ID   FKBP9_HUMAN    STANDARD;      PRT;   517 AA.
AC   O95302; Q96EX5; Q96IJ9;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   13-SEP-2005 (Rel. 48, Last annotation update)
DE   FK506 binding protein 9 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans
DE   isomerase) (PPIase) (Rotamase) (Fragment).
GN   Name=FKBP9; Synonyms=FKBP60, FKBP63;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 320-517.
RC   TISSUE=Kidney, and Muscle;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [3]
RP   CARBOHYDRATE-LINKAGE SITES ASN-121; ASN-233 AND ASN-344.
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; AF089745; AAC78853.1; -; mRNA.
DR   EMBL; BC007443; AAH07443.2; -; mRNA.
DR   EMBL; BC011872; AAH11872.1; ALT_INIT; mRNA.
DR   HSSP; P20081; 1YAT.
DR   Ensembl; ENSG00000122642; Homo sapiens.
DR   Genew; HGNC:3725; FKBP9.
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; IPR002048; EF-hand.
DR   InterPro; IPR010983; EF_Hand_like.
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; Calcium-binding; Endoplasmic reticulum; Glycoprotein;
KW   Isomerase; Phosphorylation; Repeat; Rotamase.
FT   DOMAIN       <1     89       PPIase FKBP-type 1.
FT   DOMAIN      113    201       PPIase FKBP-type 2.
FT   DOMAIN      225    312       PPIase FKBP-type 3.
FT   DOMAIN      336    424       PPIase FKBP-type 4.
FT   DOMAIN      435    470       EF-hand 1.
FT   DOMAIN      480    515       EF-hand 2.
FT   CA_BIND     448    459       1 (Potential).
FT   CA_BIND     493    504       2 (Potential).
FT   MOTIF       514    517       Prevents secretion from ER (Potential).
FT   CARBOHYD    121    121       N-linked (GlcNAc...).
FT   CARBOHYD    233    233       N-linked (GlcNAc...).
FT   CARBOHYD    249    249       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    344    344       N-linked (GlcNAc...).
FT   CONFLICT    514    514       H -> Q (in Ref. 2; AAH11872).
FT   NON_TER       1      1
SQ   SEQUENCE   517 AA;  57220 MW;  704FB0CE9C44C74B CRC64;
     GDFVRYHYVG TFPDGQKFDS SYDRDSTFNV FVGKGQLITG MDQALVGMCV NERRFVKIPP
     KLAYGNEGVS GVIPPNSVLH FDVLLMDIWN SEDQVQIHTY FKPPSCPRTI QVSDFVRYHY
     NGTFLDGTLF DSSHNRMKTY DTYVGIGWLI PGMDKGLLGM CVGEKRIITI PPFLAYGEDG
     DGKDIPGQAS LVFDVALLDL HNPKDSISIE NKVVPENCER ISQSGDFLRY HYNGTLLDGT
     LFDSSYSRNR TFDTYIGQGY VIPGMDEGLL GVCIGEKRRI VVPPHLGYGE EGRGNIPGSA
     VLVFDIHVID FHNPSDSISI TSHYKPPDCS VLSKKGDYLK YHYNASLLDG TLLDSTWNLG
     KTYNIVLGSG QVVLGMDMGL REMCVGEKRT VIIPPHLGYG EAGVDGEVPG SAVLVFDIEL
     LELVAGLPEG YMFIWNGEVS PNLFEEIDKD GNGEVLLEEF SEYIHAQVAS GKGKLAPGFD
     AELIVKNMFT NQDRNGDGKV TAEEFKLKDQ EAKHDEL
//