ID   PPI_LOTGI               Reviewed;         206 AA.
AC   B3A0R0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase {ECO:0000250|UniProtKB:P52013};
DE            Short=PPIase {ECO:0000250|UniProtKB:P52013};
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:P52013};
DE   Flags: Precursor;
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND IDENTIFICATION.
RC   TISSUE=Gonad {ECO:0000269|Ref.1};
RA   Richardson P., Lucas S., Rokhsar D., Wang M., Lindquist E.A.;
RT   "DOE Joint Genome Institute Lottia gigantea EST project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 33-52 AND 81-97, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23145877; DOI=10.1111/febs.12062;
RA   Marie B., Jackson D.J., Ramos-Silva P., Zanella-Cleon I., Guichard N.,
RA   Marin F.;
RT   "The shell-forming proteome of Lottia gigantea reveals both deep
RT   conservations and lineage-specific novelties.";
RL   FEBS J. 280:214-232(2013).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250|UniProtKB:P52013}.
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:0000250|UniProtKB:P52013};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23145877}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC       calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255}.
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DR   EMBL; FC703701; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_009066228.1; XM_009067980.1.
DR   AlphaFoldDB; B3A0R0; -.
DR   SMR; B3A0R0; -.
DR   EnsemblMetazoa; LotgiT222979; LotgiP222979; LotgiG222979.
DR   GeneID; 20247086; -.
DR   KEGG; lgi:LOTGIDRAFT_222979; -.
DR   CTD; 20247086; -.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   OMA; EHYGAGW; -.
DR   OrthoDB; 1403619at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gene3D; 2.40.100.10; -; 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   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Isomerase; Rotamase; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..206
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415262"
FT   DOMAIN          28..185
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   206 AA;  22575 MW;  4B33078851E3DE3C CRC64;
     MNSLVLPLCL LALFGFSQGE LLVTKKVYFD IKIGNEPIGR IVMGLFGNVV PRTTENFYQL
     CTGQNGYGYT GSKFHRVIPK FMIQGGDFTK GDGTGGKSIY GAKFADENFQ LEHYGAGWLS
     MANAGQDANE SQFFVTTVKC PWLDGRHVVF GKVLEGMDIV KHIEQMPTDS TDRPIEDVVI
     SESGAIELDT PFAVDKTGVG ADEEEE