ID FKBP9_HUMAN STANDARD; PRT; 570 AA. AC O95302; Q3MIR7; Q6IN76; Q6P2N1; Q96EX5; Q96IJ9; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 03-OCT-2006, entry version 54. DE FK506-binding protein 9 precursor (EC 5.2.1.8) (Peptidyl-prolyl cis- DE trans isomerase) (PPIase) (Rotamase). GN Name=FKBP9; Synonyms=FKBP60, FKBP63; 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 [LARGE SCALE MRNA]. RC TISSUE=Kidney, Liver, Lung, Muscle, and PNS; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-570. RX MEDLINE=99453729; PubMed=10524204; DOI=10.1016/S0167-4781(99)00080-9; RA Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S.; RT "Biochemical analysis of mouse FKBP60, a novel member of the FKPB RT family."; RL Biochim. Biophys. Acta 1446:295-307(1999). RN [3] RP GLYCOSYLATION AT ASN-174; ASN-286 AND ASN-397. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). CC -!- FUNCTION: PPIases accelerate the folding of proteins during CC protein synthesis. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by FK506 (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). CC -!- PTM: Phosphorylated (By similarity). CC -!- SIMILARITY: Contains 2 EF-hand domains. CC -!- SIMILARITY: Contains 4 PPIase FKBP-type domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC007443; AAH07443.2; -; mRNA. DR EMBL; BC011872; AAH11872.1; ALT_INIT; mRNA. DR EMBL; BC064418; AAH64418.1; -; mRNA. DR EMBL; BC072422; AAH72422.1; -; mRNA. DR EMBL; BC101723; AAI01724.1; -; mRNA. DR EMBL; AF089745; AAC78853.1; -; mRNA. DR UniGene; Hs.575466; -. DR HSSP; P20081; 1YAT. DR Ensembl; ENSG00000122642; Homo sapiens. DR KEGG; hsa:11328; -. DR HGNC; HGNC:3725; FKBP9. DR ArrayExpress; O95302; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS. DR GO; GO:0005509; F:calcium ion binding; ISS. DR GO; GO:0006457; P:protein folding; ISS. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR InterPro; IPR000886; ER_target_S. DR InterPro; IPR001179; FKBP_PPIase. DR Pfam; PF00036; efhand; 2. DR Pfam; PF00254; FKBP_C; 4. DR SMART; SM00054; EFh; 2. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS50059; FKBP_PPIASE; 4. KW Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; KW Phosphorylation; Repeat; Rotamase; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 570 FK506-binding protein 9. FT /FTId=PRO_0000045760. FT DOMAIN 54 142 PPIase FKBP-type 1. FT DOMAIN 166 254 PPIase FKBP-type 2. FT DOMAIN 278 365 PPIase FKBP-type 3. FT DOMAIN 389 477 PPIase FKBP-type 4. FT DOMAIN 488 523 EF-hand 1. FT DOMAIN 533 568 EF-hand 2. FT CA_BIND 501 513 1 (Potential). FT CA_BIND 546 557 2 (Potential). FT MOTIF 567 570 Prevents secretion from ER (Potential). FT CARBOHYD 174 174 N-linked (GlcNAc...). FT CARBOHYD 286 286 N-linked (GlcNAc...). FT CARBOHYD 302 302 N-linked (GlcNAc...) (Potential). FT CARBOHYD 397 397 N-linked (GlcNAc...). FT CONFLICT 567 567 H -> Q (in Ref. 1; AAH11872). SQ SEQUENCE 570 AA; 63084 MW; E1F44A2FA6E112F8 CRC64; MAFRGWRPPP PPLLLLLLWV TGQAAPVAGL GSDAELQIER RFVPDECPRT VRSGDFVRYH YVGTFPDGQK FDSSYDRDST FNVFVGKGQL ITGMDQALVG MCVNERRFVK IPPKLAYGNE GVSGVIPPNS VLHFDVLLMD IWNSEDQVQI HTYFKPPSCP RTIQVSDFVR YHYNGTFLDG TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITIPPFLAYG EDGDGKDIPG QASLVFDVAL LDLHNPKDSI SIENKVVPEN CERISQSGDF LRYHYNGTLL DGTLFDSSYS RNRTFDTYIG QGYVIPGMDE GLLGVCIGEK RRIVVPPHLG YGEEGRGNIP GSAVLVFDIH VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVAGL PEGYMFIWNG EVSPNLFEEI DKDGNGEVLL EEFSEYIHAQ VASGKGKLAP GFDAELIVKN MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL //