FKBP6_RAT
ID FKBP6_RAT Reviewed; 327 AA.
AC D3ZQF4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Inactive peptidyl-prolyl cis-trans isomerase FKBP6;
DE Short=Inactive PPIase FKBP6;
DE AltName: Full=36 kDa FK506-binding protein;
DE AltName: Full=FK506-binding protein 6;
DE AltName: Full=Immunophilin FKBP36;
GN Name=Fkbp6; Synonyms=As, Fkbp36;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISEASE.
RX PubMed=12764197; DOI=10.1126/science.1083022;
RA Crackower M.A., Kolas N.K., Noguchi J., Sarao R., Kikuchi K., Kaneko H.,
RA Kobayashi E., Kawai Y., Kozieradzki I., Landers R., Mo R., Hui C.C.,
RA Nieves E., Cohen P.E., Osborne L.R., Wada T., Kunieda T., Moens P.B.,
RA Penninger J.M.;
RT "Essential role of Fkbp6 in male fertility and homologous chromosome
RT pairing in meiosis.";
RL Science 300:1291-1295(2003).
CC -!- FUNCTION: Co-chaperone required during spermatogenesis to repress
CC transposable elements and prevent their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC govern the methylation and subsequent repression of transposons. Acts
CC as a co-chaperone via its interaction with HSP90 and is required for
CC the piRNA amplification process, the secondary piRNA biogenesis. May be
CC required together with HSP90 in removal of 16 nucleotide ping-pong by-
CC products from Piwi complexes, possibly facilitating turnover of Piwi
CC complexes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HSP72/HSPA2 and CLTC. Interacts with GAPDH;
CC leading to inhibit GAPDH catalytic activity. Interacts (via TPR
CC repeats) with HSP90 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}. Chromosome {ECO:0000250}. Note=Does not localize to pi-
CC bodies. Localizes to meiotic chromosome cores and regions of homologous
CC chromosome synapsis (By similarity). {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Fkbp6 are the cause of spontaneous male
CC sterile mutant 'As'. Males are sterile and aspermic due to abnormal
CC pairing and misalignments between homologous chromosomes, non-
CC homologous partner switches, and autosynapsis of X chromosome cores in
CC meiotic spermatocytes (PubMed:12764197). {ECO:0000269|PubMed:12764197}.
CC -!- SIMILARITY: Belongs to the FKBP6 family. {ECO:0000305}.
CC -!- CAUTION: Although it contains a PPIase FKBP-type domain, does not show
CC peptidyl-prolyl cis-trans isomerase activity. {ECO:0000305}.
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DR EMBL; AABR06071167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13376.1; -; Genomic_DNA.
DR EMBL; CH473973; EDM13377.1; -; Genomic_DNA.
DR RefSeq; NP_001099392.1; NM_001105922.1.
DR RefSeq; XP_008767352.1; XM_008769130.2.
DR RefSeq; XP_017453788.1; XM_017598299.1.
DR AlphaFoldDB; D3ZQF4; -.
DR SMR; D3ZQF4; -.
DR STRING; 10116.ENSRNOP00000001971; -.
DR PaxDb; D3ZQF4; -.
DR Ensembl; ENSRNOT00000001971; ENSRNOP00000001971; ENSRNOG00000001451.
DR GeneID; 288597; -.
DR KEGG; rno:288597; -.
DR UCSC; RGD:1308926; rat.
DR CTD; 8468; -.
DR RGD; 1308926; Fkbp6.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000158514; -.
DR HOGENOM; CLU_013615_13_2_1; -.
DR InParanoid; D3ZQF4; -.
DR OMA; GCPPRIK; -.
DR OrthoDB; 1465346at2759; -.
DR PhylomeDB; D3ZQF4; -.
DR TreeFam; TF354214; -.
DR PRO; PR:D3ZQF4; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001451; Expressed in testis and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:RGD.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR042282; FKBP6/shu.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46674; PTHR46674; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Chromosome; Cytoplasm; Differentiation; Meiosis; Nucleus;
KW Reference proteome; Repeat; RNA-mediated gene silencing; Spermatogenesis;
KW TPR repeat.
FT CHAIN 1..327
FT /note="Inactive peptidyl-prolyl cis-trans isomerase FKBP6"
FT /id="PRO_0000428726"
FT DOMAIN 54..143
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 171..204
FT /note="TPR 1"
FT REPEAT 219..252
FT /note="TPR 2"
FT REPEAT 253..286
FT /note="TPR 3"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 37455 MW; 0E68789E4E93FADC CRC64;
MSVFSRLRNG IPPSRDDCQS PYERLSQRML DISGDRGVLK DIIREGAGDP VTPDASVLVK
YSGYLEHMDK PFDSNCFRKT PRLMKLGEDI TLWGMELGLL SMRRGELARF LFKPTYAYGT
LGCPPLIPPN ATVLFEIELI DFLDSAESDK FCALSAEQQE QFPLQKVLKV AATEREFGNY
LFRQNRFCDA KVRYKRALLL LHRRLAICEE QHLVEPAELL VLLNLSFVYL KLDRPAMALR
YGEQALLIDK RNAKALFRCG QACLLLTEYE QARDFLVRAQ KEQPCNHDIN NELKKLSSHY
RDYVDREREM CHRMFAPCGS GSSVGGN
