PPIL2_SCHPO
ID PPIL2_SCHPO Reviewed; 516 AA.
AC Q09928;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase cyp8 {ECO:0000305};
DE Short=PPIase cyp8;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=RING-type E3 ubiquitin transferase cyp8 {ECO:0000305};
DE AltName: Full=Rotamase cyp8;
GN Name=cyp8; ORFNames=SPAC21E11.05c;
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 SEQUENCE REVISION TO 27, AND IDENTIFICATION OF FRAMESHIFT.
RA Pemberton T.J.;
RL Submitted (MAY-2006) to UniProtKB.
RN [3]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16134115; DOI=10.1002/yea.1288;
RA Pemberton T.J., Kay J.E.;
RT "The cyclophilin repertoire of the fission yeast Schizosaccharomyces
RT pombe.";
RL Yeast 22:927-945(2005).
CC -!- FUNCTION: May catalyze the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides thereby assisting the folding of
CC proteins. May also function as a chaperone, playing a role in
CC intracellular transport of proteins. May also have a protein ubiquitin
CC ligase activity acting as an E3 ubiquitin protein ligase or as a
CC ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on
CC proteins. {ECO:0000250|UniProtKB:Q08752, ECO:0000250|UniProtKB:Q13356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q13356};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13356}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16134115}.
CC -!- INDUCTION: Induced during the meiotic cycle.
CC {ECO:0000269|PubMed:16134115}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA91964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAA91964.1; ALT_FRAME; Genomic_DNA.
DR PIR; S62590; S62590.
DR RefSeq; NP_594502.2; NM_001019931.3.
DR AlphaFoldDB; Q09928; -.
DR SMR; Q09928; -.
DR BioGRID; 278454; 2.
DR STRING; 4896.SPAC21E11.05c.1; -.
DR iPTMnet; Q09928; -.
DR MaxQB; Q09928; -.
DR PaxDb; Q09928; -.
DR PRIDE; Q09928; -.
DR EnsemblFungi; SPAC21E11.05c.1; SPAC21E11.05c.1:pep; SPAC21E11.05c.
DR GeneID; 2541969; -.
DR KEGG; spo:SPAC21E11.05c; -.
DR PomBase; SPAC21E11.05c; cyp8.
DR VEuPathDB; FungiDB:SPAC21E11.05c; -.
DR eggNOG; KOG0883; Eukaryota.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q09928; -.
DR OMA; NFIKHCA; -.
DR PhylomeDB; Q09928; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q09928; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PTHR45625; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Isomerase; Nucleus; Reference proteome; Rotamase; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..516
FT /note="Peptidyl-prolyl cis-trans isomerase cyp8"
FT /id="PRO_0000064179"
FT DOMAIN 38..115
FT /note="U-box"
FT DOMAIN 274..428
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 197..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..461
FT /evidence="ECO:0000255"
FT COMPBIAS 199..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 58626 MW; ED4B90E68B4A01D4 CRC64;
MGKNTDKLYI TQTEHSGVHG WHGGMSGIAQ KNSTTSYKQL PFNYCSLSLQ PFNHPCCLVD
ETKQAIIFDF RFIVPWLRKH GTNPINGQKA SMSDLIKLKF AKNSAEEYCD PVTMKSFTRF
SHIVAIRSTG NCFSWDTIER LNIKPKHWRD LVNEEQFTRD DIITIQDPHN VENRDFSAIQ
KQKETARDEK ITKAKIALQA SRAKSTESTS SPELSHSLDS SKSIASDMPI HRASHTTGYA
AASLTSTSFT PVTKNERAII AEEDYMLNHT RIKHKGYARI VTNHGEINIE LHTDYAPHAV
YNFVQLAKQG YYRNTIFHRN IARFMIQGGD PSGTGRGGQS IWGKPFKDEF CNPLKHDDRG
IISMANRGKN TNGSQFFILY GPAKHLDNKH TIFGRVVGGL NVLDALEKVP TNSNDHPKLP
IKLEDIIIFV DPFEEWKKDE REKEKRKRQE EEEENNLDRT SWTGRDLSAS STDHSLNASV
GKYLKKEVSL EEKTFTSTVN PKKKKARTGF GNFDAW
