Q9Z247 (FKBP9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP9
Short name=PPIase FKBP9
EC=5.2.1.8

Alternative name(s):
63 kDa FK506-binding protein
Short name=63 kDa FKBP
Short name=FKBP-63
FK506-binding protein 9
Short name=FKBP-9
FKBP65RS
Rotamase

Gene names

Name:	Fkbp9
Synonyms:	Fkbp60, Fkbp63

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins during protein synthesis.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by FK506. Ref.1
Subcellular location	Endoplasmic reticulum lumen Ref.1.
Tissue specificity	Predominantly expressed in heart, skeletal muscle, lung, liver and kidney. Lower levels found in brain, spleen and testis. Ref.1 Ref.2
Developmental stage	Expressed in all developmental stages. Ref.1
Post-translational modification	Phosphorylated.
Sequence similarities	Contains 2 EF-hand domains. Contains 4 PPIase FKBP-type domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Isomerase Rotamase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.1. Source: UniProtKB endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome calcium ion binding Inferred from direct assay Ref.1. Source: UniProtKB peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 570	546	Peptidyl-prolyl cis-trans isomerase FKBP9		PRO_0000025516
Regions
	Domain	54 – 142	89	PPIase FKBP-type 1
	Domain	166 – 254	89	PPIase FKBP-type 2
	Domain	278 – 365	88	PPIase FKBP-type 3
	Domain	389 – 477	89	PPIase FKBP-type 4
	Domain	488 – 523	36	EF-hand 1
	Domain	533 – 568	36	EF-hand 2
	Calcium binding	501 – 512	12	1 Potential
	Calcium binding	546 – 557	12	2 Potential
	Motif	567 – 570	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	174	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	40	1	Q → R in AAH26133. Ref.3
	Sequence conflict	149	1	H → Q in AAH26133. Ref.3
	Sequence conflict	234 – 236	3	DGK → NGE in AAF79215. Ref.2
	Sequence conflict	321	1	G → S in BAB25071. Ref.4
	Sequence conflict	351	1	G → A in AAF79215. Ref.2
	Sequence conflict	353	1	A → T in BAB25071. Ref.4
	Sequence conflict	361	1	V → F in AAF79215. Ref.2
	Sequence conflict	364	1	F → V in AAF79215. Ref.2
	Sequence conflict	378	1	K → N in AAF79215. Ref.2
	Sequence conflict	386	1	S → I in AAF79215. Ref.2
	Sequence conflict	475	1	E → D in AAF79215. Ref.2
	Sequence conflict	548	1	N → S in AAH43129. Ref.3
	Sequence conflict	550	1	D → N in AAF79215. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Z247 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: DFE8B8F2F6A0F1DA	FASTA	570	62,995
	10 20 30 40 50 60 MALGARGWRR RSLLLLLLWV TGQAAPVLGL AVSSELQIQQ SFVPDECPRT VHSGDFVRYH 70 80 90 100 110 120 YVGTFLDGQK FDSSYDRDST FNVFVGKGQL IAGMDQALVG MCVNERRLVT IPPNLAYGSE 130 140 150 160 170 180 GVSGVIPPNS VLHFDVLLVD IWNSEDQVHI QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG 190 200 210 220 230 240 TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITVPPFLAYG EEGDGKDIPG 250 260 270 280 290 300 QASLVFDVAL LDLHNPKDTI SIENKVVPEN CERRSQSGDF LRYHYNGTLL DGTLFDSSYS 310 320 330 340 350 360 RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEKGRGSIP GSAVLVFDIH 370 380 390 400 410 420 VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL 430 440 450 460 470 480 GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVSGL 490 500 510 520 530 540 PEGYMFIWNG EVSPNLFEEI DRDGNGEVLL EEFSEYIHAQ VATGKGKLAP GFNAEMIVKN 550 560 570 MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biochemical analysis of mouse FKBP60, a novel member of the FKBP family." Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S. Biochim. Biophys. Acta 1446:295-307(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CALCIUM-BINDING.
[2]	"Identification and genetic mapping of the mouse Fkbp9 gene encoding a new member of FK506-binding protein family." Jo D., Lyu M.S., Cho E.-G., Park D., Kozak C.A., Kim M.G. Mol. Cells 12:272-275(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Thymus.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and Czech II. Tissue: Fetal brain and Mammary tumor.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-570. Strain: C57BL/6J. Tissue: Pancreas.
[5]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF090334 mRNA. Translation: AAC72964.1. AF279263 mRNA. Translation: AAF79215.1. BC026133 mRNA. Translation: AAH26133.1. BC043129 mRNA. Translation: AAH43129.1. AK007499 mRNA. Translation: BAB25071.1.
IPI	IPI00130486.
RefSeq	NP_036186.2. NM_012056.2.
UniGene	Mm.20943. Mm.487141.
3D structure databases
ProteinModelPortal	Q9Z247.
SMR	Q9Z247. Positions 50-477, 494-560.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z247. 1 interaction.
MINT	MINT-4095122.
STRING	10090.ENSMUSP00000031795.
Proteomic databases
PaxDb	Q9Z247.
PRIDE	Q9Z247.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031795; ENSMUSP00000031795; ENSMUSG00000029781.
GeneID	27055.
KEGG	mmu:27055.
UCSC	uc009cbp.2. mouse.
Organism-specific databases
CTD	11328.
MGI	MGI:1350921. Fkbp9.
Phylogenomic databases
eggNOG	COG0545.
GeneTree	ENSGT00530000062784.
HOGENOM	HOG000230960.
HOVERGEN	HBG051620.
InParanoid	Q9Z247.
KO	K09575.
OMA	CPRTIQV.
OrthoDB	EOG4RR6GZ.
Enzyme and pathway databases
Reactome	REACT_93132. Metabolism of proteins.
Gene expression databases
Bgee	Q9Z247.
CleanEx	MM_FKBP9.
Genevestigator	Q9Z247.
GermOnline	ENSMUSG00000029781. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
PANTHER	PTHR10516. PTHR10516. 1 hit.
Pfam	PF00254. FKBP_C. 4 hits. [Graphical view]
SMART	SM00054. EFh. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. PS00014. ER_TARGET. 1 hit. PS50059. FKBP_PPIASE. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FKBP9. mouse.
NextBio	304999.
SOURCE	Search...

Entry information

Entry name

FKBP9_MOUSE

Accession

Primary (citable) accession number: Q9Z247
Secondary accession number(s): Q80ZZ6 , Q8R386, Q9CVM0, Q9JHX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	May 1, 1999
Last modified:	May 29, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program