YKV5_SCHPO
ID YKV5_SCHPO Reviewed; 632 AA.
AC Q9P4X1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 4.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Thioredoxin domain-containing protein C959.05c;
DE EC=5.3.4.1;
DE AltName: Full=Putative protein disulfide isomerase C959.05c;
DE Flags: Precursor;
GN ORFNames=SPAC959.05c;
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).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts as a membrane-bound chaperone in endoplasmic reticulum
CC quality control. Probably facilitates presentation of substrate to
CC membrane-bound components of the degradation machinery (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB93012.4; -; Genomic_DNA.
DR RefSeq; NP_594172.4; NM_001019597.3.
DR AlphaFoldDB; Q9P4X1; -.
DR SMR; Q9P4X1; -.
DR BioGRID; 279894; 1.
DR STRING; 4896.SPAC959.05c.1; -.
DR PaxDb; Q9P4X1; -.
DR PRIDE; Q9P4X1; -.
DR EnsemblFungi; SPAC959.05c.1; SPAC959.05c.1:pep; SPAC959.05c.
DR GeneID; 2543474; -.
DR KEGG; spo:SPAC959.05c; -.
DR PomBase; SPAC959.05c; -.
DR VEuPathDB; FungiDB:SPAC959.05c; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_432898_0_0_1; -.
DR InParanoid; Q9P4X1; -.
DR OMA; RQFRSHE; -.
DR PRO; PR:Q9P4X1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
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:0003756; F:protein disulfide isomerase activity; ISO:PomBase.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0006595; P:polyamine metabolic process; ISS:PomBase.
DR GO; GO:0006621; P:protein retention in ER lumen; ISO:PomBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Membrane; Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..632
FT /note="Thioredoxin domain-containing protein C959.05c"
FT /id="PRO_0000303923"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 153..284
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 209..212
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 632 AA; 73820 MW; 6A9A1BCCEDA9245F CRC64;
MKLFLYHFTF IVYYFIISFS YAFSIKQEII VSSHNASSIL NTTAFWFVEF TESKYDKEEF
SVIWNEVSME FPDIRRAKVF CDLDLEFCAQ QEIYDHPKVV VLKNGMWMRH VLEKNQITTK
SARQFVKSHL GNCDLEQAEN ETDCFSDDGE YNSDSSSTDP AFELKEDQSW KHSSILRPLE
TLNFKRFLFG NEIMSKTRAF VMFVSLKHCE DCFHWEAVWS SITRNTDERL KMAQVNCDEE
KEMCNHFHIK KFPTFRVFQG FDSIQYNGPL KYQQLLSYSN QVASYQAIKI EEGDIESIEN
SHPVFFLVLY DFATTSEDFS IIERLKLQLA GVAPLYICNS KALANKYGAQ SQPSIIAVRN
GMPIVYQAIT PREFRDYKRI TEWINIVSSP FITELTPTKC HSLLNRKLTV LTLLQPDSEQ
FFSSQEELLR LGKRWFRFQM QRQRNDIVWS RIKKYSAIAE AKKKGFARKV KRIKYSKISH
PTYTESVSFL WLDSSLWLDW IVENLDHTVY VDSITPPVFV IDHSKGVIYV SDRNGNSLTL
EEDSLFSTLR IILEHPNSSR LQKLRAPGLC PNGSPNYRNR YKLIVFNLLI ALLILSILTI
ISASRLSRRR RQLLNKQPVF GFYHSLVIAK SD
