ID W5UDV0_ICTPU Unreviewed; 189 AA.
AC W5UDV0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN Name=PPIF {ECO:0000313|EMBL:AHH40065.1};
GN Synonyms=ppifa {ECO:0000313|RefSeq:XP_017319886.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH40065.1};
RN [1] {ECO:0000313|EMBL:AHH40065.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH40065.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [2] {ECO:0000313|RefSeq:XP_017319886.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017319886.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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 Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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DR EMBL; JT412968; AHH40065.1; -; mRNA.
DR RefSeq; XP_017319886.1; XM_017464397.3.
DR STRING; 7998.ENSIPUP00000000266; -.
DR Ensembl; ENSIPUT00000000298; ENSIPUP00000000266; ENSIPUG00000000214.
DR GeneID; 108263515; -.
DR KEGG; ipu:108263515; -.
DR CTD; 447887; -.
DR OMA; VMKMQSF; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000221080; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_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 PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF570; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 31..187
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 189 AA; 20613 MW; 4AB302F2353DE356 CRC64;
MLQMKNRLKY CSLAIAASRL LSGAVRNPLV FLDIAADGEF IGRIIIELNA DAVPKTAENF
RALCTGEHGF GYKGSIFHRI IPEFMCQGGD FTNHNGTGGK SIYGKNFKDE NFKLKHTGSG
VLSMANSGPN TNGSQFFICT AKTEWLDGKH VVFGQVNEGM ETVRVMESYG LHDGGTLKKI
VITDCGELK
//
