ROT1_ASPNC
ID ROT1_ASPNC Reviewed; 236 AA.
AC A2QMB8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Protein rot1;
DE Flags: Precursor;
GN Name=rot1; ORFNames=An07g01540;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Required for normal levels of the cell wall 1,6-beta-glucan.
CC Involved in a protein folding machinery chaperoning proteins acting in
CC various physiological processes including cell wall synthesis and lysis
CC of autophagic bodies (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ROT1 family. {ECO:0000305}.
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DR EMBL; AM270120; CAK96599.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QMB8; -.
DR PaxDb; A2QMB8; -.
DR EnsemblFungi; CAK96599; CAK96599; An07g01540.
DR VEuPathDB; FungiDB:An07g01540; -.
DR HOGENOM; CLU_071622_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006458; P:'de novo' protein folding; IEA:InterPro.
DR InterPro; IPR019623; Rot1.
DR PANTHER; PTHR28090; PTHR28090; 1.
DR Pfam; PF10681; Rot1; 1.
DR PIRSF; PIRSF017290; ROT1_prd; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..236
FT /note="Protein rot1"
FT /id="PRO_5000220114"
FT TOPO_DOM 23..217
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 178..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 236 AA; 25992 MW; 4B662B07851C0ED4 CRC64;
MATYFFLGLL LTAVGTSSSS SASDLEGTWT TKSRQVVTGP GFYDPIGDKF LEPNLTGISY
SFSADGHYEE AYYRAIANPQ DPSCPKGVMQ WQHGTYTVNS DGSVDLTPIA VDGRQLLSDP
CQSSTGTYTR YNQTEHFESF AVSVDSYHGV QRLDVKNFDG SPMHPMYLIY KPPQMLPTQT
LNPSSSSKSK RQVEGGTGGR FSIKDLVSRE KVGDPNNWLW LGIFMTTLGG ITFFRS