ROT1_COCIM
ID ROT1_COCIM Reviewed; 251 AA.
AC Q1DNE5; A0A0D6K9N3; J3K5P2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein ROT1;
DE Flags: Precursor;
GN Name=ROT1; ORFNames=CIMG_08168;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704913; EAS29422.1; -; Genomic_DNA.
DR RefSeq; XP_001241005.1; XM_001241004.2.
DR AlphaFoldDB; Q1DNE5; -.
DR STRING; 246410.Q1DNE5; -.
DR EnsemblFungi; EAS29422; EAS29422; CIMG_08168.
DR GeneID; 4560448; -.
DR KEGG; cim:CIMG_08168; -.
DR VEuPathDB; FungiDB:CIMG_08168; -.
DR InParanoid; Q1DNE5; -.
DR OMA; PMHPMYL; -.
DR OrthoDB; 1494547at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..251
FT /note="Protein ROT1"
FT /id="PRO_0000333409"
FT TOPO_DOM 20..225
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 184..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
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 251 AA; 28059 MW; 1C3A2AE79E061459 CRC64;
MVLIVALLVF FCFLTAVPAA LDPKLTGTWA TKSRKVVTGP AFYDPAEDRF QEPENTGISY
SFTEDGYFEE AYFRAIPNPT KPSCASAMMQ FQHGKYSVES NGSLVLTPFA VDGRQLISSP
CKSEGSMYFR FNQTEVFKRY EVLTDPFHNV KRLNLYQFDG TPMNPMFLVF DPPQMLPTET
LNPTAQASAT GRSKAKRGLP YGSGMASSRN KRPSTQVGGL TDPDKWWWAG VMMTLVGGVA
FLYSESPWKD W