ID FKBP7_HUMAN Reviewed; 259 AA. AC Q9Y680; Q86U65; Q96DA4; Q9Y6B0; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-OCT-2009, entry version 87. DE RecName: Full=FK506-binding protein 7; DE EC=5.2.1.8; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE Short=Rotamase; DE AltName: Full=FKBP-23; DE Flags: Precursor; GN Name=FKBP7; Synonyms=FKBP23; ORFNames=UNQ670/PRO1304; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Pituitary tumor; RA Guan Z., Zhang Q., Dai M., Song H., Mao Y., Wu X., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human FK506-binding protein (FKBP23)-isoform gene."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Pituitary; RA Han Z., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human FK506-binding protein mRNA, complete cds."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX MEDLINE=22887296; 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). 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 RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: PPIases accelerate the folding of proteins during CC protein synthesis. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y680-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y680-2; Sequence=VSP_005187; CC -!- PTM: Glycosylated (By similarity). CC -!- MISCELLANEOUS: Binds calcium (By similarity). CC -!- SIMILARITY: Contains 2 EF-hand domains. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF100751; AAD43015.1; -; mRNA. DR EMBL; AF092137; AAD40379.1; -; mRNA. DR EMBL; AY359015; AAQ89374.1; -; mRNA. DR EMBL; BT007122; AAP35786.1; -; mRNA. DR EMBL; BC009711; AAH09711.1; -; mRNA. DR IPI; IPI00001914; -. DR IPI; IPI00218686; -. DR RefSeq; NP_001128684.1; -. DR RefSeq; NP_851939.1; -. DR UniGene; Hs.410378; -. DR UniGene; Hs.645700; -. DR HSSP; Q02790; 1N1A. DR STRING; Q9Y680; -. DR PRIDE; Q9Y680; -. DR Ensembl; ENST00000233092; ENSP00000233092; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000350591; ENSP00000335194; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000412118; ENSP00000394068; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000412612; ENSP00000389914; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000419184; ENSP00000398869; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000424785; ENSP00000413152; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000434643; ENSP00000415486; ENSG00000079150; Homo sapiens. DR Ensembl; ENST00000435079; ENSP00000403801; ENSG00000079150; Homo sapiens. DR GeneID; 51661; -. DR KEGG; hsa:51661; -. DR UCSC; uc002umk.1; human. DR CTD; 51661; -. DR GeneCards; GC02M179038; -. DR H-InvDB; HIX0002629; -. DR HGNC; HGNC:3723; FKBP7. DR HPA; HPA008707; -. DR MIM; 607062; gene. DR PharmGKB; PA28164; -. DR HOGENOM; Q9Y680; -. DR HOVERGEN; Q9Y680; -. DR BRENDA; 5.2.1.8; 247. DR NextBio; 55642; -. DR ArrayExpress; Q9Y680; -. DR Bgee; Q9Y680; -. DR CleanEx; HS_FKBP7; -. DR Genevestigator; Q9Y680; -. DR GermOnline; ENSG00000079150; Homo sapiens. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR InterPro; IPR018247; EF_HAND_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR InterPro; IPR000886; ER_target_seq_motif. DR InterPro; IPR001179; PPIase_FKBP. DR PANTHER; PTHR10516; PPIase_FKBP; 1. DR Pfam; PF00254; FKBP_C; 1. DR SMART; SM00054; EFh; 2. 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; Complete proteome; KW Endoplasmic reticulum; Glycoprotein; Isomerase; Repeat; Rotamase; KW Signal. FT SIGNAL 1 23 Potential. FT CHAIN 24 259 FK506-binding protein 7. FT /FTId=PRO_0000025513. FT DOMAIN 53 182 PPIase FKBP-type. FT DOMAIN 182 217 EF-hand 1. FT DOMAIN 226 259 EF-hand 2. FT CA_BIND 195 206 1 (Potential). FT CA_BIND 239 250 2 (Potential). FT MOTIF 256 259 Prevents secretion from ER (Potential). FT CARBOHYD 45 45 N-linked (GlcNAc...) (Potential). FT CARBOHYD 158 158 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 125 161 Missing (in isoform 2). FT /FTId=VSP_005187. FT CONFLICT 124 124 Y -> H (in Ref. 2). SQ SEQUENCE 259 AA; 30009 MW; 886A1F3F5ACB9E78 CRC64; MPKTMHFLFR FIVFFYLWGL FTAQRQKKEE STEEVKIEVL HRPENCSKTS KKGDLLNAHY DGYLAKDGSK FYCSRTQNEG HPKWFVLGVG QVIKGLDIAM TDMCPGEKRK VVIPPSFAYG KEGYGSLEEV FLLQNILVSC HRTTLHVLKC MYLLVLNNNT CAEGKIPPDA TLIFEIELYA VTKGPRSIET FKQIDMDNDR QLSKAEINLY LQREFEKDEK PRDKSYQDAV LEDIFKKNDH DGDGFISPKE YNVYQHDEL //