNEPGNRYN LQLINALVLY
VGTQAIAHIH NKGSTPSMST ITHSAHMDIF QNLAVDLDTE GRYLFLNAIA NQLRYPNSHT
HYFSCTMLYL FAEANTEAIQ EQITRVLLER LIVNRPHPWG LLITFIELIK NPAFKFWNHE
FVHCAPEIEK LFQSVAQCCM GQKQAQQVME GTGAS