WSC_NEUCR
ID WSC_NEUCR Reviewed; 307 AA.
AC U9W802;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Woronin sorting complex protein {ECO:0000303|PubMed:18227279};
GN Name=wsc {ECO:0000303|PubMed:18227279}; ORFNames=NCU07842;
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 [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 [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP MUTAGENESIS OF ARG-102.
RX PubMed=18227279; DOI=10.1083/jcb.200705049;
RA Liu F., Ng S.K., Lu Y., Low W., Lai J., Jedd G.;
RT "Making two organelles from one: Woronin body biogenesis by peroxisomal
RT protein sorting.";
RL J. Cell Biol. 180:325-339(2008).
CC -!- FUNCTION: Woronin sorting complex protein involved in both Woronin
CC bodies (WB) formation and inherence (PubMed:18227279). Localizes to
CC large peroxisome membranes where it self-assembles into detergent-
CC resistant oligomers that envelop hex-1 assemblies, producing
CC asymmetrical nascent WBs (PubMed:18227279). These structures are then
CC delivered to the cell cortex, which permits partitioning of the nascent
CC WB and WB inheritance (PubMed:18227279). {ECO:0000269|PubMed:18227279}.
CC -!- SUBUNIT: Self-assembles into detergent-resistant oligomers and forms a
CC complex with hex-1 assemblies. {ECO:0000269|PubMed:18227279}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:18227279}; Multi-pass membrane protein
CC {ECO:0000255}. Cell septum {ECO:0000269|PubMed:18227279}.
CC Note=Localizes to nascent and mature Woronin bodies, fungal-specific
CC organelles that plug the septal pore in case of physical damage.
CC {ECO:0000269|PubMed:18227279}.
CC -!- DISRUPTION PHENOTYPE: Impairs the recruitment of hex-1 assemblies to
CC the matrix face of the peroxisome membrane, and the subsequent
CC production of Woronin bodies. {ECO:0000269|PubMed:18227279}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002238; ESA43145.1; -; Genomic_DNA.
DR RefSeq; XP_011393945.1; XM_011395643.1.
DR STRING; 5141.EFNCRP00000007466; -.
DR EnsemblFungi; ESA43145; ESA43145; NCU07842.
DR GeneID; 3879267; -.
DR KEGG; ncr:NCU07842; -.
DR VEuPathDB; FungiDB:NCU07842; -.
DR HOGENOM; CLU_066033_0_0_1; -.
DR OMA; KMAIYGA; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140266; C:Woronin body; IDA:GO_Central.
DR InterPro; IPR007248; Mpv17_PMP22.
DR PANTHER; PTHR11266; PTHR11266; 1.
DR Pfam; PF04117; Mpv17_PMP22; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Woronin sorting complex protein"
FT /id="PRO_0000455967"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000255|RuleBase:RU363053"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000255|RuleBase:RU363053"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|RuleBase:RU363053"
FT MUTAGEN 102
FT /note="R->Q: Shows a slight defect in association with hex-
FT 1 assemblies."
FT /evidence="ECO:0000269|PubMed:18227279"
FT MUTAGEN 102
FT /note="R->W: Leads to total defect in the production of
FT asymmetrical nascent Woronin bodies and localizes uniformly
FT in the peroxisome membrane."
FT /evidence="ECO:0000269|PubMed:18227279"
SQ SEQUENCE 307 AA; 33795 MW; 249F61D9947D4D4F CRC64;
MSVKEHHSTV GAIAEAVAEA AHGDLPGTKG HHPISAVIGT AITGGRQNAG TKGYLTAYLK
QLETNPLRTK MLTAGTLAGS QELLASWLAK DRNKNGNYFT ARVPKMATYG ALVSAPLGHF
LIWILQKMFQ NRKSLRAKIL QILVSNLIVA PIQNSVYLVA MAIIAGAKTW KQVQATVRVG
FWKVMKVSWL SSPLCLAFAQ KFLPEAAWMP FFNLVSFFIG TYINYITKKK RLAALRRKHF
GDGAHGDHRH DRERERDRER ERHSSPPHGH GPSHGGRPIN PTLGSHHGGG PVPPPQDYPS
LGQNPRY
