NDC1_SCHPO
ID NDC1_SCHPO Reviewed; 601 AA.
AC O13961; Q9UTH4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nuclear envelope protein ndc1;
DE AltName: Full=Cell untimely torn protein 11;
GN Name=cut11; Synonyms=ndc1; ORFNames=SPAC1786.03, SPAC24C9.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9763447; DOI=10.1091/mbc.9.10.2839;
RA West R.R., Vaisberg E.V., Ding R., Nurse P., McIntosh J.R.;
RT "cut11(+): a gene required for cell cycle-dependent spindle pole body
RT anchoring in the nuclear envelope and bipolar spindle formation in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 9:2839-2855(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11927555; DOI=10.1093/emboj/21.7.1713;
RA Krien M.J.E., West R.R., John U.P., Koniaras K., McIntosh J.R.,
RA O'Connell M.J.;
RT "The fission yeast NIMA kinase Fin1p is required for spindle function and
RT nuclear envelope integrity.";
RL EMBO J. 21:1713-1722(2002).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC) and the spindle
CC pole body (SPB), which plays a key role in de novo assembly and
CC insertion of both structures in the nuclear envelope. Involved in the
CC formation of the bipolar mitotic spindle. Anchors the spindle pole body
CC in the nuclear envelope. {ECO:0000269|PubMed:9763447}.
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane;
CC Multi-pass membrane protein. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body. Note=Central core structure of
CC the nuclear pore complex.
CC -!- SIMILARITY: Belongs to the NDC1 family. {ECO:0000305}.
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DR EMBL; AF079307; AAC31554.1; -; mRNA.
DR EMBL; CU329670; CAB57434.1; -; Genomic_DNA.
DR PIR; T47249; T47249.
DR RefSeq; NP_594025.2; NM_001019450.2.
DR AlphaFoldDB; O13961; -.
DR BioGRID; 278637; 365.
DR IntAct; O13961; 2.
DR MINT; O13961; -.
DR STRING; 4896.SPAC1786.03.1; -.
DR iPTMnet; O13961; -.
DR MaxQB; O13961; -.
DR PaxDb; O13961; -.
DR PRIDE; O13961; -.
DR EnsemblFungi; SPAC1786.03.1; SPAC1786.03.1:pep; SPAC1786.03.
DR GeneID; 2542161; -.
DR KEGG; spo:SPAC1786.03; -.
DR PomBase; SPAC1786.03; cut11.
DR VEuPathDB; FungiDB:SPAC1786.03; -.
DR eggNOG; ENOG502S1MG; Eukaryota.
DR HOGENOM; CLU_457203_0_0_1; -.
DR InParanoid; O13961; -.
DR OMA; FAKLFWN; -.
DR PhylomeDB; O13961; -.
DR Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:O13961; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140512; C:mitotic nuclear bridge midzone; IDA:PomBase.
DR GO; GO:0140599; C:mitotic nuclear bridge midzone membrane domain; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0106166; F:spindle pole body-nuclear membrane anchor activity; IDA:PomBase.
DR GO; GO:1903087; P:mitotic spindle pole body duplication; IMP:PomBase.
DR GO; GO:0140480; P:mitotic spindle pole body insertion into the nuclear envelope; IMP:PomBase.
DR GO; GO:1990608; P:mitotic spindle pole body localization; IMP:PomBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..601
FT /note="Nuclear envelope protein ndc1"
FT /id="PRO_0000079566"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..58
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..153
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..256
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 601 AA; 69355 MW; 15B1C8EA34D713D9 CRC64;
MVMLRTSFPS GSRTKAVRYH TLLRPILQQR FLRACFALLC LCCITSYWFS SGPFISLSFW
FLSLVRGFVC FFFMFPYFVM LKSRMSTQKV TKQSLGAQLF YDFSPKSFFL VYLTFAVSVS
CLCLFYIKGH ASSIRLQWIA SPNAYELPSL NERFVYMTYF SHILILALTV EHLYLQRDSP
SRPVINVSFF NYIFQNLGWL IRFSFRKSII CCLFTPFSYA ILRSYIWRFA ALLTSCCRRI
AYTKTPPKWP LSLRLLLHSF WMAFIVCLTF QIALLIFRVF LYSGPMIRGK LLSARSNDPN
GTLVDGMKTK KKPLTECIAT EELWFIAKRD PQRIKSIFQD IDRSVSIWQE LYSITESRCK
ELATSLKILQ STGDFSAATS KKSGLTKKTN IPYSPNSNHE EINSIPLRNK NIFVPPSQGH
SPLLEKIKKQ GSLPSTTPVN EGGISDIIPK SLYDQVIRFI STFYKAPVFG IFRKTLRRQN
EALLPNPWLF CVTVNSLTQL VLKSLKYDTY GVVARDISSI LAVYCDTFDV LVSYKRSLVK
NHSNSTNLDD DFKNLNSAAN ALHCGIIDIT EKFQDFFTQL NLSPRIERRC WVLFREYKSN
S
