ELYS_XENLA
ID ELYS_XENLA Reviewed; 2408 AA.
AC Q5U249;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein ELYS;
DE AltName: Full=Protein MEL-28;
DE AltName: Full=xELYS;
GN Name=ahctf1; Synonyms=elys;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH THE NUP107-160
RP COMPLEX.
RX PubMed=17098863; DOI=10.1073/pnas.0608484103;
RA Rasala B.A., Orjalo A.V., Shen Z., Briggs S., Forbes D.J.;
RT "ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore
RT assembly and proper cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17801-17806(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CHROMATIN-BINDING, AND
RP ASSOCIATION WITH THE NUP107-160 COMPLEX.
RX PubMed=17825564; DOI=10.1016/j.cub.2007.08.041;
RA Gillespie P.J., Khoudoli G.A., Stewart G., Swedlow J.R., Blow J.J.;
RT "ELYS/MEL-28 chromatin association coordinates nuclear pore complex
RT assembly and replication licensing.";
RL Curr. Biol. 17:1657-1662(2007).
RN [4]
RP FUNCTION, CHROMATIN-BINDING, ASSOCIATION WITH THE NUP107-160 COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17235358; DOI=10.1038/sj.embor.7400889;
RA Franz C., Walczak R., Yavuz S., Santarella R., Gentzel M., Askjaer P.,
RA Galy V., Hetzer M., Mattaj I.W., Antonin W.;
RT "MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin
RT and postmitotic nuclear pore complex assembly.";
RL EMBO Rep. 8:165-172(2007).
RN [5]
RP FUNCTION, CHROMATIN-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 2332-ARG--ARG-2334.
RX PubMed=18596237; DOI=10.1091/mbc.e08-01-0012;
RA Rasala B.A., Ramos C., Harel A., Forbes D.J.;
RT "Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate
RT nuclear pore assembly.";
RL Mol. Biol. Cell 19:3982-3996(2008).
CC -!- FUNCTION: Required for the assembly of a functional nuclear pore
CC complex (NPC) on the surface of chromosomes as nuclei form at the end
CC of mitosis. May initiate NPC assembly by binding to chromatin and
CC recruiting the Nup107-160 subcomplex, which may in turn recruit
CC membrane vesicles containing pom121 and tmem48/ndc1. Association with
CC chromatin may require the presence of the mcm2-mcm7 complex, suggesting
CC a mechanism for coordination of nuclear assembly and the inactivation
CC of replication licensing. {ECO:0000269|PubMed:17235358,
CC ECO:0000269|PubMed:17825564, ECO:0000269|PubMed:18596237}.
CC -!- SUBUNIT: Interacts with the Nup107-160 subcomplex of the NPC.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8CJF7}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17235358}. Note=Binds to chromatin during mitosis,
CC and chromatin binding increases as nuclei assemble and grows through
CC interphase (PubMed:17235358). Does not localize to the pores of
CC annulate lamellae, which are cytoplasmic stacks of membrane that form
CC in rapidly dividing cells (PubMed:18596237).
CC {ECO:0000269|PubMed:17235358, ECO:0000269|PubMed:18596237}.
CC -!- DOMAIN: The N-terminus forms a highly conserved seven-bladed beta
CC propeller decorated with long loops and mediates anchorage to the
CC Nup107-160 subcomplex of the nuclear pore, synergistically with the
CC central alpha domain. The disordered C-terminus is responsible for the
CC interactions with chromatin (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELYS 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; BC086281; AAH86281.1; -; mRNA.
DR RefSeq; NP_001081199.1; NM_001087730.1.
DR PDB; 7VCI; EM; 8.10 A; T=1-2408.
DR PDB; 7WB4; EM; 5.60 A; N/n=1-2408.
DR PDBsum; 7VCI; -.
DR PDBsum; 7WB4; -.
DR AlphaFoldDB; Q5U249; -.
DR SMR; Q5U249; -.
DR BioGRID; 99047; 8.
DR IntAct; Q5U249; 1.
DR MaxQB; Q5U249; -.
DR GeneID; 397707; -.
DR KEGG; xla:397707; -.
DR CTD; 397707; -.
DR Xenbase; XB-GENE-866620; ahctf1.L.
DR OrthoDB; 1040332at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 397707; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR032040; ELYS-bb.
DR InterPro; IPR025151; ELYS_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR Pfam; PF13934; ELYS; 1.
DR Pfam; PF16687; ELYS-bb; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..2408
FT /note="Protein ELYS"
FT /id="PRO_0000383575"
FT DNA_BIND 2329..2341
FT /note="A.T hook"
FT /evidence="ECO:0000269|PubMed:18596237"
FT REGION 1..492
FT /note="Seven-bladed beta propeller repeats"
FT /evidence="ECO:0000250|UniProtKB:Q8CJF7"
FT REGION 1016..2408
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:Q8CJF7"
FT REGION 2281..2408
FT /note="Sufficient to block nuclear pore assembly"
FT /evidence="ECO:0000269|PubMed:18596237"
FT REGION 2281..2359
FT /note="Sufficient for chromatin-binding"
FT /evidence="ECO:0000269|PubMed:18596237"
FT REGION 2359..2408
FT /note="Sufficient for chromatin-binding"
FT /evidence="ECO:0000269|PubMed:18596237"
FT COMPBIAS 1123..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2139..2160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2332..2334
FT /note="RGR->AGA: Impairs the ability of the C-terminal
FT fragment to block nuclear pore assembly."
FT /evidence="ECO:0000269|PubMed:18596237"
SQ SEQUENCE 2408 AA; 268445 MW; 4C50DFD7303DFB9E CRC64;
MQNLEAQVTG SLVAFPDVTQ KALKEDEINL DSVLRGKFST GRTSLAWLAC GPQLEITNSV
TGERISAYHF SGLTERPPVV VAVKEFTWQK KTGLLVGLVE AEGSVLCLYD IGISKVVKAV
VLPGSVTAVE PIINHGGASA STQHLHQSLR WFFGVTAVVT DVGHVLLIDL CLDEVSSNQD
ELDASDLEVM SVIPTKIPKL REAATRERRH LCLQLAAPTG TTVSCLSYIS RTNQLAVGYS
DGYFSLWNMK TLRRDYHVQI EGGRVPVCAV AFQEPENDPR NCCYLWAVQS SESGGDVSLH
LLQLAFSDRK CLASGQIMYE LLEYCEERYS LDLSGSTLSL RGQSNNTKLL GCQTIEKFRV
HGEREDGVHE VTSPDTSVSV FSWQVNTYGQ GKPSVYLGVF DINRWYQAQM PDSLRSGQFL
RNCSYFAFWS LEAVVNITTQ DIIFDILVHE RSLSRGIPPS YPPPEQFYYP STYNFDATCL
LNSGLIHFAC TGFQKETLHF LKKSGSSLNE AIPDGYNRCL AAGLLAPKFT DVQASSLSQE
EQLQAILAAA VETSSLGLLT SCIKRWTAEE QPRSAANLRF VLEWTWKKVT LTKQEFDRLC
FRLFDGSCNF IDPHTLQSLQ QCHLYFSNLT AVLNCFIAQA KEVTQQGAVD LTNKQSVTRL
LTLYASVVLW FCRSGMLPDS SDETVQLTRP FYNYQVIQQY YSDQRKKLER LARGKWDTSS
LMIDGLINQF GDRIQQLWSR DDNGTGKYPP ANLHALLDVY LLENADEMSK HAITIYFLLD
IMYSFPDKPD SSIESFPTAF FVPGSLIKLI QGFWLLDHND YQNSVDCILN PASSRVMSWQ
HSQIIENLLC HGDSRQALRY LQVMKPVATT SKEVKLHMTV LLANRSILEA WNLQRLHSSR
LNVEELLKHM YEMCQEMGLI EELLKLTFTD FEQGYLHKFL QTTGVQNQEL LLVHHLQRAN
YISALQLNQS LKTNHLNDCD RRLRERSGAR NAILDQYGKI LPRVQRTLAS ERAKPYSLPS
LVWREVARPK PLSTTAKQAA PGSIITKANF ICNVLSKIKE VSTANEKREE YSPYQSMVSE
EPTAPPLQDI DVPDAFFGTP INKSRRVSRL LDSVVHPVLM EPTPLTSSDT DNNQTPHKSP
LLKTSSPLHS SLRRIAHMRS FAKASEFSLL ETPLVVRKAK ALAANTASSG YTSITPQSIL
RSSVRTTPLV SPSVSPGRSL TPPLRPKETK ISFMELSFTR HAKAAHSSEG NLLAISPVLR
SSPDAVWSVK GKVASFTQNT PVKKLDEIDA SSSGIQEESQ DEMEVSKEIS NISVRSEQAS
LEYHDAPTPE DLENDEISGT TNSQPQVNEV HHQMEDGQLT EKPAELALTE MQEEFIDSEE
REIEYISAPL NGPNALECMT AVPDIYLEDA SQCILETPEG SSVSVTGEQE CVSSAKDSES
VISIHDSDDA HSNLSENDQD SEEIEENNLR VPTTVTRCEE FDLIETKDLE VELEEADSEK
TNYKDIYPDA TVQLGFTVES IEQRYTCELA DRRETPSETD EIEGEHFETE NNFSLVLEGD
VTEEEILEPS SSKTDLELTR PPIAHQKLIS ENRENIENCE TTEKIPANMS PLVDSDHESK
TLETLPSEAD LSVAEKVLKG TEEKDVPPEV HSEVVLESKL VGNAMMSLDS SESQEVIISQ
YDNVISIEKL EMTQEKMYGE KTEQINEGQV SPNRDQSTLV KPLTPRRSIR KSSKPADSST
DIIGNITLPT TPKRGLKKAK ENVDTLKNSI SVVPEEELTL GTRRITRKAT LTALDNPEPL
QIKEPPSGED LQVQPSTPTR GRRGKVITSD DLKEPPSGED LQVQPSTPTR GRRGRVITSD
DLREPPPGED LQVQPSTPTR GRRGRVITSD DIKESPSVED LQVQPSTPTR GRRGKVITSD
DIKEPPSVED LQVQPSTPTR GRKGKVITSD DIKEPLSGED LQVQPSTPTR GRKGKVITSD
DIKEPLSEEV LQEQPSTPTR GRRGRVITSD GKGYECVEEK NALPLTPTRI TRSKNILEPE
KGISQIEPEK GISQIEPDKG LSQIEDTGET EHEVVTPRRG RRGKRVVNEL VKHFERNSSQ
PNIKADTSPP VSPKKVSLRW TRTRSENQRI NATEEQASKI QEDLSDTPRK RYKKSSNKMG
FEETTDTVTE GAIVEDVQES LIISHLGKNP NTSIVRSARK TALPPVTEDH SEQPLLPPES
HSKVHSSLAI ADEENKTNTR TRSGNKSSVD VSAITFEFST PKARTKKTAK GSAVPTELIP
STQYVFSPPS TRTRRATRAN VSEAVIEPQL QFQESCEIAE TEVPEVPASK PRGRPPKHKA
KAVTRVLKKP SWSTPPVEIK LISPPESPAV SETNTKTDST EAKGAEKISV RRTRRRIIAK
PVTRRKMR
