ID H0YWR2_TAEGU Unreviewed; 1245 AA.
AC H0YWR2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=FKBP15 {ECO:0000313|Ensembl:ENSTGUP00000002736.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000002736.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000002736.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000002736.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR AlphaFoldDB; H0YWR2; -.
DR STRING; 59729.ENSTGUP00000002736; -.
DR Ensembl; ENSTGUT00000002764.2; ENSTGUP00000002736.2; ENSTGUG00000002641.2.
DR GeneTree; ENSGT00530000064286; -.
DR HOGENOM; CLU_007194_0_0_1; -.
DR InParanoid; H0YWR2; -.
DR OMA; VALKAHY; -.
DR OrthoDB; 3152232at2759; -.
DR TreeFam; TF328592; -.
DR Proteomes; UP000007754; Chromosome 17.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR44927; FK506-BINDING PROTEIN 15; 1.
DR PANTHER; PTHR44927:SF1; FK506-BINDING PROTEIN 15; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 193..285
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 292..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..790
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 815..870
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 293..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 135335 MW; 27344CE4C7D4C517 CRC64;
MFAAAEEDDA DFLSPASGAR LASLFGLDQT VSNQGNEFFQ FTAPKQPKKG QTAAGQPQKA
PVAASGAPSV LVATAVLAYR YTNGQYLKQG KYGAAVVGNH ATKEYRILLY ISQQQQITSA
RIHPGFVLTV QPNNYSTFYD DQRQNWSIMF ESEKAAVDFS KQVCIAKCNS SPALDSVLCQ
DLLLGEGQGV EGGDSLEVAY TGWLFQNNGL GQVFDSNVNK DKLLRLKLGS GKVIKGWEEG
MLGMKKGGRR FLIIPPAWAY GAQGVAARVP PDSTLAFEVE VRRVKLAKEC SGSDGLSVSS
RDSPAPSPVP SSDGFSSDSG LVPPSTIPPK PGEPAVRAKS NSISEQLANP DVAKAKLISR
MAKMGQPMLP FLAGTAGSQL DSSDSEIEDP NTLRGTTQPV ASTRPSQPAQ AVLPTVSTQV
PQASGAAPSV SSAALIPATI QPHSALPGGA QGFQAYPGVA FAYPQTAASA SQLQPVGQMY
PAPYQAPGDV TSFLMTEARQ HNTEIRLAVS KVVDKMDHLA AKVEELKKQS TANSSLLPGI
SSVTMEASMI MSNIQRIIQE NERLKQEIFE KSSRIEEQNE KISELIERNQ RYVEQSNLLM
EQRNHSLQTT NENTQARVLH AEQEKHMLPV DRGWDQAKVA EELAAATAQV SQLQLELTAH
QKKEMDLRKQ LSCAVQDAER QEAQLNKLQA QVAELQEASQ DTRSRFKAEK QSRKQLDMKI
AALEEELTDL RVEKETLERN LAERKKKSLS ERAQAEEEME EIRRSHQQEL DKLRQLLKKA
RTSTDQAAAE QLSVIQAELE SQCEAKCERA LASAREQHAR QCQELCEQRD SLQHQLAQLE
EKLTALKHSK KAEEQKLSEA QQRLEELEPI QEKYSALQAD VGVLRARYEE QIRELQKDQD
GSSPADYTEQ VKKIMNGVFQ SLRGEFELDE MYSGRTVLGV VMNTIKTVTL QLLNRQQEKP
EHGSENEESG TGAGRQEGSP GAKTEHREPL QHSPAHSTAD PGEETRGCLQ PEQQGQAAPH
PAGPRAPEEE QETQSTEVAE EEKVQEEHLP PAADCSLDAE KGPELAGQPV PGLEQRLEGA
PIGQADPEQD PSAVSLQAAA AEPSVPGAKP GEVDEAALPA QTAVEQKAEE AGGGLEPPPL
NGEEGSGTEP WDGAGSEQER ASVSSRAEPG SAVLGEAPGS QEHSPRHTDS SLFEDDNFFE
TASPKPLKPQ VPSEEEDEEE VSMKGRPPPA PLFGDDDDDD LDWLG
//
