NDC1_CHATD
ID NDC1_CHATD Reviewed; 646 AA.
AC G0S235; G0ZGV7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Nucleoporin NDC1 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein NDC1;
GN Name=NDC1; ORFNames=CTHT_0015840;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the spindle pole body (SPB), probably by playing a key role in de
CC novo assembly and insertion of both structures in the nuclear envelope.
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. {ECO:0000250|UniProtKB:P32500}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:P32500, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P32500}. Nucleus membrane; Multi-pass membrane
CC protein {ECO:0000255}. Note=Central core structure of the nuclear pore
CC complex. {ECO:0000250|UniProtKB:P32500}.
CC -!- SIMILARITY: Belongs to the NDC1 family. {ECO:0000305}.
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DR EMBL; GL988039; EGS23095.1; -; Genomic_DNA.
DR EMBL; JF276302; AEL00695.1; -; Genomic_DNA.
DR RefSeq; XP_006692087.1; XM_006692024.1.
DR AlphaFoldDB; G0S235; -.
DR STRING; 759272.G0S235; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS23095; EGS23095; CTHT_0015840.
DR GeneID; 18255622; -.
DR KEGG; cthr:CTHT_0015840; -.
DR eggNOG; ENOG502S1MG; Eukaryota.
DR HOGENOM; CLU_029386_1_0_1; -.
DR OrthoDB; 556184at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR019049; Nucleoporin_prot_Ndc1/Nup.
DR PANTHER; PTHR13269; PTHR13269; 1.
DR Pfam; PF09531; Ndc1_Nup; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Nucleoporin NDC1"
FT /id="PRO_0000433181"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..52
FT /note="Perinuclear space"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..144
FT /note="Perinuclear space"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..271
FT /note="Perinuclear space"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P32500"
FT REGION 380..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 542..602
FT /evidence="ECO:0000255"
FT COMPBIAS 380..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 71820 MW; 5920053EFF185884 CRC64;
MAAAVRRSPY KDFLQPALQR RFATATLVVL ATAYFEALLL ARWSSWLWSW FPLGPTGFRA
ALFFLCGIFV IILRISQYHP GIRTSDSPIA TLVRYAPRWT TFETLFTYAL SAWIFSLVYL
GTVPDDAGFE RITYFTYDRA RLNEKPIFLT THLVLLGIYQ GVRHLYSDID RLSLGTAQPS
NGDSSKATGE DGHVSTQMRR FRDQLPKIVV HSLHQSVMGL LLSASLYPLL LRDLLWRVNM
TMLRPLYSLP RTNVPPANLP YSPSTLLRCL AASVMVMFAW TAANTAFSLL LVKSPLKNGK
PLTADAKDPN GSLLNGLKNK KLSIKCFAMW ELAYIARDFP DRRKAIFEDM DRKDGPMWSQ
VYKICLDTLH TLSSNIDAYT APPAPATTPQ QAETALGDKP RTSAPPKEDH IFAPLPSNKS
AFRTSVSSAF QNAALAGPGG PPASLSPVAK RTLHAARSRL LEAAAPNAEI EVTPSSFFRE
LALKYVLSSP LAGYPFRQTR RRRLASAVLG SPYGEPSLYV NAASAVSGLA VSSLREDRYG
HVQRDVASLI RELTSLGEKL NAFVNEGGMG KHWTDVVELE GEDKCEEVEE VVNAVKHALK
RVIVAFEPYA RDLRLTRGEV KKAREVAGLE QEVEVREVMP EMVQIR
