NDC1_RAT
ID NDC1_RAT Reviewed; 673 AA.
AC Q6AXN4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Nucleoporin NDC1;
DE AltName: Full=Transmembrane protein 48;
GN Name=Ndc1; Synonyms=Tmem48;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP INTERACTION WITH NUP35.
RX PubMed=16600873; DOI=10.1016/j.molcel.2006.02.015;
RA Mansfeld J., Guettinger S., Hawryluk-Gara L.A., Pante N., Mall M., Galy V.,
RA Haselmann U., Muehlhaeusser P., Wozniak R.W., Mattaj I.W., Kutay U.,
RA Antonin W.;
RT "The conserved transmembrane nucleoporin NDC1 is required for nuclear pore
RT complex assembly in vertebrate cells.";
RL Mol. Cell 22:93-103(2006).
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. {ECO:0000269|PubMed:16600873}.
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; BC079443; AAH79443.1; -; mRNA.
DR RefSeq; NP_001020194.1; NM_001025023.1.
DR AlphaFoldDB; Q6AXN4; -.
DR STRING; 10116.ENSRNOP00000014275; -.
DR PhosphoSitePlus; Q6AXN4; -.
DR jPOST; Q6AXN4; -.
DR PaxDb; Q6AXN4; -.
DR PRIDE; Q6AXN4; -.
DR GeneID; 362557; -.
DR KEGG; rno:362557; -.
DR UCSC; RGD:1560173; rat.
DR CTD; 55706; -.
DR RGD; 1560173; Ndc1.
DR eggNOG; KOG4358; Eukaryota.
DR HOGENOM; CLU_027343_0_0_1; -.
DR InParanoid; Q6AXN4; -.
DR OrthoDB; 556184at2759; -.
DR PhylomeDB; Q6AXN4; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q6AXN4; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q6AXN4; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:RGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISO:RGD.
DR GO; GO:0051664; P:nuclear pore localization; ISO:RGD.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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_0000235243"
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..273
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 406..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q9BTX1"
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; 75713 MW; 6BF73F12AFFE4C0A CRC64;
MATAASGPCA GGSPRDILWR VLGWRIVTSV VWSVLLLPVC ITAFIVFSSI DLFHPIQWLS
DSLNEFYSSQ VIFYLLLLAV VIIIISIFNV EFYTVVPSIP GSRLALIARI LHPQQLTHSF
IHAVMGMAVA WCAAIMTKGQ SRSLVVPCTG TESLDSPAAQ TCMNEYHLFF LLSGAFMGYS
YSLLYFINNM NYLPFPIIQQ YKFLRFRRSL LLLVKHSCVE SLFMVRNFCI VYYFFGHIPK
AWISTALDLR TDEQAHRPLD TIGGLLNVSL LYHVWLCGVF LLMTWYISWI LFKIYATEAY
MFPVQPPFAE ESDECLPKVL NSNPPLIIKY LALQDLMLLS QYSPSRRQEV FSLSQPGGHP
HNWTAISREC LSLLNDMTQK LVLYQEAAAT NGRMYSSYSV EPKRLSSPEE TAFQTPKPSQ
MPSVPPLVKT SLFSPKLSTP DGSSPFGTPF GSSVVNRMAG IFDVNTCCGS PQSPQLVRRG
PRLWTHTSDQ QVSAVSNPSP CASVTAEGKT VRQPSVLYSW IQNKREQIKN FLSKRVLIMY
FFSKHPEASI QAVFSDAQMH IWALEGLSHL VAASFTEDRF GVVQTTLPAI LNTLLTLQEA
VDKYFKLPHA SSKPPRTSGS LVDTSYKTLR FAFRASLKTA IYRITTTFGE HLNAVQASAE
HQKRLQQFLE FKE
