SEH1_DANRE
ID SEH1_DANRE Reviewed; 364 AA.
AC Q6TGU2; Q1LXR9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
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; Synonyms=sec13l; ORFNames=si:dkey-263o22.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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 complex may function in the amino
CC acid-sensing branch of the TORC1 signaling pathway.
CC {ECO:0000250|UniProtKB:Q96EE3}.
CC -!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). Probably part of the GATOR complex.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY398414; AAQ97847.1; -; mRNA.
DR EMBL; BX294130; CAK10890.1; -; Genomic_DNA.
DR RefSeq; NP_956217.2; NM_199923.2.
DR AlphaFoldDB; Q6TGU2; -.
DR SMR; Q6TGU2; -.
DR STRING; 7955.ENSDARP00000003173; -.
DR PaxDb; Q6TGU2; -.
DR Ensembl; ENSDART00000013865; ENSDARP00000003173; ENSDARG00000004280.
DR GeneID; 334749; -.
DR KEGG; dre:334749; -.
DR CTD; 81929; -.
DR ZFIN; ZDB-GENE-030131-6689; seh1l.
DR eggNOG; KOG2445; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_1_2_1; -.
DR InParanoid; Q6TGU2; -.
DR OMA; NAPTRRW; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; Q6TGU2; -.
DR TreeFam; TF105924; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DRE-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DRE-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DRE-191859; snRNP Assembly.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-DRE-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DRE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DRE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DRE-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-DRE-9639288; Amino acids regulate mTORC1.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q6TGU2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000004280; Expressed in presomitic mesoderm and 26 other tissues.
DR ExpressionAtlas; Q6TGU2; baseline and differential.
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: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; IBA:GO_Central.
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; IBA:GO_Central.
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 Kinetochore; Lysosome; Membrane; Mitosis; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..364
FT /note="Nucleoporin SEH1"
FT /id="PRO_0000383047"
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 CONFLICT 353
FT /note="T -> S (in Ref. 1; AAQ97847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39817 MW; F31094B978B03263 CRC64;
MFVAKSIAAD HKDLIHDVSY DFHGRRMATC SSDQSVKVWD KGDDGEWHCT ASWKTHSGSV
WRVTWAHPEF GQVLASCSFD RTAAVWEEIV GESNDKQRGQ SHWIKRTTLV DSRTSVTDVK
FAPKHMGLML TTCSADGVVR IYEAPDVMNL SQWSLQHEIS CKLACSCISW NPSSSRAHPP
MIAVGGDDSN GAYSGKVQIH EYNENTRKYA KAETLMTVTD PVHDIAFAPN LGRSFHVLAI
ATKDVRIFKL LPLRRESANS SGPTKFEVQV MAQFDSHNSQ VWRVSWNITS TLLASSGDDG
CVRLWKANYM DNWKCTGILR GDGSPVNGSS GPSAALSAVG VPGAAQMIVG AATAGRKKAQ
LMPG
