AMO1_CHATD
ID AMO1_CHATD Reviewed; 557 AA.
AC G0S381; G0ZGU0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Nucleoporin AMO1 {ECO:0000303|PubMed:21784248};
DE AltName: Full=Nuclear pore protein AMO1;
GN Name=AMO1; ORFNames=CTHT_0020020;
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. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). AMO1 is specifically important
CC for nuclear protein and mRNA export. {ECO:0000250|UniProtKB:P49686}.
CC -!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive means
CC of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC ions and small molecules and the active, nuclear transport receptor-
CC mediated bidirectional transport of macromolecules such as proteins,
CC RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC nuclear envelope. The 55-60 MDa NPC is composed of at least 28
CC different subunits: AMO1, ELYS, GLE1, GLE2, MLP1, NDC1, NIC96, NSP1,
CC NUP133, NUP145, NUP152, NUP159, NUP170, NUP188, NUP192, NUP37, NUP49,
CC NUP53, NUP56, NUP57, NUP82, NUP84, NUP85, POM152, POM33, POM34, SEC13
CC and SEH1. Due to its 8-fold rotational symmetry, all subunits are
CC present with 8 copies or multiples thereof.
CC {ECO:0000250|UniProtKB:P49686, ECO:0000305|PubMed:21784248}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P49686}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P49686}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49686}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P49686}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: SXFG/PXFG
CC repeats are especially abundant in NUPs on the cytoplasmic side.
CC {ECO:0000250|UniProtKB:P49686}.
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DR EMBL; GL988040; EGS22464.1; -; Genomic_DNA.
DR EMBL; JF276280; AEL00678.1; -; Genomic_DNA.
DR RefSeq; XP_006692483.1; XM_006692420.1.
DR PDB; 6B4G; X-ray; 2.65 A; B/D/F/H=493-557.
DR PDB; 6B4H; X-ray; 2.17 A; B/D=493-557.
DR PDBsum; 6B4G; -.
DR PDBsum; 6B4H; -.
DR AlphaFoldDB; G0S381; -.
DR SMR; G0S381; -.
DR STRING; 759272.G0S381; -.
DR TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR EnsemblFungi; EGS22464; EGS22464; CTHT_0020020.
DR GeneID; 18256040; -.
DR KEGG; cthr:CTHT_0020020; -.
DR eggNOG; ENOG502RVHV; Eukaryota.
DR HOGENOM; CLU_028685_1_0_1; -.
DR OrthoDB; 1562631at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Metal-binding; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Translocation; Transport; Zinc; Zinc-finger.
FT CHAIN 1..557
FT /note="Nucleoporin AMO1"
FT /id="PRO_0000433186"
FT REPEAT 171..174
FT /note="SXFG 1"
FT REPEAT 200..203
FT /note="SXFG 2"
FT REPEAT 213..216
FT /note="SXFG 3"
FT REPEAT 228..231
FT /note="SXFG 4"
FT REPEAT 240..243
FT /note="SXFG 5"
FT REPEAT 249..252
FT /note="SXFG 6"
FT REPEAT 262..265
FT /note="SXFG 7"
FT REPEAT 282..285
FT /note="SXFG 8"
FT REPEAT 303..306
FT /note="SXFG 9"
FT REPEAT 314..317
FT /note="SXFG 10"
FT REPEAT 348..351
FT /note="SXFG 11"
FT REPEAT 370..373
FT /note="SXFG 12"
FT REPEAT 387..390
FT /note="SXFG 13"
FT REPEAT 407..410
FT /note="SXFG 14"
FT ZN_FING 1..25
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 161..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..141
FT /evidence="ECO:0000255"
FT COMPBIAS 161..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 48
FT /note="S -> SAP (in Ref. 1; AEL00678)"
FT /evidence="ECO:0000305"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 518..522
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 524..536
FT /evidence="ECO:0007829|PDB:6B4H"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6B4H"
SQ SEQUENCE 557 AA; 57987 MW; C2C6C2116C34C98F CRC64;
MTVCRFWQQG YCRNGNACKF EHPPKGGQNY NRFGALSGSG QGMGGRVSEP PHYPGLSEDA
IQKDLTSELP TWILSCYGPG RDAPEQLFGG YPREQSFEEI RLHFYNGLMA GNPQGALNEI
QAAYQAAQQQ IQNTLQNIPA AVQFILDAAN KHPNRIDICR ESSKGSSTGG SVFGRNVNPF
QQSSAAPLNP FGAPSTPSTS AFGQPSPLGQ KSSAFGTPAF GQPSQPVSAF GKPSALGGGS
AFGSPQTGST FGQPSVLGAK PSAFGQPAFG QPAFGQPAFG QSAFGQPSAL GPKPGAFGTS
AGSAFGASTT TAPSPFGAAA QATQPANPFG QPSQQAANSF GKPAAPASAF GQPSTTTAQN
PFGQPSTQSS AFGQQQPQQA GTFGSPSLFG QQQQQPSNVF GQPSTTSAFG SQAATSGFSQ
LGNATSTIGA SPAGAQAPAS KSPYHPGSTR QHPDLLSYAT KNPAGGLDTF KGKPVVYETP
KGAAKPVPHI RQFDGTLVRI WMPDGAPAYT ADTEAEDPKV YEDEGVKRQW QSFLEKGRFE
GGMPEVPPRR EWCVWDF
