SEH1_MOUSE
ID SEH1_MOUSE Reviewed; 360 AA.
AC Q8R2U0; Q3TLC9; Q3UP79; Q9D0K7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Nucleoporin SEH1 {ECO:0000305};
DE AltName: Full=GATOR complex protein SEH1 {ECO:0000305};
DE AltName: Full=Nup107-160 subcomplex subunit SEH1;
GN Name=Seh1l;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, Spleen, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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).
CC -!- FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). The Nup107-160 subcomplex is required for the assembly
CC of a functional NPC. The Nup107-160 subcomplex is also required for
CC normal kinetochore microtubule attachment, mitotic progression and
CC chromosome segregation. This subunit plays a role in recruitment of the
CC Nup107-160 subcomplex to the kinetochore.
CC {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex. It is negatively regulated by the
CC upstream amino acid sensors SESN2 and CASTOR1.
CC {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133,
CC NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. The SEH1 subunit
CC appears to be only weakly associated with the Nup107-160 subcomplex.
CC Within the GATOR complex, component of the GATOR2 subcomplex, made of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2
CC complex interacts with CASTOR2 and CASTOR1; the interaction is
CC negatively regulated by arginine. The GATOR2 complex interacts with
CC SESN1, SESN2 and SESN3; the interaction is negatively regulated by
CC amino acids. {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q96EE3}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q96EE3}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2U0-2; Sequence=VSP_037232;
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25518.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK011330; BAB27549.1; -; mRNA.
DR EMBL; AK088835; BAC40603.1; -; mRNA.
DR EMBL; AK143727; BAE25518.1; ALT_FRAME; mRNA.
DR EMBL; AK166573; BAE38863.1; -; mRNA.
DR EMBL; AK169231; BAE41000.1; -; mRNA.
DR EMBL; AK169388; BAE41135.1; -; mRNA.
DR EMBL; AK170591; BAE41899.1; -; mRNA.
DR EMBL; CH466528; EDL09627.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL09628.1; -; Genomic_DNA.
DR EMBL; BC027244; AAH27244.1; -; mRNA.
DR CCDS; CCDS50312.1; -. [Q8R2U0-1]
DR CCDS; CCDS89269.1; -. [Q8R2U0-2]
DR RefSeq; NP_001034177.1; NM_001039088.1. [Q8R2U0-1]
DR RefSeq; NP_082388.1; NM_028112.2. [Q8R2U0-2]
DR AlphaFoldDB; Q8R2U0; -.
DR SMR; Q8R2U0; -.
DR BioGRID; 215167; 29.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR STRING; 10090.ENSMUSP00000025421; -.
DR iPTMnet; Q8R2U0; -.
DR PhosphoSitePlus; Q8R2U0; -.
DR EPD; Q8R2U0; -.
DR MaxQB; Q8R2U0; -.
DR PaxDb; Q8R2U0; -.
DR PeptideAtlas; Q8R2U0; -.
DR PRIDE; Q8R2U0; -.
DR ProteomicsDB; 256538; -. [Q8R2U0-1]
DR ProteomicsDB; 256539; -. [Q8R2U0-2]
DR Antibodypedia; 48526; 21 antibodies from 10 providers.
DR DNASU; 72124; -.
DR Ensembl; ENSMUST00000025421; ENSMUSP00000025421; ENSMUSG00000079614. [Q8R2U0-1]
DR Ensembl; ENSMUST00000237700; ENSMUSP00000157877; ENSMUSG00000079614. [Q8R2U0-2]
DR GeneID; 72124; -.
DR KEGG; mmu:72124; -.
DR UCSC; uc008fmx.1; mouse. [Q8R2U0-1]
DR CTD; 81929; -.
DR MGI; MGI:1919374; Seh1l.
DR VEuPathDB; HostDB:ENSMUSG00000079614; -.
DR eggNOG; KOG2445; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_1_2_1; -.
DR InParanoid; Q8R2U0; -.
DR OMA; NAPTRRW; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q8R2U0; -.
DR TreeFam; TF105924; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 72124; 30 hits in 73 CRISPR screens.
DR ChiTaRS; Seh1l; mouse.
DR PRO; PR:Q8R2U0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8R2U0; protein.
DR Bgee; ENSMUSG00000079614; Expressed in metanephric ureteric bud and 267 other tissues.
DR Genevisible; Q8R2U0; MM.
DR GO; GO:0061700; C:GATOR2 complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0035859; C:Seh1-associated complex; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037597; Nucleoporin_Seh1.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF3; PTHR11024:SF3; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Isopeptide bond; Kinetochore; Lysosome; Membrane;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..360
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000373806"
FT REPEAT 10..49
FT /note="WD 1"
FT REPEAT 55..96
FT /note="WD 2"
FT REPEAT 111..152
FT /note="WD 3"
FT REPEAT 160..210
FT /note="WD 4"
FT REPEAT 217..258
FT /note="WD 5"
FT REPEAT 276..315
FT /note="WD 6"
FT REGION 326..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EE3"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96EE3"
FT VAR_SEQ 358..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037232"
FT CONFLICT 37
FT /note="K -> R (in Ref. 1; BAE38863)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="L -> V (in Ref. 1; BAE25518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39775 MW; 3B47A6357F1D37A9 CRC64;
MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV
WRVTWAHPEF GQVLASCSFD RTAAVWEEIV GESNDKLRGQ SHWVKRTTLV DSRTSVTDVK
FAPKHMGLML ATCSADGIVR VYEAPDVMNL SQWSLQHEVS CKLCCSCISW NPSSSRAHPP
MIAVGSDDSS PNSMAKVQIF EYNENTRKYA KAETLMTVTD PVHDIAFAPN LGRSFHILAV
ATKDVRIFTL KPLRKELTSS GGPTKFEIHI VAQFDNHNSQ VWRVSWNITG TVLASSGDDG
CVRLWKANYM DNWKCTGILK GNGSPVNGSS QLGNSNPSLS SNIPNLQNSL NGTSASRKHS
