FKBP7_HUMAN
ID FKBP7_HUMAN Reviewed; 222 AA.
AC Q9Y680; Q4ZG70; Q6V3B2; Q86U65; Q96DA4; Q9Y6B0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP7;
DE Short=PPIase FKBP7;
DE EC=5.2.1.8;
DE AltName: Full=23 kDa FK506-binding protein;
DE Short=23 kDa FKBP;
DE Short=FKBP-23;
DE AltName: Full=FK506-binding protein 7;
DE Short=FKBP-7;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP7; Synonyms=FKBP23; ORFNames=UNQ670/PRO1304;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Pituitary, and Pituitary tumor;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovial cell;
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 MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Li H., Zhong G., Yu R., Shen C., Zhou G., Li M., Xiao W., Lin L., Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
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;
CC -!- INTERACTION:
CC Q9Y680; O95870: ABHD16A; NbExp=3; IntAct=EBI-3918971, EBI-348517;
CC Q9Y680; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-3918971, EBI-10827839;
CC Q9Y680; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-3918971, EBI-541426;
CC Q9Y680; P05090: APOD; NbExp=3; IntAct=EBI-3918971, EBI-715495;
CC Q9Y680; Q12797-6: ASPH; NbExp=3; IntAct=EBI-3918971, EBI-12092171;
CC Q9Y680; O95393: BMP10; NbExp=3; IntAct=EBI-3918971, EBI-3922513;
CC Q9Y680; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-3918971, EBI-12244618;
CC Q9Y680; O14735: CDIPT; NbExp=3; IntAct=EBI-3918971, EBI-358858;
CC Q9Y680; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-3918971, EBI-12261896;
CC Q9Y680; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-3918971, EBI-752069;
CC Q9Y680; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3918971, EBI-12256978;
CC Q9Y680; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-3918971, EBI-517508;
CC Q9Y680; Q92520: FAM3C; NbExp=3; IntAct=EBI-3918971, EBI-2876774;
CC Q9Y680; O95363: FARS2; NbExp=3; IntAct=EBI-3918971, EBI-2513774;
CC Q9Y680; O43681: GET3; NbExp=3; IntAct=EBI-3918971, EBI-2515857;
CC Q9Y680; Q99525: H4C7; NbExp=3; IntAct=EBI-3918971, EBI-10294329;
CC Q9Y680; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-3918971, EBI-5916693;
CC Q9Y680; C9JCN9: HSBP1L1; NbExp=3; IntAct=EBI-3918971, EBI-2685549;
CC Q9Y680; P46695: IER3; NbExp=3; IntAct=EBI-3918971, EBI-1748945;
CC Q9Y680; Q01628: IFITM3; NbExp=3; IntAct=EBI-3918971, EBI-7932862;
CC Q9Y680; Q8TAC2: JOSD2; NbExp=3; IntAct=EBI-3918971, EBI-12205593;
CC Q9Y680; O43561-2: LAT; NbExp=3; IntAct=EBI-3918971, EBI-8070286;
CC Q9Y680; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-3918971, EBI-12243024;
CC Q9Y680; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-3918971, EBI-11988931;
CC Q9Y680; Q6IN84: MRM1; NbExp=3; IntAct=EBI-3918971, EBI-5454865;
CC Q9Y680; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-3918971, EBI-725252;
CC Q9Y680; Q9Y5X5-3: NPFFR2; NbExp=3; IntAct=EBI-3918971, EBI-18076879;
CC Q9Y680; Q9NX40: OCIAD1; NbExp=3; IntAct=EBI-3918971, EBI-2683029;
CC Q9Y680; Q96HP4: OXNAD1; NbExp=3; IntAct=EBI-3918971, EBI-2862111;
CC Q9Y680; Q96AL5: PBX3; NbExp=3; IntAct=EBI-3918971, EBI-741171;
CC Q9Y680; P49585: PCYT1A; NbExp=3; IntAct=EBI-3918971, EBI-2563309;
CC Q9Y680; P40855: PEX19; NbExp=3; IntAct=EBI-3918971, EBI-594747;
CC Q9Y680; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-3918971, EBI-11721828;
CC Q9Y680; Q59EV6: PPGB; NbExp=3; IntAct=EBI-3918971, EBI-14210385;
CC Q9Y680; P30405: PPIF; NbExp=3; IntAct=EBI-3918971, EBI-5544229;
CC Q9Y680; O75127: PTCD1; NbExp=3; IntAct=EBI-3918971, EBI-2560233;
CC Q9Y680; P43378: PTPN9; NbExp=3; IntAct=EBI-3918971, EBI-742898;
CC Q9Y680; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-3918971, EBI-3232108;
CC Q9Y680; Q9NS64: RPRM; NbExp=3; IntAct=EBI-3918971, EBI-1052363;
CC Q9Y680; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3918971, EBI-8636004;
CC Q9Y680; O43765: SGTA; NbExp=6; IntAct=EBI-3918971, EBI-347996;
CC Q9Y680; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-3918971, EBI-10314552;
CC Q9Y680; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-3918971, EBI-5235586;
CC Q9Y680; Q13596: SNX1; NbExp=3; IntAct=EBI-3918971, EBI-2822329;
CC Q9Y680; Q9UMY4-1: SNX12; NbExp=3; IntAct=EBI-3918971, EBI-22419305;
CC Q9Y680; O15400: STX7; NbExp=3; IntAct=EBI-3918971, EBI-3221827;
CC Q9Y680; Q9UNK0: STX8; NbExp=3; IntAct=EBI-3918971, EBI-727240;
CC Q9Y680; Q9P2R7: SUCLA2; NbExp=3; IntAct=EBI-3918971, EBI-2269898;
CC Q9Y680; Q9BW92: TARS2; NbExp=3; IntAct=EBI-3918971, EBI-1045099;
CC Q9Y680; Q8WY91: THAP4; NbExp=3; IntAct=EBI-3918971, EBI-726691;
CC Q9Y680; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-3918971, EBI-17192156;
CC Q9Y680; Q6UXF1: TMEM108; NbExp=3; IntAct=EBI-3918971, EBI-7100456;
CC Q9Y680; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-3918971, EBI-10171534;
CC Q9Y680; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-3918971, EBI-12195227;
CC Q9Y680; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-3918971, EBI-11528917;
CC Q9Y680; Q969K7: TMEM54; NbExp=3; IntAct=EBI-3918971, EBI-3922833;
CC Q9Y680; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-3918971, EBI-12015604;
CC Q9Y680; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-3918971, EBI-2548832;
CC Q9Y680; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-3918971, EBI-12111910;
CC Q9Y680; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-3918971, EBI-11996766;
CC Q9Y680; O60636: TSPAN2; NbExp=3; IntAct=EBI-3918971, EBI-3914288;
CC Q9Y680; P49638: TTPA; NbExp=3; IntAct=EBI-3918971, EBI-10210710;
CC Q9Y680; O95881: TXNDC12; NbExp=3; IntAct=EBI-3918971, EBI-2564581;
CC Q9Y680; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-3918971, EBI-2819725;
CC Q9Y680; O75841: UPK1B; NbExp=3; IntAct=EBI-3918971, EBI-12237619;
CC Q9Y680; Q8IW00: VSTM4; NbExp=3; IntAct=EBI-3918971, EBI-4311759;
CC Q9Y680; Q14508: WFDC2; NbExp=3; IntAct=EBI-3918971, EBI-723529;
CC Q9Y680; Q9Y4P8-4: WIPI2; NbExp=3; IntAct=EBI-3918971, EBI-12205107;
CC Q9Y680; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-3918971, EBI-751210;
CC Q9Y680; O95159: ZFPL1; NbExp=3; IntAct=EBI-3918971, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=Q9Y680-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9Y680-3; Sequence=VSP_041018;
CC Name=1;
CC IsoId=Q9Y680-1; Sequence=VSP_059387, VSP_059388;
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds calcium. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF092137; AAD40379.1; -; mRNA.
DR EMBL; AF100751; AAD43015.1; ALT_FRAME; mRNA.
DR EMBL; AY359015; AAQ89374.1; -; mRNA.
DR EMBL; AK292145; BAF84834.1; -; mRNA.
DR EMBL; BT007122; AAP35786.1; -; mRNA.
DR EMBL; AY353086; AAQ57208.1; -; mRNA.
DR EMBL; AC009948; AAX88883.1; -; Genomic_DNA.
DR EMBL; BC009711; AAH09711.1; -; mRNA.
DR CCDS; CCDS2280.1; -. [Q9Y680-2]
DR CCDS; CCDS46462.1; -. [Q9Y680-3]
DR RefSeq; NP_001128684.1; NM_001135212.1. [Q9Y680-3]
DR RefSeq; NP_851939.1; NM_181342.2. [Q9Y680-2]
DR AlphaFoldDB; Q9Y680; -.
DR SMR; Q9Y680; -.
DR BioGRID; 119666; 111.
DR IntAct; Q9Y680; 85.
DR MINT; Q9Y680; -.
DR STRING; 9606.ENSP00000413152; -.
DR GlyGen; Q9Y680; 1 site.
DR iPTMnet; Q9Y680; -.
DR MetOSite; Q9Y680; -.
DR PhosphoSitePlus; Q9Y680; -.
DR BioMuta; FKBP7; -.
DR DMDM; 23396602; -.
DR EPD; Q9Y680; -.
DR jPOST; Q9Y680; -.
DR MassIVE; Q9Y680; -.
DR MaxQB; Q9Y680; -.
DR PeptideAtlas; Q9Y680; -.
DR PRIDE; Q9Y680; -.
DR ProteomicsDB; 86619; -. [Q9Y680-1]
DR ProteomicsDB; 86620; -. [Q9Y680-2]
DR ProteomicsDB; 86621; -. [Q9Y680-3]
DR Antibodypedia; 2249; 172 antibodies from 24 providers.
DR DNASU; 51661; -.
DR Ensembl; ENST00000233092.10; ENSP00000233092.6; ENSG00000079150.19. [Q9Y680-1]
DR Ensembl; ENST00000424785.7; ENSP00000413152.2; ENSG00000079150.19. [Q9Y680-2]
DR Ensembl; ENST00000434643.6; ENSP00000415486.2; ENSG00000079150.19. [Q9Y680-3]
DR Ensembl; ENST00000470945.2; ENSP00000510163.1; ENSG00000079150.19. [Q9Y680-1]
DR GeneID; 51661; -.
DR KEGG; hsa:51661; -.
DR MANE-Select; ENST00000424785.7; ENSP00000413152.2; NM_181342.3; NP_851939.1.
DR UCSC; uc002umk.4; human. [Q9Y680-2]
DR CTD; 51661; -.
DR DisGeNET; 51661; -.
DR GeneCards; FKBP7; -.
DR HGNC; HGNC:3723; FKBP7.
DR HPA; ENSG00000079150; Tissue enhanced (ovary).
DR MIM; 607062; gene.
DR neXtProt; NX_Q9Y680; -.
DR OpenTargets; ENSG00000079150; -.
DR PharmGKB; PA28164; -.
DR VEuPathDB; HostDB:ENSG00000079150; -.
DR GeneTree; ENSGT00940000159964; -.
DR HOGENOM; CLU_013615_5_0_1; -.
DR InParanoid; Q9Y680; -.
DR OMA; FFYVWGI; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q9Y680; -.
DR TreeFam; TF105296; -.
DR PathwayCommons; Q9Y680; -.
DR SignaLink; Q9Y680; -.
DR BioGRID-ORCS; 51661; 6 hits in 1082 CRISPR screens.
DR ChiTaRS; FKBP7; human.
DR GenomeRNAi; 51661; -.
DR Pharos; Q9Y680; Tbio.
DR PRO; PR:Q9Y680; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y680; protein.
DR Bgee; ENSG00000079150; Expressed in stromal cell of endometrium and 156 other tissues.
DR ExpressionAtlas; Q9Y680; baseline and differential.
DR Genevisible; Q9Y680; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005528; F:FK506 binding; ISS:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:FlyBase.
DR GO; GO:0018208; P:peptidyl-proline modification; ISS:FlyBase.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Isomerase; Metal-binding; Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..222
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP7"
FT /id="PRO_0000025513"
FT DOMAIN 53..145
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 145..180
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 189..222
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 200..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..222
FT /note="Retention in the endoplasmic reticulum"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 125..127
FT /note="AEG -> GST (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_059387"
FT VAR_SEQ 125
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041018"
FT VAR_SEQ 128..222
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_059388"
FT CONFLICT 124
FT /note="Y -> H (in Ref. 1; AAD40379)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> M (in Ref. 5; AAQ57208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25794 MW; 362957BAD3C5C2A6 CRC64;
MPKTMHFLFR FIVFFYLWGL FTAQRQKKEE STEEVKIEVL HRPENCSKTS KKGDLLNAHY
DGYLAKDGSK FYCSRTQNEG HPKWFVLGVG QVIKGLDIAM TDMCPGEKRK VVIPPSFAYG
KEGYAEGKIP PDATLIFEIE LYAVTKGPRS IETFKQIDMD NDRQLSKAEI NLYLQREFEK
DEKPRDKSYQ DAVLEDIFKK NDHDGDGFIS PKEYNVYQHD EL
