CYPR_CALVI
ID CYPR_CALVI Reviewed; 234 AA.
AC P28517;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=NINAA;
OS Calliphora vicina (Blue blowfly) (Calliphora erythrocephala).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Calliphorinae; Calliphora.
OX NCBI_TaxID=7373;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1644830; DOI=10.1016/s0021-9258(18)42025-x;
RA Ondek B., Hardy R.W., Baker E.K., Stamnes M.A., Shieh B.-H., Zuker C.S.;
RT "Genetic dissection of cyclophilin function. Saturation mutagenesis of the
RT Drosophila cyclophilin homolog ninaA.";
RL J. Biol. Chem. 267:16460-16466(1992).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts on the folding of rhodopsin RH1 and RH2 (but not
CC RH3) and is required for visual transduction.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in photoreceptor cells.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P28517; -.
DR SMR; P28517; -.
DR PRIDE; P28517; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Isomerase; Membrane; Rotamase; Sensory transduction; Signal;
KW Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..234
FT /note="Peptidyl-prolyl cis-trans isomerase, rhodopsin-
FT specific isozyme"
FT /id="PRO_0000025492"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 29..187
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 26380 MW; 61992B951A8E5E19 CRC64;
MNILKILILL ELIYTCVSGL SFTVTSKIYM DVKHQKKPLG RIVFGLFGKR APKTVTNFRH
ICLRGINGTT YVGSEFHRVI SRFLIQGGDI VNNDGTGSTS IYGDFFQDEA LDVEHLRPGY
LGMANRGPDT NGCQFYVTTV AAQWLNGKHT VFGKVIEGMD TVYAIEDVKT DTDDHPIDPV
IIVNCGEMPT EPYEFYPDDF SILGWIKAAG LPFCSSFIVL MIFHYFFRQL NMYC
