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   27-MAR-2024, entry version 197.
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; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-3918971, EBI-311394;
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; 114.
DR   IntAct; Q9Y680; 87.
DR   MINT; Q9Y680; -.
DR   STRING; 9606.ENSP00000413152; -.
DR   GlyCosmos; Q9Y680; 1 site, No reported glycans.
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   PaxDb; 9606-ENSP00000413152; -.
DR   PeptideAtlas; Q9Y680; -.
DR   ProteomicsDB; 86619; -. [Q9Y680-1]
DR   ProteomicsDB; 86620; -. [Q9Y680-2]
DR   ProteomicsDB; 86621; -. [Q9Y680-3]
DR   Pumba; Q9Y680; -.
DR   Antibodypedia; 2249; 198 antibodies from 25 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   AGR; HGNC:3723; -.
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; 25281at2759; -.
DR   PhylomeDB; Q9Y680; -.
DR   TreeFam; TF105296; -.
DR   PathwayCommons; Q9Y680; -.
DR   SignaLink; Q9Y680; -.
DR   BioGRID-ORCS; 51661; 6 hits in 1162 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q9Y680; baseline and differential.
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   Gene3D; 1.10.238.10; EF-hand; 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   PANTHER; PTHR46222:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP7; 1.
DR   PANTHER; PTHR46222; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP7/14; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF54534; FKBP-like; 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.
DR   Genevisible; Q9Y680; HS.
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
//