SEH1_PONAB
ID SEH1_PONAB Reviewed; 360 AA.
AC Q5RAN6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; CR858979; CAH91174.1; -; mRNA.
DR RefSeq; NP_001125688.1; NM_001132216.1.
DR AlphaFoldDB; Q5RAN6; -.
DR SMR; Q5RAN6; -.
DR STRING; 9601.ENSPPYP00000010077; -.
DR GeneID; 100172610; -.
DR KEGG; pon:100172610; -.
DR CTD; 81929; -.
DR eggNOG; KOG2445; Eukaryota.
DR InParanoid; Q5RAN6; -.
DR OrthoDB; 944756at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
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: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:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Isopeptide bond; Kinetochore; Lysosome; Membrane; Mitosis; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Ubl conjugation;
KW WD repeat.
FT CHAIN 1..360
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000373807"
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 324..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EE3"
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"
SQ SEQUENCE 360 AA; 39671 MW; 1286531774C7C9B9 CRC64;
MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV
WRVTWAHPEF GQVLASCSFD RTAAVWEEIV GESNDKLRGQ SHWVKRTTLV DSRTSVTDVK
FAPKHMGLML ATCSADGIVR IYEAPDVMNL SQWSLQHEIS CKLSCSCISW NPSSSRAHSP
MIAVGSDDSS PNAMAKVQIF EYNENTRKYA KAETLMTVTD PVHDIAFAPN LGRSFHILAI
ATKDVRIFTL KPVRKELTSS GGPTKFEIHI VAHFDNHNSQ VWRVSWNITG TVLASSGDDG
CVRLWKANYM DNWKCTGILK GNGSPVNGSS QQGTSNPSLG SNIPSLQNSL NGSSAGRKHS
