ROT1_SCHPO
ID ROT1_SCHPO Reviewed; 232 AA.
AC O14103;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Protein rot1;
DE Flags: Precursor;
GN Name=rot1; ORFNames=SPAC31G5.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB11686.1; -; Genomic_DNA.
DR PIR; T38619; T38619.
DR RefSeq; NP_594002.1; NM_001019428.2.
DR AlphaFoldDB; O14103; -.
DR BioGRID; 278119; 2.
DR STRING; 4896.SPAC31G5.02.1; -.
DR MaxQB; O14103; -.
DR PaxDb; O14103; -.
DR EnsemblFungi; SPAC31G5.02.1; SPAC31G5.02.1:pep; SPAC31G5.02.
DR GeneID; 2541623; -.
DR KEGG; spo:SPAC31G5.02; -.
DR PomBase; SPAC31G5.02; rot1.
DR VEuPathDB; FungiDB:SPAC31G5.02; -.
DR eggNOG; ENOG502QQTG; Eukaryota.
DR HOGENOM; CLU_071622_0_0_1; -.
DR InParanoid; O14103; -.
DR OMA; IWQHGKY; -.
DR PhylomeDB; O14103; -.
DR PRO; PR:O14103; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..232
FT /note="Protein rot1"
FT /id="PRO_0000333416"
FT TOPO_DOM 22..211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 232 AA; 26432 MW; 1A23B6B0BFE5AA00 CRC64;
MHLLYQIGLF TCLWLTQYVG AEIDNYDENL VGTWSSKSET VLTGPDFFDP LDEDFFEPEL
PGISYSFTDD GFFEEAIYII KSNATKPQCP KGFLQWQHGT YAINDTGTLV LTPFVGDGRQ
LESDPCTSNF SVYTRYDQVE TMEKYEISMD RYHGRYKLEL YEWDGTPKQP MFLAYRPPKM
LPTSTIAVNT IQTAAKRWTA PLVPLAQKHT NTIWWVGLGL IAIGSIGYLV VS