NDC1_PONAB
ID NDC1_PONAB Reviewed; 674 AA.
AC Q5RBY5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Nucleoporin NDC1;
DE AltName: Full=Transmembrane protein 48;
GN Name=NDC1; Synonyms=TMEM48;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858497; CAH90725.1; -; mRNA.
DR RefSeq; NP_001125404.1; NM_001131932.1.
DR AlphaFoldDB; Q5RBY5; -.
DR STRING; 9601.ENSPPYP00000001548; -.
DR GeneID; 100172309; -.
DR KEGG; pon:100172309; -.
DR CTD; 55706; -.
DR eggNOG; KOG4358; Eukaryota.
DR InParanoid; Q5RBY5; -.
DR OrthoDB; 556184at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..674
FT /note="Nucleoporin NDC1"
FT /id="PRO_0000235242"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..68
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..165
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..272
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 394..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTX1"
SQ SEQUENCE 674 AA; 76078 MW; 21A3796EF0BF611F CRC64;
MATAVSGPCA GRSRDILWRV LGWRIVASII WSVLLLPICT TVFIIFSRID LFHPIQWLSD
SFSDLYSSYV IFYLLLLSVV IIIISIFNVE FYAVVPSIPC SRLALIGKII HPQQLMHSFI
HAAMGMVMAW CAAVITQGQY SFLVVPCTGA NSFGSPAAQT CLNEYHLFFL LAGALMGYSY
SLLYFVNNMN YLPFPIIQQY KFLRFRRSLL LLVKHSCVES LFLVRNFCIL YYFLGYIPKA
WISTAMNLHI DEQVHRPLDT VSGLLNLSLL YHVWLCGAFL LTTWYVSWIL FKIYATEAHV
FPVQPPFAEG SDECLPKVLN SNPPPIIKYL ALQDLMLFSQ YSPSRRQEVF SLSQPGGHPH
NWTAISRECL NLLNGMTQKL VLYQEAAATN GRVSSSYPVE PKKLNSPEET TFQTPKSSQM
PRPSVPPLVK TSLFSSKLST PEVVSPFGTP FGSSVMNRMA GIFDVNTCFG SPQSPQLIRR
GPRLWTSASD QQMTEFSNPS PSTSISAEGK TMRQPSVIYS WIQNKREQIK NFLSKRVLIM
YFFSKHPEAS IQAVFSDAQM HIWALEGLSH LVAASFTEDR FGVVQTTLPA ILNTLLTLQE
AVDKYFKLPH ASSKPPRISG SLVDTSYKTL RFAFRASLKT AIYRITTTFG EHLNAVQASA
EHQKRLQQFL EFKE