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Database: UniProt
Entry: A0A2K6BQS3_MACNE
LinkDB: A0A2K6BQS3_MACNE
Original site: A0A2K6BQS3_MACNE 
ID   A0A2K6BQS3_MACNE        Unreviewed;       456 AA.
AC   A0A2K6BQS3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   Name=FKBP8 {ECO:0000313|Ensembl:ENSMNEP00000013735.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000013735.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000013735.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR   AlphaFoldDB; A0A2K6BQS3; -.
DR   STRING; 9545.ENSMNEP00000013735; -.
DR   Ensembl; ENSMNET00000037936.1; ENSMNEP00000013735.1; ENSMNEG00000031077.1.
DR   GeneTree; ENSGT00940000156705; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000031077; Expressed in temporal lobe and 12 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0070585; P:protein localization to mitochondrion; IEA:Ensembl.
DR   GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:Ensembl.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46512:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP8; 1.
DR   PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   DOMAIN          120..205
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REPEAT          307..340
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  49091 MW;  091B16DA30EFA71C CRC64;
     MASCAEPSEP SAPLPAGVPP LEDFEVLDGV EDAEGEEEEE EEEEEEDDLS ELPPLEDMGQ
     PPVEEAEQPG ALAREFLAAM EPEPAPAPAP EEWLDILGNG LLRKKTLVPG PPGSSRPVKG
     QVVTVHLQTS LENGTRVQEE PELVFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG
     PQGSRSPYIP PHAALCLEVT LKTAVDGPDL EMLTGQERVA LANRKRECGN AHYQRADFVL
     AANSYDLAIK AITSSAKVDM TFEEEAQLLQ LKVKCLNNLA ASQLKLDHYR AALRSCSLVL
     EHQPDNIKAL FRKGKVLAQQ GEYSEAIPIL RAALKLEPSN KTIHAELSKL VKKHAAQRST
     ETALYRKMLG NPSRLPAKCP GKGAWVSWGT EWAGAACRAS LPEGFYFAYM NVLGDWAILG
     DAGDMEKAQP CVIMSGVEGG IQAGGLRVGN GASSRA
//
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