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Database: UniProt
Entry: B5X288_SALSA
LinkDB: B5X288_SALSA
Original site: B5X288_SALSA 
ID   B5X288_SALSA            Unreviewed;       342 AA.
AC   B5X288;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   Name=AIP {ECO:0000313|EMBL:ACI33419.1};
GN   Synonyms=aip {ECO:0000313|RefSeq:NP_001133532.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI33419.1};
RN   [1] {ECO:0000313|EMBL:ACI33419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33419.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI33419.1, ECO:0000313|RefSeq:NP_001133532.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33419.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACI33419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33419.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001133532.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a positive role in AHR-mediated (aromatic
CC       hydrocarbon receptor) signaling, possibly by influencing its
CC       receptivity for ligand and/or its nuclear targeting.
CC       {ECO:0000256|ARBA:ARBA00002518}.
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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
CC   -!- SUBUNIT: Interacts with RET in the pituitary gland; this interaction
CC       prevents the formation of the AIP-survivin complex.
CC       {ECO:0000256|ARBA:ARBA00011636}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; BT045157; ACI33419.1; -; mRNA.
DR   EMBL; BT046084; ACI34346.1; -; mRNA.
DR   RefSeq; NP_001133532.1; NM_001140060.1.
DR   STRING; 8030.ENSSSAP00000072118; -.
DR   PaxDb; 8030-ENSSSAP00000072118; -.
DR   Ensembl; ENSSSAT00000105333; ENSSSAP00000072113; ENSSSAG00000063862.
DR   Ensembl; ENSSSAT00000181177; ENSSSAP00000138975; ENSSSAG00000063862.
DR   GeneID; 100195031; -.
DR   KEGG; sasa:100195031; -.
DR   CTD; 9049; -.
DR   OMA; HIHEEGN; -.
DR   OrthoDB; 11153at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
DR   Bgee; ENSSSAG00000063862; Expressed in spleen and 16 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR039663; AIP/AIPL1/TTC9.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11242:SF3; AH RECEPTOR-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR11242; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN RELATED; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   2: Evidence at transcript level;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT   DOMAIN          31..85
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   342 AA;  38310 MW;  06CB43BEF9D94820 CRC64;
     MEELATKLLA EGIQKKVVSP GKGDLSTFPD GTKVIFHYRS SLCDGTVLDD SRTMGGRSKP
     MELILGKKFK LAVWERVIAT MREGEVADFT CDVKHTALYP LVSQSLRNIS AGKDPLEGQR
     HCCGIAQIHS HHSLGHCDLD KLQANPQPLV FTLELMEVLT PGSFRLDIWA MTDDEKLEVV
     PQIHVEGNAL YKKGDVKEAA EKYHNAIACL KNLQMKERPG DEGWIKLDLM ITPLMLNYCQ
     CQLIQGQYYE VLDHCSSILS KYEDNVKAYF KRAKAHAAVW NETEARADFA KVVELDPSLG
     SSVAKELRAM EERIRSKEKE EKGRYKSLFS YDSNAPATAT TG
//
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