HEX1_NEUCR
ID HEX1_NEUCR Reviewed; 176 AA.
AC P87252; Q7RV36;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Woronin body major protein {ECO:0000303|PubMed:11273682};
DE Flags: Precursor;
GN Name=hex-1 {ECO:0000303|PubMed:11273682}; ORFNames=NCU08332;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11273682; DOI=10.1006/fgbi.2000.1230;
RA Tenney K., Hunt I., Sweigard J., Pounder J.I., McClain C., Bowman E.J.,
RA Bowman B.J.;
RT "Hex-1, a gene unique to filamentous fungi, encodes the major protein of
RT the Woronin body and functions as a plug for septal pores.";
RL Fungal Genet. Biol. 31:205-217(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10783241; DOI=10.1038/35008652;
RA Jedd G., Chua N.-H.;
RT "A new self-assembled peroxisomal vesicle required for efficient resealing
RT of the plasma membrane.";
RL Nat. Cell Biol. 2:226-231(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, FUNCTION, AND MUTAGENESIS
RP OF HIS-39; GLN-127; LYS-143 AND ARG-149.
RX PubMed=12640443; DOI=10.1038/nsb910;
RA Yuan P., Jedd G., Kumaran D., Swaminathan S., Shio H., Hewitt D.,
RA Chua N.-H., Swaminathan K.;
RT "A HEX-1 crystal lattice required for Woronin body function in Neurospora
RT crassa.";
RL Nat. Struct. Biol. 10:264-270(2003).
CC -!- FUNCTION: Major component of Woronin bodies, fungal-specific organelles
CC that occlude septal pores in order to separate intact from damaged
CC compartments (PubMed:11273682, PubMed:10783241). Hex-1 binds directly
CC or indirectly to the Woronin body tether that in turn is anchored at
CC the rim of the septal pore (PubMed:11273682, PubMed:10783241).
CC {ECO:0000269|PubMed:10783241, ECO:0000269|PubMed:11273682}.
CC -!- SUBUNIT: Forms oligomers (PubMed:11273682, PubMed:10783241). Self-
CC assembles into hexagonal rods (PubMed:10783241, PubMed:12640443).
CC {ECO:0000269|PubMed:10783241, ECO:0000269|PubMed:11273682,
CC ECO:0000269|PubMed:12640443}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:10783241,
CC ECO:0000269|PubMed:11273682}. Note=Localizes at Woronin bodies, fungal-
CC specific organelles that plug the septal pore in case of physical
CC damage. {ECO:0000269|PubMed:10783241, ECO:0000269|PubMed:11273682}.
CC -!- DISRUPTION PHENOTYPE: Impairs plugging of septal pores and leads to the
CC loss of cytoplasm in hyphae severed by lightly drawing a scalpel blade.
CC {ECO:0000269|PubMed:10783241, ECO:0000269|PubMed:11273682}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. Hex1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF001033; AAB61278.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA34471.1; -; Genomic_DNA.
DR PIR; T47216; T47216.
DR RefSeq; XP_963707.1; XM_958614.3.
DR PDB; 1KHI; X-ray; 1.78 A; A=1-176.
DR PDB; 7NJH; X-ray; 2.50 A; A=1-176.
DR PDB; 7NJI; X-ray; 2.30 A; A=1-176.
DR PDBsum; 1KHI; -.
DR PDBsum; 7NJH; -.
DR PDBsum; 7NJI; -.
DR AlphaFoldDB; P87252; -.
DR SASBDB; P87252; -.
DR SMR; P87252; -.
DR STRING; 5141.EFNCRP00000006501; -.
DR PRIDE; P87252; -.
DR EnsemblFungi; EAA34471; EAA34471; NCU08332.
DR GeneID; 3879856; -.
DR KEGG; ncr:NCU08332; -.
DR VEuPathDB; FungiDB:NCU08332; -.
DR HOGENOM; CLU_021655_0_0_1; -.
DR InParanoid; P87252; -.
DR OMA; TFTIPCH; -.
DR EvolutionaryTrace; P87252; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0140266; C:Woronin body; IDA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR CDD; cd04469; S1_Hex1; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR037318; Hex1_S1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR020189; Transl_elong_IF5A_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome.
FT PROPEP 1..16
FT /id="PRO_0000007793"
FT CHAIN 17..176
FT /note="Woronin body major protein"
FT /id="PRO_0000007794"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..176
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305|PubMed:12640443"
FT MUTAGEN 39
FT /note="H->G: Abolishes the ability to self-assemble."
FT /evidence="ECO:0000269|PubMed:12640443"
FT MUTAGEN 127
FT /note="Q->A: Abolishes the ability to self-assemble."
FT /evidence="ECO:0000269|PubMed:12640443"
FT MUTAGEN 143
FT /note="K->A: Does not affect self-assembly."
FT /evidence="ECO:0000269|PubMed:12640443"
FT MUTAGEN 149
FT /note="R->A: Does not affect self-assembly."
FT /evidence="ECO:0000269|PubMed:12640443"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1KHI"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:1KHI"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1KHI"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7NJI"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1KHI"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:1KHI"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1KHI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1KHI"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1KHI"
SQ SEQUENCE 176 AA; 19127 MW; 8C1B2A85A85FCCF8 CRC64;
MGYYDDDAHG HVEADAAPRA TTGTGTGSAS QTVTIPCHHI RLGDILILQG RPCQVIRIST
SAATGQHRYL GVDLFTKQLH EESSFVSNPA PSVVVQTMLG PVFKQYRVLD MQDGSIVAMT
ETGDVKQNLP VIDQSSLWNR LQKAFESGRG SVRVLVVSDH GREMAVDMKV VHGSRL
