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Peptidyl-prolyl cis-trans isomerase FKBP9 (PPIase FKBP9) (EC 5.2.1.8) (63 kDa FK506-binding protein) (63 kDa FKBP) (FKBP-63) (FK506-binding protein 9) (FKBP-9) (FKBP65RS) (Rotamase)

 FKBP9_MOUSE             Reviewed;         570 AA.
Q9Z247; Q80ZZ6; Q8R386; Q9CVM0; Q9JHX5;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-FEB-2018, entry version 147.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP9;
Short=PPIase FKBP9;
EC=5.2.1.8;
AltName: Full=63 kDa FK506-binding protein;
Short=63 kDa FKBP;
Short=FKBP-63;
AltName: Full=FK506-binding protein 9;
Short=FKBP-9;
AltName: Full=FKBP65RS;
AltName: Full=Rotamase;
Flags: Precursor;
Name=Fkbp9; Synonyms=Fkbp60, Fkbp63;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND CALCIUM-BINDING.
PubMed=10524204; DOI=10.1016/S0167-4781(99)00080-9;
Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S.;
"Biochemical analysis of mouse FKBP60, a novel member of the FKBP
family.";
Biochim. Biophys. Acta 1446:295-307(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=11710534;
Jo D., Lyu M.S., Cho E.-G., Park D., Kozak C.A., Kim M.G.;
"Identification and genetic mapping of the mouse Fkbp9 gene encoding a
new member of FK506-binding protein family.";
Mol. Cells 12:272-275(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and Czech II; TISSUE=Fetal brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-570.
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: PPIases accelerate the folding of proteins during
protein synthesis.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Inhibited by FK506.
{ECO:0000269|PubMed:10524204}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138,
ECO:0000269|PubMed:10524204}.
-!- TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal
muscle, lung, liver and kidney. Lower levels found in brain,
spleen and testis. {ECO:0000269|PubMed:10524204,
ECO:0000269|PubMed:11710534}.
-!- DEVELOPMENTAL STAGE: Expressed in all developmental stages.
{ECO:0000269|PubMed:10524204}.
-!- PTM: Phosphorylated.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF090334; AAC72964.1; -; mRNA.
EMBL; AF279263; AAF79215.1; -; mRNA.
EMBL; BC026133; AAH26133.1; -; mRNA.
EMBL; BC043129; AAH43129.1; -; mRNA.
EMBL; AK007499; BAB25071.1; -; mRNA.
CCDS; CCDS39494.1; -.
RefSeq; NP_036186.2; NM_012056.2.
UniGene; Mm.20943; -.
ProteinModelPortal; Q9Z247; -.
SMR; Q9Z247; -.
BioGrid; 205110; 1.
IntAct; Q9Z247; 3.
MINT; Q9Z247; -.
STRING; 10090.ENSMUSP00000031795; -.
iPTMnet; Q9Z247; -.
PhosphoSitePlus; Q9Z247; -.
MaxQB; Q9Z247; -.
PaxDb; Q9Z247; -.
PeptideAtlas; Q9Z247; -.
PRIDE; Q9Z247; -.
Ensembl; ENSMUST00000031795; ENSMUSP00000031795; ENSMUSG00000029781.
GeneID; 27055; -.
KEGG; mmu:27055; -.
UCSC; uc009cbp.2; mouse.
CTD; 11328; -.
MGI; MGI:1350921; Fkbp9.
eggNOG; KOG0549; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00530000062784; -.
HOGENOM; HOG000230960; -.
HOVERGEN; HBG051620; -.
InParanoid; Q9Z247; -.
KO; K09575; -.
OMA; EMIVKNM; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; Q9Z247; -.
TreeFam; TF105296; -.
ChiTaRS; Fkbp9; mouse.
PRO; PR:Q9Z247; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029781; -.
CleanEx; MM_FKBP9; -.
Genevisible; Q9Z247; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0006457; P:protein folding; IDA:UniProtKB.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 7.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF00254; FKBP_C; 4.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS50059; FKBP_PPIASE; 4.
1: Evidence at protein level;
Calcium; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Isomerase; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
Rotamase; Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 570 Peptidyl-prolyl cis-trans isomerase
FKBP9.
/FTId=PRO_0000025516.
DOMAIN 54 142 PPIase FKBP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 166 254 PPIase FKBP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 278 365 PPIase FKBP-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 389 477 PPIase FKBP-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 488 523 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 533 568 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 501 512 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 546 557 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
MOTIF 567 570 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 40 40 Q -> R (in Ref. 3; AAH26133).
{ECO:0000305}.
CONFLICT 149 149 H -> Q (in Ref. 3; AAH26133).
{ECO:0000305}.
CONFLICT 234 236 DGK -> NGE (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 321 321 G -> S (in Ref. 4; BAB25071).
{ECO:0000305}.
CONFLICT 351 351 G -> A (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 353 353 A -> T (in Ref. 4; BAB25071).
{ECO:0000305}.
CONFLICT 361 361 V -> F (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 364 364 F -> V (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 378 378 K -> N (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 386 386 S -> I (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 475 475 E -> D (in Ref. 2; AAF79215).
{ECO:0000305}.
CONFLICT 548 548 N -> S (in Ref. 3; AAH43129).
{ECO:0000305}.
CONFLICT 550 550 D -> N (in Ref. 2; AAF79215).
{ECO:0000305}.
SEQUENCE 570 AA; 62995 MW; DFE8B8F2F6A0F1DA CRC64;
MALGARGWRR RSLLLLLLWV TGQAAPVLGL AVSSELQIQQ SFVPDECPRT VHSGDFVRYH
YVGTFLDGQK FDSSYDRDST FNVFVGKGQL IAGMDQALVG MCVNERRLVT IPPNLAYGSE
GVSGVIPPNS VLHFDVLLVD IWNSEDQVHI QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG
TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITVPPFLAYG EEGDGKDIPG
QASLVFDVAL LDLHNPKDTI SIENKVVPEN CERRSQSGDF LRYHYNGTLL DGTLFDSSYS
RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEKGRGSIP GSAVLVFDIH
VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL
GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVSGL
PEGYMFIWNG EVSPNLFEEI DRDGNGEVLL EEFSEYIHAQ VATGKGKLAP GFNAEMIVKN
MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL


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