NDC1_MOUSE
ID NDC1_MOUSE Reviewed; 673 AA.
AC Q8VCB1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nucleoporin NDC1;
DE AltName: Full=Transmembrane protein 48;
GN Name=Ndc1; Synonyms=Tmem48;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16702233; DOI=10.1083/jcb.200601001;
RA Stavru F., Hulsmann B.B., Spang A., Hartmann E., Cordes V.C., Gorlich D.;
RT "NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore
RT complexes.";
RL J. Cell Biol. 173:509-519(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), which plays a
CC key role in de novo assembly and insertion of NPC in the nuclear
CC envelope. Required for NPC and nuclear envelope assembly, possibly by
CC forming a link between the nuclear envelope membrane and soluble
CC nucleoporins, thereby anchoring the NPC in the membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the NUP35/NUP53.
CC {ECO:0000250|UniProtKB:Q6AXN4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}.
CC Nucleus membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Central core structure of the nuclear pore complex.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDC1 family. {ECO:0000305}.
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DR EMBL; DQ141695; AAZ73086.1; -; mRNA.
DR EMBL; AK144734; BAE26039.1; -; mRNA.
DR EMBL; BC021337; AAH21337.1; -; mRNA.
DR CCDS; CCDS18438.1; -.
DR RefSeq; NP_082631.1; NM_028355.3.
DR AlphaFoldDB; Q8VCB1; -.
DR SMR; Q8VCB1; -.
DR BioGRID; 215568; 5.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8VCB1; 1.
DR STRING; 10090.ENSMUSP00000120365; -.
DR iPTMnet; Q8VCB1; -.
DR PhosphoSitePlus; Q8VCB1; -.
DR EPD; Q8VCB1; -.
DR MaxQB; Q8VCB1; -.
DR PaxDb; Q8VCB1; -.
DR PeptideAtlas; Q8VCB1; -.
DR PRIDE; Q8VCB1; -.
DR ProteomicsDB; 293532; -.
DR Antibodypedia; 33093; 71 antibodies from 17 providers.
DR Ensembl; ENSMUST00000139560; ENSMUSP00000120365; ENSMUSG00000028614.
DR GeneID; 72787; -.
DR KEGG; mmu:72787; -.
DR UCSC; uc008tzt.1; mouse.
DR CTD; 55706; -.
DR MGI; MGI:1920037; Ndc1.
DR VEuPathDB; HostDB:ENSMUSG00000028614; -.
DR eggNOG; KOG4358; Eukaryota.
DR GeneTree; ENSGT00390000014590; -.
DR HOGENOM; CLU_027343_0_0_1; -.
DR InParanoid; Q8VCB1; -.
DR OMA; MIYSWIQ; -.
DR OrthoDB; 556184at2759; -.
DR PhylomeDB; Q8VCB1; -.
DR TreeFam; TF324843; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 72787; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Ndc1; mouse.
DR PRO; PR:Q8VCB1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VCB1; protein.
DR Bgee; ENSMUSG00000028614; Expressed in embryonic post-anal tail and 235 other tissues.
DR ExpressionAtlas; Q8VCB1; baseline and differential.
DR Genevisible; Q8VCB1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IDA:MGI.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISO:MGI.
DR GO; GO:0051664; P:nuclear pore localization; ISO:MGI.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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 Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..673
FT /note="Nucleoporin NDC1"
FT /id="PRO_0000235241"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..71
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..166
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..261
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
SQ SEQUENCE 673 AA; 75409 MW; 0957ED1C3C4DB6B7 CRC64;
MATAASGPCA GGSPRDILWR VLGWRIVTSI VWSVVLLPVC ITAFIVLSSI NLFHPIQWLS
DSCNDFYSSQ VIFHLLLLAV VIIIISIFNV EFYTVVPSIS GSRLALIARI LHPQQLTHSF
IHAAMGMAVA WCAAIMTKGQ YSSLVVPCTG TESLDSPAAQ TCLNEYHLFF LLSGAFMGYS
YSLLYFINNM NYLPFPIIQQ YKFLRFRRSL LLLVKHSCVE SLFMVRNFCI VYYFFGHIPK
AWISTALDLH TDEQAHRPLD TIGGLLNVSL LYHVWLCGVF LLVTWYSSWI LFKIYATEAH
VFPVQPPFAE ASDECLPKVL NSNPPRIVKY LALQDLMLLS QYSPSRRQEV FSLSQPGGHP
HNWTAISREC LNLLNDMTQK LVLYQEAAAT NGRMYSSYSV EPKKLSSAEE TAFQTPKPSQ
TPSVPPLVKT SLFSPKLSTP NVSSPFGTPF GSSVVNRMAG ILDVNPFSGS PQSPQLIRRG
PRLWTHTSDQ QVSAISNPSP CASVTAEGKT VRQPSVIYSW IQNKREQIKN FLSKRVLIMY
FFSKHPEASI QAVFSDAQMH IWALEGLSHL VAASFTEDRF GVVQTTLPAI LHTLLTLQEA
VDKYFKLPHA SSKPPRASGS LVDTSYKTLR FAFRASLKTA IYRITTTFGE HLNAVQASAE
HQKRLQQFLE FKE
