NU214_CAEEL
ID NU214_CAEEL Reviewed; 1390 AA.
AC Q17602;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nuclear pore complex protein 14 {ECO:0000312|WormBase:C03D6.4};
DE AltName: Full=Nuclear pore complex protein Nup214 {ECO:0000305};
DE AltName: Full=Nucleoporin npp-14 {ECO:0000305};
GN Name=npp-14 {ECO:0000312|WormBase:C03D6.4};
GN ORFNames=C03D6.4 {ECO:0000312|WormBase:C03D6.4};
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 DISRUPTION PHENOTYPE.
RX PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA Galy V., Mattaj I.W., Askjaer P.;
RT "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT of nuclear pore complex size exclusion in vivo.";
RL Mol. Biol. Cell 14:5104-5115(2003).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CED-3, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27723735; DOI=10.1038/nsmb.3308;
RA Chen X., Wang Y., Chen Y.Z., Harry B.L., Nakagawa A., Lee E.S., Guo H.,
RA Xue D.;
RT "Regulation of CED-3 caspase localization and activation by C. elegans
RT nuclear-membrane protein NPP-14.";
RL Nat. Struct. Mol. Biol. 23:958-964(2016).
CC -!- FUNCTION: May serve as a docking site in the receptor-mediated import
CC of substrates across the nuclear pore complex (By similarity). Plays a
CC role in apoptosis by tethering caspase ced-3 to the nuclear membrane
CC preventing its autoprocessing in absence of ced-4.
CC {ECO:0000250|UniProtKB:P35658, ECO:0000269|PubMed:27723735}.
CC -!- SUBUNIT: Interacts with caspase ced-3 (via propeptide); the interaction
CC tethers ced-3 to the nuclear membrane and prevents its autoprocessing
CC in absence of ced-4. {ECO:0000269|PubMed:27723735}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P35658}. Nucleus membrane
CC {ECO:0000269|PubMed:27723735}; Peripheral membrane protein
CC {ECO:0000305|PubMed:27723735}. Note=Cytoplasmic side of the nuclear
CC pore complex (By similarity). Co-localizes with caspase ced-3 to the
CC perinuclear region in germ cells. {ECO:0000250|UniProtKB:P35658,
CC ECO:0000269|PubMed:27723735}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no visible
CC phenotype (PubMed:12937276). Simultaneous knockdown of npp-2 results in
CC embryonic lethality (PubMed:12937276). RNAi-mediated knockdown in a
CC ced-1 (e1735) and ced-3 (n718) double mutant background partially
CC restores embryonic cell apoptosis (PubMed:27723735).
CC {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:27723735}.
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; BX284601; CAA99763.1; -; Genomic_DNA.
DR PIR; T18883; T18883.
DR RefSeq; NP_492568.1; NM_060167.6.
DR AlphaFoldDB; Q17602; -.
DR SMR; Q17602; -.
DR STRING; 6239.C03D6.4; -.
DR EPD; Q17602; -.
DR PaxDb; Q17602; -.
DR PeptideAtlas; Q17602; -.
DR EnsemblMetazoa; C03D6.4.1; C03D6.4.1; WBGene00003800.
DR GeneID; 172813; -.
DR KEGG; cel:CELE_C03D6.4; -.
DR UCSC; C03D6.4; c. elegans.
DR CTD; 172813; -.
DR WormBase; C03D6.4; CE05198; WBGene00003800; npp-14.
DR eggNOG; KOG3630; Eukaryota.
DR GeneTree; ENSGT00940000165854; -.
DR HOGENOM; CLU_253002_0_0_1; -.
DR InParanoid; Q17602; -.
DR OMA; WLSTFQF; -.
DR OrthoDB; 302566at2759; -.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-191859; snRNP Assembly.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q17602; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003800; Expressed in adult organism and 4 other tissues.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR23193; PTHR23193; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1390
FT /note="Nuclear pore complex protein 14"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440164"
FT REPEAT 1073..1074
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 1091..1092
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 1111..1112
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 1122..1123
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 1125..1126
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 1163..1164
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 1166..1167
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 1178..1179
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1244..1245
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1283..1284
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1289..1290
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1295..1296
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1300..1301
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1315..1316
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1344..1345
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1357..1358
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1372..1373
FT /note="17"
FT /evidence="ECO:0000305"
FT REGION 434..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1373
FT /note="17 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1183..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 147968 MW; 2FD1DB4D3B7E43D3 CRC64;
MSNEDVAEDV SQVTDFHFHT CRKFRLFSSK SDGYSQNEIN IRNRVATSSQ LGVTFVTVNS
NQLSCFHTKS LLGYKITREN MNVEVTDLPI KTIRLHGVVL INDMGVNSDG TVLGVLHTKN
NDVSVDVFDI KKICTSSSIE PFKPLCTTRV GTEQINQGSC LEWNPAFPDT FAASSTDRSI
LVAKINVQSP ANQKLVGIGK FGAVTTAISW SPKGKQLTIG DSLGKIVQLK PELEVVRSQH
GPENKPNYGR ITGLCWLATT EWLVSLENGT DQDAYLMRCK KDKPTEWIQF HELSYSSSKW
PLPPQLFPAT QLLVDWNVVI VGNSKTSEIS TVGKRDDWQT WVPVEGESIY LPTTSSGKDT
VPIGVAVDRS MTDEVLLNPD GSQRHRPSPL VLCLTNDGIL TAHHIISTFA AHIPCQMSSQ
NLAINDLKKL QFDSQKPISA PPSDQTPVTK PSTVFGQKPE AETLKSSLVG SPSSVQTPKP
SSSLFNPKSI ASNIETSQLT ESKPSTPAAP SSQPKIASTP KSEAIPKISD KTLEHKKAEL
IATKKQVLIE RMDKINDSMA GAKDATMKLS FAVGKVKTTI MECADVVRAS LGDSKEVMDE
LKNLILSIER MSDRTQHTVK EMDFEIDEKM ELVAGVEDGN QVLEKLRNMS ETEKLMRFNK
LETAADLLNG KYEECSDLIK KLRMSLSEKE SLRKQAILSP LRLSSNLNQL RSGSETELAL
KVMRNVSKII MDTREQIQRT ELEFVRFQRD VKFQNFKKGK ENLNFTQPLE MSSLDGDAPQ
GKSLTDAESI KVRQALVNQI QKRGIVKTRN VIVESYKKSE NSAAMKNDLL DTSNLSNAIL
KLSMTPRRVM PSSSLFSASP STPSTKSDAA TQADEPPIVK TVVVTVESPA KPIASAPAVS
SPLIKLNTTT ATTTMTTPKV TVPKEEANKT QDQKPIISTP ASSSIFSSGS LFGTKTQTPL
VSKEESTLTT GVPSLINSSL SISPQEIEKA SSKVETLNKT EEVKDEKSEN EVTPDLKSEE
PKSLETKVKE EPKPAVQTPV KEEETGSNIQ KTPSFSFNST TTPKSTSSTS SIFGGGLKTQ
TPSSSNSTNI FGARTTTTAT PTPASNTSSI FGGGSKAASS PFGSFGQAGC QPAKTSNPAT
STASVTFSFN TGATSASAKP AGFGSFGAGA SAKPSSVFGG SVTAPTVPNV DDGMEDDSMA
NGGGSGGFMS GLGNARTSNT SGGNNPFAPK TSTGTSASSS SWLFGGGGNQ QQQQQQKPSF
SFNTAGSSAQ QASAPATGTS SVFGGAPKFG SQPAFGAKPF GGGANAGLSK NASIFGGATS
STTNNPATGG FAQFASGQKT SSLFGGGATP QTNTSIFGGG ANTTPAPTSS VFGGGASANA
NKPTSFTSWR
