PPIL2_CAEEL
ID PPIL2_CAEEL Reviewed; 523 AA.
AC P52012; Q09548;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase 4 {ECO:0000305};
DE Short=PPIase 4;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=Cyclophilin mog-6;
DE AltName: Full=Cyclophilin-4;
DE AltName: Full=Masculinization of germline protein 6;
DE AltName: Full=RING-type E3 ubiquitin transferase isomerase 4 {ECO:0000305};
DE AltName: Full=Rotamase 4;
GN Name=cyn-4; Synonyms=cyp-4, mog-6; ORFNames=F59E10.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9803414; DOI=10.1016/s0166-6851(98)00096-6;
RA Page A.P., Winter A.D.;
RT "A divergent multi-domain cyclophilin is highly conserved between parasitic
RT and free-living nematode species and is important in larval muscle
RT development.";
RL Mol. Biochem. Parasitol. 95:215-227(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 255-435.
RC STRAIN=Bristol N2;
RX PubMed=8694762; DOI=10.1042/bj3170179;
RA Page A.P., Macniven K., Hengartner M.O.;
RT "Cloning and biochemical characterization of the cyclophilin homologues
RT from the free-living nematode Caenorhabditis elegans.";
RL Biochem. J. 317:179-185(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pugnale P., Puoti A.;
RT "The sex determination gene mog-6 codes for a cyclophilin that interacts
RT with MEP-1 in C. elegans.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [5]
RP FUNCTION.
RX PubMed=8111975; DOI=10.1002/dvg.1020140608;
RA Graham P.L., Schedl T., Kimble J.;
RT "More mog genes that influence the switch from spermatogenesis to oogenesis
RT in the hermaphrodite germ line of Caenorhabditis elegans.";
RL Dev. Genet. 14:471-484(1993).
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. Influences the hermaphrodite switch from spermatogenesis to
CC oogenesis. Required for body wall muscle cell development.
CC {ECO:0000250|UniProtKB:Q08752, ECO:0000250|UniProtKB:Q13356,
CC ECO:0000269|PubMed:8111975, ECO:0000269|PubMed:9803414}.
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 -!- SUBUNIT: Interacts with mep-1.
CC -!- INTERACTION:
CC P52012; Q21502: mep-1; NbExp=3; IntAct=EBI-3513766, EBI-319858;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09928,
CC ECO:0000250|UniProtKB:Q13356}.
CC -!- TISSUE SPECIFICITY: Exclusively in the larval body wall striated muscle
CC cells. {ECO:0000269|PubMed:9803414}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in the early larval stages
CC with lower levels at later larval and adult stages.
CC {ECO:0000269|PubMed:9803414}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
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DR EMBL; U36187; AAC06337.1; -; mRNA.
DR EMBL; AF421146; AAL27008.1; -; mRNA.
DR EMBL; Z36949; CAA85417.1; -; Genomic_DNA.
DR EMBL; Z46935; CAA85417.1; JOINED; Genomic_DNA.
DR PIR; T23003; T23003.
DR RefSeq; NP_496337.1; NM_063936.6.
DR AlphaFoldDB; P52012; -.
DR SMR; P52012; -.
DR BioGRID; 39984; 3.
DR IntAct; P52012; 1.
DR STRING; 6239.F59E10.2; -.
DR EPD; P52012; -.
DR PaxDb; P52012; -.
DR PeptideAtlas; P52012; -.
DR PRIDE; P52012; -.
DR EnsemblMetazoa; F59E10.2.1; F59E10.2.1; WBGene00000880.
DR GeneID; 174674; -.
DR KEGG; cel:CELE_F59E10.2; -.
DR UCSC; F59E10.2.1; c. elegans.
DR CTD; 174674; -.
DR WormBase; F59E10.2; CE01596; WBGene00000880; cyn-4.
DR eggNOG; KOG0883; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; P52012; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; P52012; -.
DR Reactome; R-CEL-210991; Basigin interactions.
DR UniPathway; UPA00143; -.
DR PRO; PR:P52012; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000880; Expressed in embryo and 4 other tissues.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0040022; P:feminization of hermaphroditic germ-line; IMP:WormBase.
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 GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
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 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 1: Evidence at protein level;
KW Developmental protein; Differentiation; Isomerase; Nucleus;
KW Reference proteome; Rotamase; Sexual differentiation; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..523
FT /note="Peptidyl-prolyl cis-trans isomerase 4"
FT /id="PRO_0000064193"
FT DOMAIN 38..111
FT /note="U-box"
FT DOMAIN 278..433
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 523 AA; 58534 MW; 399967A6303989DE CRC64;
MGKKQHQKDK LYLTTSEWKS IGGHKDDTGT RLQRAQFKRL PINHCSLSLL PFEDPVCARS
GEIFDLTAIV PYLKKHGKNP CTGKPLVAKD LIHLKFDKGE DGKFRCPVTF RTFTDHSHIL
AIATSGNVYS HEAVQELNLK RNHLKDLLTD VPFTRADIID LQDPNHLEKF NMEQFLHVKL
DLKTSEEIKK EKDAMKDPKF YIRRMNNACK SVLDQLDKEY VPKKSSTETD ETADEINAAH
YSQGKVAAGF TSTVMAPVTS NKAAVLDNDT VRYSRVKKNA FVRLVTNFGP LNLELFAPKV
PKACENFITH CSNGYYNNTK FHRLIKNFML QGGDPTGTGH GGESIWDKPF SDEFISGFSH
DARGVLSMAN KGSNTNGSQF FITFRPCKYL DRKHTIFGRL VGGQDTLTTI EKLETEEGTD
VPMVSVVIMR AEVFVDPFEE AEKEVQAERA EILKKTSKDA ASLANKKAKE TATKPEAVGT
GVGKYMKSAA AVNKRQGKME DVPLEAAKKT KFARAGLGDF SKW
