PO152_CHATD
ID PO152_CHATD Reviewed; 1270 AA.
AC G0SB44; G0ZGV5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Nucleoporin POM152 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein POM152;
DE AltName: Full=Pore membrane protein POM152;
GN Name=POM152; ORFNames=CTHT_0048830;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. POM152 is important for the de novo assembly of NPCs.
CC {ECO:0000250|UniProtKB:P39685}.
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:P39685, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P39685}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P39685}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P39685}. Note=Central core structure of the
CC nuclear pore complex. {ECO:0000250|UniProtKB:P39685}.
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DR EMBL; GL988044; EGS19424.1; -; Genomic_DNA.
DR EMBL; JF276300; AEL00693.1; -; Genomic_DNA.
DR RefSeq; XP_006695246.1; XM_006695183.1.
DR AlphaFoldDB; G0SB44; -.
DR STRING; 759272.G0SB44; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS19424; EGS19424; CTHT_0048830.
DR GeneID; 18258921; -.
DR KEGG; cthr:CTHT_0048830; -.
DR eggNOG; ENOG502QQ5B; Eukaryota.
DR HOGENOM; CLU_002415_0_0_1; -.
DR OrthoDB; 76544at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
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:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR037701; Pom152.
DR PANTHER; PTHR28206; PTHR28206; 1.
PE 3: Inferred from homology;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1270
FT /note="Nucleoporin POM152"
FT /id="PRO_0000433180"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P39685"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..95
FT /note="Perinuclear space"
FT /evidence="ECO:0000250|UniProtKB:P39685"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P39685"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..1270
FT /note="Perinuclear space"
FT /evidence="ECO:0000250|UniProtKB:P39685"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 756..763
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 141551 MW; D114EA9AA965C577 CRC64;
MSDAPAVGAF PQTPVAARRG PARPSDSTTS TTIKRTSPLP LAPQAGRQAT NISPVIPLHI
LDAPTQRFYA FAFYLALTAW KLYDWTQVLE EDTESFLLFL KWIAIDCVFL FGLPELRIPW
LELSQPFVMV AFAIHAMFDW ILMFNIGFPW QSWVIGLLKV FYDREIAISE HNVKLSSILQ
NSSLIMGRQI INILPEGSAI LNPELQPFCL GGDRKTANIP IFFNSTIPVE VELIRTDFET
GQQESIKLSK SQLRDIERRA KRESQDGDTV QSIVQFDFPV KKTGAYRLGR VLDEYKLEVQ
RRNPLTFVVS CPKAWVGPAL SAHRCVGDLS DLSMMVEGTP PLKIKYSRMI NGKDHSFHFQ
SLQPEGFVSP LSGLRSNNWG YDEDDISWAR AQKVPVGLNE SMHSSGDWQY SIDEVQDGFG
NIIKYDSLAD DPDGKPKPKH LTQSFVVKKR PVIRLEGCDL RHPLKVAKGK SKNLPVSYGL
SGGSREDSTY QIAWQFSPID TLTESGDHGD VVTIGTYTAK NNRDRPTISA PGLYTLKSVS
ASQCEGEIQE PSSCLLLNPL EPRLSLRHEE IPDTCAGNSI GLRVDLDLIG TPPFIVRYDV
ISNGERRSER VSIPGLRYQL DLVPRIAGHH KYIFTHVGDS IYDGQKLSGP EYVLEQDVKP
AAAALIQHST GKMSSCLGDQ VTVDILLLGD PPFTLEWELI HDGKRKQFKV PNIQENSYQI
KTAPLTTGGE YTLGLTSVQD KRGCRNFLQE ELKISVRRQS PRAAFGQVDG KRKILAVEGS
SVKLPLRLTG EGPWKVYYAN LHDGSPDKPK VQEKIIKSDN GFLEVRGRGA FAITDVWDSQ
CHGVVDPKAS RFDVDWFPRP ELSVALTHGV SKTETGFQLQ DVCEGDVSGF EVALKGTPPF
TVEYEVRHHP LQGSSSLSKK KIEGVVGKEA IQADTSKAGT YTYKFTALED DLYSSNRGFQ
PIIVKQNVNR KPTASFVKPG QTFKYCKSEQ DNEDGIPITL TGVPPFFLEV EIKHQSAAVP
EIYRTPAIDS HSYELKIPRH HLRLGTQHIR IRDIRDGSGC HSTSGILSGP SVQVQLFEAP
TIYPLETRTD YCVGERISYT LSGQAPFEVW YTFNGVELKA KSPNTNFRRI AESPGEFTIT
SVSDKASECR APVSITKTIH PLPAVRISKG KSVRVDIHEG GEVDILFEFF GTPPFEFTYT
RSTNARKGQK SQVLETRHDI SHEHSKVIKA SQEGTYEVVA IKDKYCSFST QAVVGLEGGK
KDKTKKLKVY
