MEL28_CAEEL
ID MEL28_CAEEL Reviewed; 1784 AA.
AC Q18508;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein mel-28 {ECO:0000305};
DE AltName: Full=Maternal effect lethal protein 28 {ECO:0000305};
GN Name=mel-28 {ECO:0000312|WormBase:C38D4.3};
GN ORFNames=C38D4.3 {ECO:0000312|WormBase:C38D4.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16950114; DOI=10.1016/j.cub.2006.06.067;
RA Galy V., Askjaer P., Franz C., Lopez-Iglesias C., Mattaj I.W.;
RT "MEL-28, a novel nuclear-envelope and kinetochore protein essential for
RT zygotic nuclear-envelope assembly in C. elegans.";
RL Curr. Biol. 16:1748-1756(2006).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16950115; DOI=10.1016/j.cub.2006.07.071;
RA Fernandez A.G., Piano F.;
RT "MEL-28 is downstream of the Ran cycle and is required for nuclear-envelope
RT function and chromatin maintenance.";
RL Curr. Biol. 16:1757-1763(2006).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26166571; DOI=10.1016/j.celrep.2015.06.046;
RA Sonneville R., Craig G., Labib K., Gartner A., Blow J.J.;
RT "Both chromosome decondensation and condensation are dependent on DNA
RT replication in C. elegans embryos.";
RL Cell Rep. 12:405-417(2015).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 409-ASP--PRO-417.
RX PubMed=27341616; DOI=10.1371/journal.pgen.1006131;
RA Gomez-Saldivar G., Fernandez A., Hirano Y., Mauro M., Lai A., Ayuso C.,
RA Haraguchi T., Hiraoka Y., Piano F., Askjaer P.;
RT "Identification of conserved MEL-28/ELYS domains with essential roles in
RT nuclear assembly and chromosome segregation.";
RL PLoS Genet. 12:E1006131-E1006131(2016).
CC -!- FUNCTION: Nuclear envelope protein which has essential roles in
CC assembly of nuclear pore complexes and in chromatin maintenance during
CC the cell cycle (PubMed:16950114, PubMed:16950115, PubMed:26166571,
CC PubMed:27341616). Appears to be a stable structural component of the
CC nuclear envelope during interphase (PubMed:16950114, PubMed:16950115).
CC In dividing cells, localizes to kinetochores during early stages of
CC mitosis and then to chromatin during late mitosis (PubMed:16950114,
CC PubMed:27341616). Important for several mitotic processes including
CC chromosome condensation, kinetochore assembly, chromosome segregation
CC and cell-cycle timing (PubMed:16950114, PubMed:16950115,
CC PubMed:26166571, PubMed:27341616). In postmitotic cells, plays a role
CC in the early steps of nuclear pore complex assembly by recruiting the
CC nucleoporins npp-10 and npp-5 to chromatin (PubMed:16950114,
CC PubMed:16950115). Also involved in meiotic chromosome segregation
CC (PubMed:27341616). May function downstream of the Ran GTPase signaling
CC pathway (PubMed:16950115). {ECO:0000269|PubMed:16950114,
CC ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:26166571,
CC ECO:0000269|PubMed:27341616}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16950114,
CC ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:27341616}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:27341616}. Nucleus envelope
CC {ECO:0000269|PubMed:27341616}. Nucleus inner membrane
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:16950114}. Chromosome
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115,
CC ECO:0000269|PubMed:27341616}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115,
CC ECO:0000269|PubMed:27341616}. Note=Has a dynamic expression pattern
CC during the cell cycle (PubMed:16950114, PubMed:27341616). During
CC interphase, localizes to nuclear pore complexes and is also found in
CC the nucleoplasm (PubMed:16950114, PubMed:27341616). During early
CC mitosis, localizes to kinetochores in a hcp-3/CENP-A and hcp-4/CENP-C
CC dependent manner (PubMed:16950114, PubMed:16950115, PubMed:27341616).
CC At later stages of mitosis (anaphase), widely distributed on chromatin
CC (PubMed:16950114, PubMed:27341616). During telophase, localizes again
CC to the reforming nuclear envelope (PubMed:16950114, PubMed:27341616).
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115,
CC ECO:0000269|PubMed:27341616}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:16950114}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development.
CC {ECO:0000269|PubMed:27341616}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality (PubMed:16950114). Impairs assembly of the nuclear pore
CC complex, the integrity of the nuclear envelope and distribution of the
CC integral nuclear envelope proteins lmn-1, lem-2 and emr-1 and the
CC nuclear pore complex proteins npp-9, npp-10 and npp-1 (PubMed:16950114,
CC PubMed:16950115). Reduces the recruitment of npp-10 and npp-5 to
CC chromatin (PubMed:16950114). Leads to hypercondensation and
CC mispositioning of chromatin, defects in migration and positioning of
CC the pronuclei, dissociation of centrosomes from chromatin, precocious
CC centrosome separation, as well as defects in kinetochore assembly,
CC spindle assembly, chromosome segregation and chromatin distribution in
CC meiosis and mitosis (PubMed:16950114, PubMed:16950115). Impairs mitotic
CC progression and leads to chromatin bridges (PubMed:16950114,
CC PubMed:16950115). Reduces knl-3 localization to the kinetochores
CC (PubMed:16950115). Suppresses the chromosome-decondensation defect in
CC evl-18/cdc-45 mutant embryos (PubMed:26166571).
CC {ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115,
CC ECO:0000269|PubMed:26166571}.
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DR EMBL; BX284603; CAA86316.2; -; Genomic_DNA.
DR PIR; T19823; T19823.
DR RefSeq; NP_497987.2; NM_065586.6.
DR AlphaFoldDB; Q18508; -.
DR IntAct; Q18508; 4.
DR STRING; 6239.C38D4.3; -.
DR EPD; Q18508; -.
DR PaxDb; Q18508; -.
DR PeptideAtlas; Q18508; -.
DR PRIDE; Q18508; -.
DR EnsemblMetazoa; C38D4.3.1; C38D4.3.1; WBGene00003210.
DR GeneID; 175634; -.
DR KEGG; cel:CELE_C38D4.3; -.
DR UCSC; C38D4.3; c. elegans.
DR CTD; 175634; -.
DR WormBase; C38D4.3; CE36378; WBGene00003210; mel-28.
DR eggNOG; ENOG502TKKA; Eukaryota.
DR HOGENOM; CLU_001014_0_0_1; -.
DR InParanoid; Q18508; -.
DR OMA; CMRNHTK; -.
DR OrthoDB; 1040332at2759; -.
DR PRO; PR:Q18508; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003210; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding;
KW Kinetochore; Meiosis; Membrane; Mitosis; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..1784
FT /note="Protein mel-28"
FT /id="PRO_0000439084"
FT DNA_BIND 1630..1642
FT /note="A.T hook 1"
FT /evidence="ECO:0000305"
FT DNA_BIND 1746..1758
FT /note="A.T hook 2"
FT /evidence="ECO:0000305"
FT REGION 1..956
FT /note="Required for nuclear envelope and kinetochore
FT localization"
FT /evidence="ECO:0000269|PubMed:27341616"
FT REGION 566..778
FT /note="Required for association with mitotic chromosomes"
FT /evidence="ECO:0000269|PubMed:27341616"
FT REGION 846..1071
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000269|PubMed:27341616"
FT REGION 945..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1601
FT /note="Chromatin binding"
FT /evidence="ECO:0000269|PubMed:27341616"
FT REGION 1601..1784
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000269|PubMed:27341616"
FT REGION 1630..1784
FT /note="Required for chromosome segregation, nuclear growth,
FT nucleoplasmic accumulation and cell cycle timing, but not
FT required for nuclear envelope and kinetochore localization"
FT /evidence="ECO:0000269|PubMed:27341616"
FT COMPBIAS 945..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1626..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 409..417
FT /note="DSWYYKRVP->SSWSYKASG: Defects in chromosome
FT segregation in meiosis and mitosis."
FT /evidence="ECO:0000269|PubMed:27341616"
SQ SEQUENCE 1784 AA; 200846 MW; 891F17E3FB674B6B CRC64;
MDNENSSIFK SYQGYECWRG EKQIILKDSI GRQLPYIVNF KKNTCQIFDI EWERVTHSFV
FPEGCALIDA DYFPTEEGKL GILVGVEDPR QSCGAEHFVL ALAVDPDSPA MTITHSLEVP
SKITVVKTLF SSADMADETQ RTVLKLYHRL MTWQHIVAIG CKETQCYLAR LVAVETPSSP
VITVHSEKKY LINLMNAYVS GSVLQYTLDD GAYREYPTAA VYISALSLMP RSRTLLVGLS
MGGILAASLN PSNQMMLLEL RHERLVRKIA PLEPEDDPDK FEYFIATVDC SPRHPIMIQL
WRGSFKTLED VDGEEKYDRP SFSVCLEHKI LFGERWLAVN PIVTERDHMM LTRKRGTEDS
MHNVSQTFGS TSNRNSVLLA YERKKMVIGT EDPNAEPEYI VEAAIFDIDS WYYKRVPGRV
STDGTVLKQC AFLSTIKSNI RSEDVNDIGI LTNEATDVSS FSSMVSDADQ LFYPSALSFE
RVFVAKNTRI DWMKIQNIQD TILNKCAVKL PALIRNPEMI SSVVMAAGLV RKNILSGSPN
SSAAEINELQ LSSDQKVLLN VIVYYGKIEE FCQLASRPDI SDTLKRELAE WALHEAVDYK
RTISDKMVSL FQGRSLALSP LAEESIAQGI KLFRVVYEYL KACSKALKDD RLRNLAHSVI
CMRNHTKLTS QFINFAIIPV DPIRQQRMKD LHSKRKNMAR KNSSSLPVQS VVRKMNRQAP
NAQFWNDIPH DEWYPPTPLD LLECLLNVSI SESIKRELVV QYVIDWISTS PEDSEHSEKQ
LALETIKIMT NQMLNVNLEK IYYILDQGKK ALTSSKTSDD MRALGEKVFS MKDDEISYEK
LWGKDAPMTV TIGKHDLQRF EQRMKMQMEG GKVRLPVLDP ESEILYQMFL FENEKFEAMS
SEAISSNKLL SAFLPGMIKK DGRGRQKTAK EQEIEISVKK MFERKVQNDD EDMPEVFASV
NDKTERKRKS SQFGEDDESS VSSSQYVPPT AKRIQQWKSA VESVANNSSI NSITSPDSHQ
NAEINMMIAT PARYYKRHNE EENVQDGFLS PAGNRPPPVS AHNSILKTAK GGQSASRGRI
RFRADVPRGA DESIEDNGRK GLALNFAILE DEEEETMTIR KSRSMGKHDE EKDSEKNVVD
EMEEVKDQEQ ENDECIESEK TFENQDDFEV LEDTSAPEAA NTENGSETPP MEDTFEVRDD
DVMPPTDETY LSHLQTDKTG ILEEEGEDED IWDGVQRSFE VQMDEDCEAV PTIDVADDLE
SKSEEVNEEE VVESEEVQQD AKEPEKTEKR QEEPEPEVMQ PVIPEEPQNE SLESSIKLQE
ELQEEPDIVP TGDEDTADKV QEQAVEEDRP PSRNTRSSSV QKSTSQVEDR DPKELVEEER
PPSRNTRSAS VQKSSNQEKT SESGEVTEED RPPSRNTRSA SVQKSSSKVK DQKPEELIEE
DRPPSRNTRS ASAQKTVAAN KSVLESEIPS RSASRRTRST SLRNDTVAEP DETSVAMTTR
RRTRATSEVV SKQSSEDDGR STPKTGRTPT KKAAASTSSS RAGSVTRGKK SIIQKMPSPL
EVTMEVQEEE EEEAEEERPA SRSTRSASVK NTTVDPSSSA LASTKRTTSR KRGNSETIDF
NQDDKSAPTT PKRGRPAKKD AGSPKVGSKA RGTKPKSIFE NQEDEEDRSS SPDIEQPATP
TRSSKRTARS RANSESIDDD SKQKTPKKKN AAVNEAGTSK QSRSVTRSRA SSIDVQQEVE
EPTTPKRGRG RPPKTVLENI EEGEEERKET AATPLLRSAR RAKQ
