FKBP6_HUMAN
ID FKBP6_HUMAN Reviewed; 327 AA.
AC O75344; B4DXT7; G3V0I2; Q7Z4T4; Q9UDS0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Inactive peptidyl-prolyl cis-trans isomerase FKBP6;
DE Short=Inactive PPIase FKBP6;
DE AltName: Full=36 kDa FK506-binding protein;
DE Short=36 kDa FKBP;
DE Short=FKBP-36;
DE AltName: Full=FK506-binding protein 6;
DE Short=FKBP-6;
DE AltName: Full=Immunophilin FKBP36;
GN Name=FKBP6; Synonyms=FKBP36;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=9782077; DOI=10.1006/geno.1998.5412;
RA Meng X., Lu X., Morris C.A., Keating M.T.;
RT "A novel human gene FKBP6 is deleted in Williams syndrome.";
RL Genomics 52:130-137(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Zan Q., Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP POSSIBLE INVOLVEMENT IN WBS.
RX PubMed=15770126; DOI=10.1097/00019605-200504000-00002;
RA Metcalfe K., Simeonov E., Beckett W., Donnai D., Tassabehji M.;
RT "Autosomal dominant inheritance of Williams-Beuren syndrome in a father and
RT son with haploinsufficiency for FKBP6.";
RL Clin. Dysmorphol. 14:61-65(2005).
RN [8]
RP VARIANT CYS-183, AND POSSIBLE INVOLVEMENT IN AZOOSPERMIA.
RX PubMed=16227348; DOI=10.1093/molehr/gah232;
RA Westerveld G.H., Repping S., Lombardi M.P., van der Veen F.;
RT "Mutations in the chromosome pairing gene FKBP6 are not a common cause of
RT non-obstructive azoospermia.";
RL Mol. Hum. Reprod. 11:673-675(2005).
RN [9]
RP POSSIBLE INVOLVEMENT IN AZOOSPERMIA.
RX PubMed=17307919; DOI=10.1530/rep-06-0125;
RA Zhang W., Zhang S., Xiao C., Yang Y., Zhoucun A.;
RT "Mutation screening of the FKBP6 gene and its association study with
RT spermatogenic impairment in idiopathic infertile men.";
RL Reproduction 133:511-516(2007).
RN [10]
RP INTERACTION WITH HSPA2 AND CLTC.
RX PubMed=18529014; DOI=10.1021/bi8001506;
RA Jarczowski F., Fischer G., Edlich F.;
RT "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.";
RL Biochemistry 47:6946-6952(2008).
RN [11]
RP INTERACTION WITH GAPDH.
RX PubMed=19001379; DOI=10.1074/jbc.m709779200;
RA Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G.,
RA Edlich F.;
RT "FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate
RT dehydrogenase inhibitor.";
RL J. Biol. Chem. 284:766-773(2009).
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 (via TPR repeats) with HSP90 (By similarity).
CC Interacts with HSP72/HSPA2 and CLTC. Interacts with GAPDH; leading to
CC inhibit GAPDH catalytic activity. {ECO:0000250,
CC ECO:0000269|PubMed:18529014, ECO:0000269|PubMed:19001379}.
CC -!- INTERACTION:
CC O75344; P30838: ALDH3A1; NbExp=3; IntAct=EBI-744771, EBI-3905126;
CC O75344; P23560-2: BDNF; NbExp=3; IntAct=EBI-744771, EBI-12275524;
CC O75344; P35520: CBS; NbExp=3; IntAct=EBI-744771, EBI-740135;
CC O75344; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-744771, EBI-11748295;
CC O75344; Q96JB5: CDK5RAP3; NbExp=12; IntAct=EBI-744771, EBI-718818;
CC O75344; P27918: CFP; NbExp=4; IntAct=EBI-744771, EBI-9038570;
CC O75344; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-744771, EBI-739773;
CC O75344; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-744771, EBI-742054;
CC O75344; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-744771, EBI-12000556;
CC O75344; Q16610: ECM1; NbExp=3; IntAct=EBI-744771, EBI-947964;
CC O75344; P29692-2: EEF1D; NbExp=3; IntAct=EBI-744771, EBI-5280572;
CC O75344; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-744771, EBI-744099;
CC O75344; O75344: FKBP6; NbExp=7; IntAct=EBI-744771, EBI-744771;
CC O75344; Q14318: FKBP8; NbExp=2; IntAct=EBI-744771, EBI-724839;
CC O75344; P04406: GAPDH; NbExp=3; IntAct=EBI-744771, EBI-354056;
CC O75344; O15499: GSC2; NbExp=3; IntAct=EBI-744771, EBI-19954058;
CC O75344; Q8IYA8: IHO1; NbExp=8; IntAct=EBI-744771, EBI-8638439;
CC O75344; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-744771, EBI-2556193;
CC O75344; O95678: KRT75; NbExp=3; IntAct=EBI-744771, EBI-2949715;
CC O75344; Q9BRK4: LZTS2; NbExp=7; IntAct=EBI-744771, EBI-741037;
CC O75344; A8MW99: MEI4; NbExp=3; IntAct=EBI-744771, EBI-19944212;
CC O75344; P50222: MEOX2; NbExp=3; IntAct=EBI-744771, EBI-748397;
CC O75344; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-744771, EBI-16439278;
CC O75344; Q9Y5B8: NME7; NbExp=4; IntAct=EBI-744771, EBI-744782;
CC O75344; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-744771, EBI-741158;
CC O75344; P22059: OSBP; NbExp=3; IntAct=EBI-744771, EBI-2681902;
CC O75344; O75928-2: PIAS2; NbExp=5; IntAct=EBI-744771, EBI-348567;
CC O75344; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-744771, EBI-79165;
CC O75344; Q7Z5V6-2: PPP1R32; NbExp=6; IntAct=EBI-744771, EBI-12000762;
CC O75344; Q7L804: RAB11FIP2; NbExp=3; IntAct=EBI-744771, EBI-1049676;
CC O75344; P78317: RNF4; NbExp=3; IntAct=EBI-744771, EBI-2340927;
CC O75344; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-744771, EBI-357085;
CC O75344; G2XKQ0: SUMO1P1; NbExp=6; IntAct=EBI-744771, EBI-10175576;
CC O75344; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-744771, EBI-11139477;
CC O75344; Q9NQ34: TMEM9B; NbExp=3; IntAct=EBI-744771, EBI-724458;
CC O75344; Q8N720: ZNF655; NbExp=3; IntAct=EBI-744771, EBI-625509;
CC O75344; Q3UJD6-2: Usp19; Xeno; NbExp=2; IntAct=EBI-744771, EBI-9359023;
CC O75344; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=6; IntAct=EBI-744771, EBI-6863748;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75344-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75344-2; Sequence=VSP_042038;
CC Name=3;
CC IsoId=O75344-3; Sequence=VSP_054251;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined, with higher
CC expression in testis, heart, skeletal muscle, liver, and kidney.
CC -!- DISEASE: Note=FKBP6 is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region. Haploinsufficiency of FKBP6 may
CC be the cause of certain cardiovascular and musculo-skeletal
CC abnormalities observed in the disease (PubMed:9782077). A father and
CC son with Williams-Beuren syndrome appear to have a common heterozygous
CC deletion that includes FKBP6 gene. However, the haploinsufficiency for
CC FKBP6 does not appear to preclude male fertility (PubMed:15770126).
CC {ECO:0000269|PubMed:15770126, ECO:0000269|PubMed:9782077}.
CC -!- DISEASE: Note=Defects in FKBP6 may be a cause of azoospermia. A study
CC based on 323 patients with azoospermia or severe oligozoospermia
CC suggested an association between FKBP6 variants and azoospermia
CC (PubMed:17307919). However, other studies suggest that defects in FKBP6
CC are not a common cause of non-obstructive azoospermia
CC (PubMed:16227348). {ECO:0000269|PubMed:16227348,
CC ECO:0000269|PubMed:17307919}.
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; AF038847; AAC64249.1; -; mRNA.
DR EMBL; AF447060; AAP97324.1; -; mRNA.
DR EMBL; AK302121; BAG63499.1; -; mRNA.
DR EMBL; BC036817; AAH36817.1; -; mRNA.
DR EMBL; AC005049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471200; EAW69684.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69686.1; -; Genomic_DNA.
DR CCDS; CCDS43595.1; -. [O75344-1]
DR CCDS; CCDS47604.1; -. [O75344-2]
DR CCDS; CCDS64670.1; -. [O75344-3]
DR RefSeq; NP_001128683.1; NM_001135211.2. [O75344-2]
DR RefSeq; NP_001268233.1; NM_001281304.1. [O75344-3]
DR RefSeq; NP_003593.3; NM_003602.4. [O75344-1]
DR PDB; 3B7X; X-ray; 2.10 A; A=12-144.
DR PDBsum; 3B7X; -.
DR AlphaFoldDB; O75344; -.
DR SMR; O75344; -.
DR BioGRID; 114046; 81.
DR IntAct; O75344; 77.
DR STRING; 9606.ENSP00000252037; -.
DR iPTMnet; O75344; -.
DR PhosphoSitePlus; O75344; -.
DR BioMuta; FKBP6; -.
DR MassIVE; O75344; -.
DR MaxQB; O75344; -.
DR PaxDb; O75344; -.
DR PeptideAtlas; O75344; -.
DR PRIDE; O75344; -.
DR ProteomicsDB; 32205; -.
DR ProteomicsDB; 49912; -. [O75344-1]
DR ProteomicsDB; 49913; -. [O75344-2]
DR Antibodypedia; 7933; 277 antibodies from 29 providers.
DR DNASU; 8468; -.
DR Ensembl; ENST00000252037.5; ENSP00000252037.4; ENSG00000077800.13. [O75344-1]
DR Ensembl; ENST00000413573.6; ENSP00000394952.2; ENSG00000077800.13. [O75344-3]
DR Ensembl; ENST00000431982.6; ENSP00000416277.2; ENSG00000077800.13. [O75344-2]
DR GeneID; 8468; -.
DR KEGG; hsa:8468; -.
DR MANE-Select; ENST00000252037.5; ENSP00000252037.4; NM_003602.5; NP_003593.3.
DR UCSC; uc003tya.4; human. [O75344-1]
DR CTD; 8468; -.
DR DisGeNET; 8468; -.
DR GeneCards; FKBP6; -.
DR HGNC; HGNC:3722; FKBP6.
DR HPA; ENSG00000077800; Tissue enriched (testis).
DR MIM; 604839; gene.
DR neXtProt; NX_O75344; -.
DR OpenTargets; ENSG00000077800; -.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA28163; -.
DR VEuPathDB; HostDB:ENSG00000077800; -.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000158514; -.
DR InParanoid; O75344; -.
DR OMA; GCPPRIK; -.
DR OrthoDB; 1465346at2759; -.
DR PhylomeDB; O75344; -.
DR TreeFam; TF354214; -.
DR PathwayCommons; O75344; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; O75344; -.
DR BioGRID-ORCS; 8468; 11 hits in 1068 CRISPR screens.
DR EvolutionaryTrace; O75344; -.
DR GenomeRNAi; 8468; -.
DR Pharos; O75344; Tbio.
DR PRO; PR:O75344; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75344; protein.
DR Bgee; ENSG00000077800; Expressed in left testis and 133 other tissues.
DR ExpressionAtlas; O75344; baseline and differential.
DR Genevisible; O75344; HS.
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:0005528; F:FK506 binding; TAS:ProtInc.
DR GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IMP:AgBase.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm; Differentiation;
KW Meiosis; Nucleus; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis; TPR repeat; Williams-Beuren syndrome.
FT CHAIN 1..327
FT /note="Inactive peptidyl-prolyl cis-trans isomerase FKBP6"
FT /id="PRO_0000075329"
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 VAR_SEQ 1..19
FT /note="MGGSALNQGVLEGDDAPGQ -> MSASSWPQNGMPPS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042038"
FT VAR_SEQ 59..88
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_054251"
FT VARIANT 183
FT /note="R -> C (in dbSNP:rs147213094)"
FT /evidence="ECO:0000269|PubMed:16227348"
FT /id="VAR_070840"
FT CONFLICT 103
FT /note="R -> Q (in Ref. 2; AAP97324)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="C -> S (in Ref. 2; AAP97324)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="E -> K (in Ref. 2; AAP97324)"
FT /evidence="ECO:0000305"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3B7X"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 30..44
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3B7X"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3B7X"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3B7X"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:3B7X"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3B7X"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:3B7X"
SQ SEQUENCE 327 AA; 37214 MW; C137FA629B676623 CRC64;
MGGSALNQGV LEGDDAPGQS LYERLSQRML DISGDRGVLK DVIREGAGDL VAPDASVLVK
YSGYLEHMDR PFDSNYFRKT PRLMKLGEDI TLWGMELGLL SMRRGELARF LFKPNYAYGT
LGCPPLIPPN TTVLFEIELL DFLDCAESDK FCALSAEQQD QFPLQKVLKV AATEREFGNY
LFRQNRFYDA KVRYKRALLL LRRRSAPPEE QHLVEAAKLP VLLNLSFTYL KLDRPTIALC
YGEQALIIDQ KNAKALFRCG QACLLLTEYQ KARDFLVRAQ KEQPFNHDIN NELKKLASCY
RDYVDKEKEM WHRMFAPCGD GSTAGES
