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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
 
 
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