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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
 
 
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