| UniProt functional annotation for P49687 | |||
| UniProt code: P49687. |
| Organism: | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Taxonomy: | Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. | |
| Function: | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. It is also required for normal NPC distribution (probably through interactions with MLP1 and MLP2) and NPC assembly, as well as for normal nuclear envelope organization. {ECO:0000269|PubMed:10542288, ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11823431, ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8195299, ECO:0000269|PubMed:8524308, ECO:0000269|PubMed:9305650}. | |
| Subunit: | Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. NUP145C is part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). NUP145N may bind homomeric RNA and interacts through its FG repeats with karyopherins. Interacts with MLP1 and MLP2. {ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:18160040}. | |
| Subcellular location: | [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. | |
| Subcellular location: | [Nucleoporin NUP145N]: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards the nucleoplasmic side, nuclear pore complex. | |
| Domain: | Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: GLFG repeats are especially abundant in NUPs in the central region (lacking a charged environment but are enriched in Ser, Thr, Gln, and Asn). | |
| Ptm: | NUP145 is autocatalytically cleaved in NUP145N and NUP145C. {ECO:0000269|PubMed:9305650}. | |
| Miscellaneous: | Present with 4630 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. | |
| Similarity: | Belongs to the nucleoporin GLFG family. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.