ID   MLP1_CHATD              Reviewed;        2085 AA.
AC   G0SA56; G0ZGV4;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Protein MLP1 homolog {ECO:0000303|PubMed:21784248};
GN   Name=MLP1; ORFNames=CTHT_0041070;
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: Involved in the structural and functional organization of
CC       perinuclear chromatin. Associates with the nuclear pore complex and
CC       form filamentous structures along the nuclear periphery.
CC       {ECO:0000250|UniProtKB:Q02455}.
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:O74424, ECO:0000305|PubMed:21784248}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02455}.
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DR   EMBL; GL988043; EGS19628.1; -; Genomic_DNA.
DR   EMBL; JF276299; AEL00692.1; -; Genomic_DNA.
DR   RefSeq; XP_006694513.1; XM_006694450.1.
DR   AlphaFoldDB; G0SA56; -.
DR   SMR; G0SA56; -.
DR   DIP; DIP-61564N; -.
DR   IntAct; G0SA56; 2.
DR   STRING; 759272.G0SA56; -.
DR   TCDB; 1.I.1.1.2; the nuclear pore complex (npc) family.
DR   EnsemblFungi; EGS19628; EGS19628; CTHT_0041070.
DR   GeneID; 18258145; -.
DR   KEGG; cthr:CTHT_0041070; -.
DR   eggNOG; KOG4674; Eukaryota.
DR   HOGENOM; CLU_001250_0_0_1; -.
DR   OrthoDB; 20957at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProt.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR   InterPro; IPR012929; TPR/MLP1.
DR   Pfam; PF07926; TPR_MLP1_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Nucleus; Reference proteome.
FT   CHAIN           1..2085
FT                   /note="Protein MLP1 homolog"
FT                   /id="PRO_0000433195"
FT   REGION          365..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1482..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1567..1591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1816..2085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          44..367
FT                   /evidence="ECO:0000255"
FT   COILED          399..513
FT                   /evidence="ECO:0000255"
FT   COILED          568..630
FT                   /evidence="ECO:0000255"
FT   COILED          675..1205
FT                   /evidence="ECO:0000255"
FT   COILED          1232..1667
FT                   /evidence="ECO:0000255"
FT   COILED          1744..1799
FT                   /evidence="ECO:0000255"
FT   MOTIF           1159..1166
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        374..398
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1570..1584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1819..1846
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1909..1965
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2085 AA;  231069 MW;  0D7256FEA6B938F2 CRC64;
     MAAAEVDLGY LSAQANISQV DLETVVSAPT ADLVKSVLAA VLSKIRELEQ DKFHLNVELE
     GAIRGAESRC EQFKATSDKA LKEVEELRQK LQSEESARRT LENELQTLKS SGSASLSEIE
     TLRARIASLE TSNRETLAIV DSKASANAAL SEELQKQHQK ILKLNQEINN LNQAVQTAQT
     AANSAKYREE SLKQELELAK KNNDWYDNEL KTKAAENLKI RKEKGAQIAQ LQREKEDALS
     TIQSLQKTEQ QLRKRLQEAQ SKAEEALTKV QQLQESAARA EESFRQELES SKRLVELKDQ
     QAQTHRNRLK EVELRLEKVK DDSAEEIRRV RRELEQAKED LSQSEQQVQD LQSEVDRLRT
     LVESHDGVPG SVPQTPRANG SLLARPSSPF GTPASLRGKA TQRATETLEE LLKVKAQLAS
     EQRRSQKLQE DLDDAVSMLE AKLPEIDELN AESERLRNEV IQMSEIMQQS YEERDAAVKA
     ARKAEAAASQ AQAEVKILRA QLRDLSTQIH VLIFNAHAKE KGMDQLTEEE IAQFERLQRG
     EISEGALEDL SDTHRFITER FTVFKDIYEL QQKNEELLKL TRELATKMEN EEALAAQRQA
     AQEHEEVQQL RATVAALQDE VRSITIRMKS HMTERDMFRR MLQQRATPAE IQKVLGTQAD
     GEQREVLPSV EQPHANEAQL AAALRELQAQ FDAYRNDQVT DRNAMREQID KLSGEKGSLQ
     SEVTKLSSQL TLATERYNML ESNFKALQSE NQELQKRNQS LSEAAAKQDI RTQQVAEDLV
     EARGLVESLR SENANLKAEK ALWRTIQERL TQDNESLAQE KTRLNGLLAS QQSLLNEREL
     SEAETKRRLQ AQIDSLEAEL STTKRKLSEE IEESKKVQLR KEFDAQQFQK RIDELTSMIS
     QVKEENIQVK TTRDHLQARV SELEIEVRNA QERAERLRPL PTPRAPAAAE QPSEEAQARI
     EELEGEVQEL KNNLDLLTVQ LEHAKQQAEQ FKQLSKDMEE ELSSLNESHE QYRQEMDAAL
     ASKANTINEL QQRVEALTAE LSNTNNELNM LRDSQSDVAR KFEEKERMLN AEIARLKDEE
     ERYKEAARFH QQDLRAQAEI ATKAQQDYEQ ELVKHAEAAK LLQQLRAEHN ELKTQAAAWR
     AEADSAKISL AQSEQSWEER RQRLEQEIAE IKARRDDMAA QNKLLHQQLD AVTAQITALQ
     QKRTQGDVSG EAAAPAIADM ATEGLRELNS YLRREKEILE VQYDIKVQEA KRLQQQLEYT
     QSQLDETRLK LEQERASQAD STRTSLTHKE LMEKLNELNL IRESNVTLRN ENQRAQALLE
     QKAARITELE AKIQPLEARI AELELDKGFK EEEIRQLQEA RDGLQKRIET ILSKYGQADP
     QEVEQLKAMI AALEGERDVL KQSEQALQQK VKEAENALET KTNEWKATRE KLAEDFKARF
     RNMKTQRDEA TNEKNTLQAT LDGVKEQLAA LEKELETTKQ QLATATEKNT SLQQQLAASS
     TEQPAAAPVS AAPSDQINEL TQQLQAVKQQ LESVSAQKAA AEAQVEQLKQ ELAAAIAERD
     RALAATSGGD VATAETSVSA QPSAGLSDEE RKALEEKIAA AEAKAAEFEK RAKELEEQAD
     NIVKQRSDKM KTALNKKLQE SKEAMEKQIQ EEKAKLQAEF DLKLQQELAI IKAEQQTAGP
     QNGVPATPVK TEANAAPGTP VPDITNMTDA QIREAVAKNP TISAIVKSNV KRMVAAETKK
     IKEEIEAALK AEYEQKITNA KEQATALTEK KSALRINMLD RQHKTAQAKL AIVETAAKET
     PQKPVVEVWN IAKDAKPPAP AQAPAPAPAS AAPSPAPTPA QPVAPATAAP AAPAQAPSAA
     PPKEETKQEA KTTTAAPPSA IPKPAVNPFT APLNPFGAPA PTSNIPAPPQ AGQQPQQTQP
     QQPQQPQQQQ QQQKGQQQQQ QQQQQQQGQQ QQQQGQQQAG GQNQPQRMGI PVPAGRGGPG
     GARTARGLYQ AGPRGARGGR GGGFVGAGRG AGGAAGGLNP NAGEFTPGGA TATAAAAAAA
     GGAGGSAGAG NAGNKRQRDG EGGQPQGERG GKRARGGGGG GGGNQ