PPIL2_NEUCR
ID PPIL2_NEUCR Reviewed; 597 AA.
AC Q7RXA6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000305};
DE Short=PPIase;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=Cyclophilin-60;
DE AltName: Full=Cyclophilin-like protein Cyp-60;
DE AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000305};
DE AltName: Full=Rotamase;
GN Name=ppi-2; Synonyms=cyp6; ORFNames=NCU00181;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:0000250|UniProtKB:Q09928,
CC ECO:0000250|UniProtKB:Q13356}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
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DR EMBL; CM002238; EAA27168.1; -; Genomic_DNA.
DR RefSeq; XP_956404.1; XM_951311.2.
DR AlphaFoldDB; Q7RXA6; -.
DR SMR; Q7RXA6; -.
DR STRING; 5141.EFNCRP00000000156; -.
DR EnsemblFungi; EAA27168; EAA27168; NCU00181.
DR GeneID; 3872544; -.
DR KEGG; ncr:NCU00181; -.
DR VEuPathDB; FungiDB:NCU00181; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q7RXA6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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: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; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF04564; U-box; 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 3: Inferred from homology;
KW Isomerase; Nucleus; Reference proteome; Rotamase; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..597
FT /note="Peptidyl-prolyl cis-trans isomerase-like 2"
FT /id="PRO_0000232987"
FT DOMAIN 41..114
FT /note="U-box"
FT DOMAIN 328..483
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 495..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65801 MW; 3F30184DC195CABA CRC64;
MGKGTDKLYI THSEWSSSDA YGASTGANAG ARAQRRGASF KKLPFNFCAA SLQPFKNPVC
TPDGTIFDVE VIGSWLEKHK TNPVTGEPLS AKDLIKLNFA RNGDTTDSDE NKGDLIDPVT
FKVFTDNTHI VAIRHGSYAN VFAWETVERM NIKPKMWRDL VDDEEFGRRD IITLQDPQNV
SASRDLSQFK YLQDGQDAIL TKEQEEERKG GTVNIEALGR VGEKVLRAKE AVERARAARQ
AGGADVNRLT QALTTTSTNS ATNNNKTAIA RGQSLIQERK RPANAATYTT GLTAASFTST
GLTPSTSGSL ALLSDEQYLL KPSHRIKNKG YVRMETNLGP LTLELLPEFA PKAVWNFLRL
SEKGYYRDVA FHRSIRNFMI QGGDPSGTGR GGSSIWGKNF EDEFEGPNTH SARGIVSMAN
KGKNTNSSQF FITYRPASHL DRKHTIFAKV IEGQDTTLTA MENVATDGSD RPLNKIVIKD
MIILIDPFAE WMKEKKQKEG EEERKREVAR QGGTEDDRTT WTGKRIRADG TMEGQGMGEG
GGGGPKVGKY LDVGAVKKAA TTTTTTTRKA EEEEVDTWEE PVRKKAKMGG FGNFDGW
