ID PPIL3_RAT Reviewed; 161 AA.
AC Q812D3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 3;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=CYP10L;
DE AltName: Full=Cyclophilin-like protein PPIL3;
DE AltName: Full=Rotamase PPIL3;
GN Name=Ppil3; Synonyms=Cyp10l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu L.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. May be involved in pre-mRNA splicing (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Identified in the spliceosome C complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF315802; AAO32943.1; -; mRNA.
DR EMBL; BC087645; AAH87645.1; -; mRNA.
DR RefSeq; NP_783638.1; NM_175707.3.
DR RefSeq; XP_006245026.1; XM_006244964.3.
DR RefSeq; XP_017451851.1; XM_017596362.1.
DR AlphaFoldDB; Q812D3; -.
DR SMR; Q812D3; -.
DR STRING; 10116.ENSRNOP00000018284; -.
DR PhosphoSitePlus; Q812D3; -.
DR jPOST; Q812D3; -.
DR PaxDb; 10116-ENSRNOP00000018284; -.
DR Ensembl; ENSRNOT00000103798.1; ENSRNOP00000079425.1; ENSRNOG00000013636.6.
DR Ensembl; ENSRNOT00055039591; ENSRNOP00055032147; ENSRNOG00055023010.
DR Ensembl; ENSRNOT00060046105; ENSRNOP00060038294; ENSRNOG00060026550.
DR Ensembl; ENSRNOT00065051236; ENSRNOP00065042177; ENSRNOG00065029653.
DR GeneID; 301432; -.
DR KEGG; rno:301432; -.
DR UCSC; RGD:631415; rat.
DR AGR; RGD:631415; -.
DR CTD; 53938; -.
DR RGD; 631415; Ppil3.
DR eggNOG; KOG0884; Eukaryota.
DR GeneTree; ENSGT00940000163579; -.
DR HOGENOM; CLU_012062_16_3_1; -.
DR InParanoid; Q812D3; -.
DR OrthoDB; 554597at2759; -.
DR PhylomeDB; Q812D3; -.
DR TreeFam; TF352224; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q812D3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013636; Expressed in quadriceps femoris and 20 other cell types or tissues.
DR Genevisible; Q812D3; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd01928; Cyclophilin_PPIL3_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 3; 1.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isomerase; Methylation; mRNA processing; mRNA splicing;
KW Reference proteome; Rotamase; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H2H8"
FT CHAIN 2..161
FT /note="Peptidyl-prolyl cis-trans isomerase-like 3"
FT /id="PRO_0000064168"
FT DOMAIN 2..154
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2H8"
FT MOD_RES 61
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6L8"
SQ SEQUENCE 161 AA; 18113 MW; CB6171376B85F82A CRC64;
MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC VFHRNIKGFM VQTGDPTGTG
RGGSSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK
VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q
//
