NDC1_YEAST
ID NDC1_YEAST Reviewed; 655 AA.
AC P32500; D6VZE3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Nucleoporin NDC1;
DE AltName: Full=Nuclear division cycle protein 1;
DE AltName: Full=Nuclear pore protein NDC1;
GN Name=NDC1; OrderedLocusNames=YML031W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8349727; DOI=10.1083/jcb.122.4.743;
RA Winey M., Hoyt M.A., Chan C., Goetsch L., Botstein D., Byers B.;
RT "NDC1: a nuclear periphery component required for yeast spindle pole body
RT duplication.";
RL J. Cell Biol. 122:743-751(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND ROLE IN NPC AND SPB.
RX PubMed=9864355; DOI=10.1083/jcb.143.7.1789;
RA Chial H.J., Rout M.P., Giddings T.H. Jr., Winey M.;
RT "Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore
RT complexes and spindle pole bodies.";
RL J. Cell Biol. 143:1789-1800(1998).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [6]
RP INTERACTION.
RX PubMed=10688190; DOI=10.1038/35001009;
RA Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R.,
RA Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A.,
RA Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M.,
RA Johnston M., Fields S., Rothberg J.M.;
RT "A comprehensive analysis of protein-protein interactions in Saccharomyces
RT cerevisiae.";
RL Nature 403:623-627(2000).
RN [7]
RP FUNCTION, AND DE NOVO NPC ASSEMBLY.
RX PubMed=11352933; DOI=10.1083/jcb.153.4.709;
RA Marelli M., Lusk C.P., Chan H., Aitchison J.D., Wozniak R.W.;
RT "A link between the synthesis of nucleoporins and the biogenesis of the
RT nuclear envelope.";
RL J. Cell Biol. 153:709-724(2001).
RN [8]
RP INTERACTION.
RX PubMed=11283351; DOI=10.1073/pnas.061034498;
RA Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT "A comprehensive two-hybrid analysis to explore the yeast protein
RT interactome.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN [9]
RP REVIEW.
RX PubMed=11935220; DOI=10.1007/s00294-001-0263-x;
RA Helfant A.H.;
RT "Composition of the spindle pole body of Saccharomyces cerevisiae and the
RT proteins involved in its duplication.";
RL Curr. Genet. 40:291-310(2002).
RN [10]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION, AND NPC AND SPB ASSEMBLY.
RX PubMed=15075274; DOI=10.1128/ec.3.2.447-458.2004;
RA Lau C.K., Giddings T.H. Jr., Winey M.;
RT "A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role
RT for the spindle pole body component Ndc1p in nuclear pore assembly.";
RL Eukaryot. Cell 3:447-458(2004).
RN [13]
RP INTERACTION WITH NBP1.
RX PubMed=16436507; DOI=10.1091/mbc.e05-07-0668;
RA Araki Y., Lau C.K., Maekawa H., Jaspersen S.L., Giddings T.H. Jr.,
RA Schiebel E., Winey M.;
RT "The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is
RT required for SPB membrane insertion and interacts with the integral
RT membrane proteins Ndc1p and Mps2p.";
RL Mol. Biol. Cell 17:1959-1970(2006).
RN [14]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 In SPB duplication NDC1 is required for the insertion of the
CC cytoplasmic side of the SPB in the nuclear envelope, thus allowing for
CC the assembly of the nucleoplasmic SPB side. NPC components,
CC collectively referred to as nucleoporins (NUPs), can play the role of
CC both NPC structural components and of docking or interaction partners
CC for transiently associated nuclear transport factors.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11352933,
CC ECO:0000269|PubMed:15075274, ECO:0000269|PubMed:9864355}.
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 NDC1 may form a subcomplex with ASM4 and NUP53 at the NPC. Interactions
CC at the SPB have not been determined. {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC P32500; Q05166: ASM4; NbExp=4; IntAct=EBI-11950, EBI-3035;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane
CC protein. Cytoplasm, cytoskeleton, microtubule organizing center,
CC spindle pole body. Note=Central core structure of the nuclear pore
CC complex. Spindle pole body, central plaque.
CC -!- MISCELLANEOUS: Present with 3030 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NDC1 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; X70281; CAA49767.1; -; Genomic_DNA.
DR EMBL; Z46659; CAA86624.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09867.1; -; Genomic_DNA.
DR PIR; A40675; A40675.
DR RefSeq; NP_013681.1; NM_001182389.1.
DR AlphaFoldDB; P32500; -.
DR BioGRID; 35138; 69.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-1465N; -.
DR IntAct; P32500; 22.
DR MINT; P32500; -.
DR STRING; 4932.YML031W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P32500; -.
DR MaxQB; P32500; -.
DR PaxDb; P32500; -.
DR PRIDE; P32500; -.
DR EnsemblFungi; YML031W_mRNA; YML031W; YML031W.
DR GeneID; 854977; -.
DR KEGG; sce:YML031W; -.
DR SGD; S000004493; NDC1.
DR VEuPathDB; FungiDB:YML031W; -.
DR eggNOG; ENOG502RZSR; Eukaryota.
DR HOGENOM; CLU_028040_0_0_1; -.
DR InParanoid; P32500; -.
DR OMA; CLHKGKP; -.
DR BioCyc; YEAST:G3O-32632-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR PRO; PR:P32500; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32500; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0106166; F:spindle pole body-nuclear membrane anchor activity; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IGI:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR GO; GO:0070631; P:spindle pole body localization; IBA:GO_Central.
DR InterPro; IPR019049; Nucleoporin_prot_Ndc1/Nup.
DR PANTHER; PTHR13269; PTHR13269; 1.
DR Pfam; PF09531; Ndc1_Nup; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..655
FT /note="Nucleoporin NDC1"
FT /id="PRO_0000204862"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..58
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 89..108
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 110..130
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..224
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 655 AA; 74134 MW; 43C34B253D979EC6 CRC64;
MIQTPRELLN PRYTYHTIFS DVCKTRFNHL VTRLFFICSI IQTVVISLLA LPHSPLWELA
LAFIPNILAL NLVSLLIIVT RKNYMHVKNF GFANSLTFIL GQLLSVKFLV YQGVYSMGSI
LLSFVLGVVF GRGGSGWKPY YKLFIWLVVP TIYNLQHHVT DADKLSFNCE NFFQAPQDYV
LERVKRIMEK SVILSVISMF VLPIFTTVFF SRQKSGLFDS FTNGVLAVTN LLIISCIIFI
TFEFINIAFD AHMSIGCLHK GKLISNLSST PMETLLSGLS ADKPFTRLTA YQELAYRATS
LDPSLRAPIY HSKFRSSSGN TWSLILNECL KTIQINNEKV VQYLRSVQDL GGSATARHKK
KVENLDYMYE NGKLTSANER LFGNRPSMMA PLRDNGLLDE SPNRLRVRTD DSVLLNRGNK
KRHRSSYYDN DLDETTQTFN GSIFTHETTF MTAMRLMLKK LKNSIMSFIF PSYAERQSSD
ESDNYRLLPN GSNKAQISII DIWSISKKRQ AEKLVPLPIC HANSVVALTG LLIRSKTEDP
KGGIIASVGD ILKTLERSIC ALGEFADWDP ESMAYTAFQT QRTAQDRVQQ DSEDEDSMKD
TTDMISVLYQ LSTSAFMEIV LEYNVALNDV YLDADVAKLA NWFLEVYASG NPNAT
