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FK506-binding protein 15 (FKBP-15) (133 kDa FK506-binding protein) (133 kDa FKBP) (FKBP-133) (WASP and FKBP-like) (WAFL)

 FKB15_MOUSE             Reviewed;        1216 AA.
Q6P9Q6; Q3TSY4; Q5SQG3; Q80TU5;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
07-NOV-2018, entry version 117.
RecName: Full=FK506-binding protein 15;
Short=FKBP-15;
AltName: Full=133 kDa FK506-binding protein;
Short=133 kDa FKBP;
Short=FKBP-133;
AltName: Full=WASP and FKBP-like;
Short=WAFL;
Name=Fkbp15; Synonyms=Fkbp133, Kiaa0674;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-704.
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-1216 (ISOFORM B).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[5]
IDENTIFICATION, ALTERNATIVE SPLICING (ISOFORMS A AND B), FUNCTION,
DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16756961; DOI=10.1016/j.bbrc.2006.05.113;
Nakajima O., Nakamura F., Yamashita N., Tomita Y., Suto F., Okada T.,
Iwamatsu A., Kondo E., Fujisawa H., Takei K., Goshima Y.;
"FKBP133: a novel mouse FK506-binding protein homolog alters growth
cone morphology.";
Biochem. Biophys. Res. Commun. 346:140-149(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093 AND
SER-1159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-1159, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-310; SER-617;
SER-1050; SER-1091; THR-1093; SER-1157; SER-1159 AND SER-1190, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, 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).
[10]
INTERACTION WITH TBC1D23.
PubMed=29084197; DOI=10.1038/ncb3627;
Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
"TBC1D23 is a bridging factor for endosomal vesicle capture by golgins
at the trans-Golgi.";
Nat. Cell Biol. 19:1424-1432(2017).
-!- FUNCTION: Involved in the transport of early endosomes at the
level of transition between microfilament-based and microtubule-
based movement (By similarity). May be involved in the
cytoskeletal organization of neuronal growth cones. Seems to be
inactive as a PPIase. {ECO:0000250, ECO:0000269|PubMed:16756961}.
-!- SUBUNIT: Interacts with WIP and actin (By similarity). Interacts
with TBC1D23 (PubMed:29084197). {ECO:0000250|UniProtKB:Q5T1M5,
ECO:0000269|PubMed:29084197}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16756961}.
Cell projection, axon {ECO:0000269|PubMed:16756961}. Early
endosome {ECO:0000269|PubMed:16756961}. Note=Present in axons and
neuronal growth cones. {ECO:0000269|PubMed:16756961}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q6P9Q6-1; Sequence=Displayed;
Name=B;
IsoId=Q6P9Q6-2; Sequence=VSP_027759;
-!- TISSUE SPECIFICITY: Expressed in brain, with highest levels in the
granular cell layer of cerebellum and in the granule cell layer of
dentate gyrus. {ECO:0000269|PubMed:16756961}.
-!- DEVELOPMENTAL STAGE: Strongly expressed in the developing nervous
system at E18.5. Present in brain, heart, lung, kidney and thymus
at E18.5 (at protein level). {ECO:0000269|PubMed:16756961}.
-!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
FK506-binding and enzymatic activity.
-!- DOMAIN: The central coiled-coil region is responsible for
association with early endosomes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL683829; CAI25942.1; -; Genomic_DNA.
EMBL; AL732548; CAI25942.1; JOINED; Genomic_DNA.
EMBL; AL732548; CAI26145.1; -; Genomic_DNA.
EMBL; AL683829; CAI26145.1; JOINED; Genomic_DNA.
EMBL; BC060651; AAH60651.1; -; mRNA.
EMBL; AK161705; BAE36541.1; -; mRNA.
EMBL; AK122343; BAC65625.1; -; mRNA.
CCDS; CCDS51201.1; -. [Q6P9Q6-1]
RefSeq; NP_001038993.1; NM_001045528.1. [Q6P9Q6-1]
RefSeq; XP_006538097.1; XM_006538034.3. [Q6P9Q6-2]
UniGene; Mm.357792; -.
ProteinModelPortal; Q6P9Q6; -.
SMR; Q6P9Q6; -.
BioGrid; 237211; 2.
IntAct; Q6P9Q6; 2.
iPTMnet; Q6P9Q6; -.
PhosphoSitePlus; Q6P9Q6; -.
EPD; Q6P9Q6; -.
PaxDb; Q6P9Q6; -.
PeptideAtlas; Q6P9Q6; -.
PRIDE; Q6P9Q6; -.
Ensembl; ENSMUST00000084527; ENSMUSP00000081575; ENSMUSG00000066151. [Q6P9Q6-1]
GeneID; 338355; -.
KEGG; mmu:338355; -.
UCSC; uc008teh.2; mouse. [Q6P9Q6-1]
UCSC; uc008tei.1; mouse. [Q6P9Q6-2]
CTD; 23307; -.
MGI; MGI:2444782; Fkbp15.
eggNOG; ENOG410INYI; Eukaryota.
eggNOG; ENOG4112APP; LUCA.
GeneTree; ENSGT00530000064286; -.
HOGENOM; HOG000112601; -.
HOVERGEN; HBG067251; -.
InParanoid; Q6P9Q6; -.
KO; K17478; -.
OMA; LIIPPAC; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; Q6P9Q6; -.
TreeFam; TF328592; -.
ChiTaRS; Fkbp15; mouse.
PRO; PR:Q6P9Q6; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000066151; Expressed in 277 organ(s), highest expression level in stroma of bone marrow.
CleanEx; MM_FKBP15; -.
ExpressionAtlas; Q6P9Q6; baseline and differential.
Genevisible; Q6P9Q6; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
InterPro; IPR001179; PPIase_FKBP_dom.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Alternative splicing; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Endocytosis; Endosome;
Phosphoprotein; Reference proteome; Transport.
CHAIN 1 1216 FK506-binding protein 15.
/FTId=PRO_0000299557.
DOMAIN 196 289 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REGION 71 168 Important for function in growth cone
organization.
COILED 519 790 {ECO:0000255}.
COILED 820 865 {ECO:0000255}.
COMPBIAS 929 941 Glu-rich.
COMPBIAS 944 1045 Pro-rich.
COMPBIAS 1203 1211 Poly-Asp.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 617 617 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 948 948 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 1018 1018 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 1050 1050 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1091 1091 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1093 1093 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1108 1108 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 1153 1153 Phosphoserine.
{ECO:0000250|UniProtKB:Q5T1M5}.
MOD_RES 1157 1157 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1190 1190 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1198 1198 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5T1M5}.
VAR_SEQ 1190 1216 SMKGRPPPTPLFGDDDDDDDDDIGWLG -> VRRPQALLSP
HTTTWGLFPAGSETRKGVCWWLVSWTLCTGPCGSKLGAQSG
QLCKHDGDGQLPLYS (in isoform B).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_027759.
CONFLICT 652 652 H -> R (in Ref. 3; BAE36541).
{ECO:0000305}.
SEQUENCE 1216 AA; 132961 MW; 8F8130D5038122FF CRC64;
MFGAGDEDDT DFLSPSGGAK LASLFGLDQA TMGHGNEFFQ YTAPKQPKKG QGTAAGNQTA
PKPAPATTGT SSVLFATAVH AYRYINGQYA KQGKFGAAVL GNHTSREYRI LLYISQQQPV
TVATIHLNFE LMVRPNNYST FYDDQRQNWS IMFESEKAAV SFNKQVCVAK CNSISSLDAV
LCQDLVAAEG PAVETGDSLE VAYTGWLLQN HVLGQVFDST ANKDKPLRLK LGSGKVVKGL
EDGLLGMKKG GKRLIITPSA CAAGSEGVIG WTQPTDSILV FEVEVRRVKF ARDSGSDGHS
VSSRDSAAPS PIPASDSLSA DPVVTPLPLP LKPGEPGLRS KSNSLSEQLT VNSNPDTVKA
KLISRMAKMG QPMLPILPPQ LDSNDSETED ATVLRGAGQS LVTPSIQPSL QPAHPVLPQM
ASQAPQPSGS GLQTPSAALM QAVSLDSHSA VSGNAQNFQP YAGVQAYAYP QTPSVTSQLQ
PVRPLYPAPL SQAPHFQGSG DMMSFLMTEA RQHNTEIRMA VNKVADKMDH LMTKVEELQK
HSSGNSMLLP SMSVTMETSM IMSNIQRIIQ ENERLKQELL EKSSRIEEQN DKISDLIERN
QRYVEQSNLM MEKRNNSLQT ATENTQARIL HAEQEKAKVT EELAAATAQV SHLQLKMTAH
QKKETELQLQ LTDNLKETDL LRGHVTRLQA DLSELREASE QTQTKFKSEK QSRRQLELKV
TSLEEELTDL RAEKTSLEKN LSERKKKSAQ ERCQAEAEMD EIRKSHQEEL DRLRQLLKKA
RVSTDQAAAE QLTLAQAELQ SQWEAKCEQL LASARDEHLQ QYREVCAQRD AHQQKLALLQ
DECLALQAQI AAFTEQKEHM QRLEKTKSQA PAGRAAADPS EKVKKIMNQV FQSLRGEFEL
EESYDGGTIL RTIMHTIKMV TLQLLNHQEE EEEEEEEEEE EKKPLRPSLE QPGPATPGMP
PAPPSGETQE APEVLPEQVV GETTPLPLQA LPTPENGAQT RKGEPAEAEV PSEIKDSSLP
PQPAGIPAHR VLGPPTSIPP KPPGPVTMDS ESEEMLAADQ RTVQPNGLLG EEHVREVATD
GLLQGNSRRL SLTPDPEKGE PPALDPESQG GEAQPPECKQ AEDVSSSGPR ETLLDTELAS
AAAGTSLRHN QDSQHCSLSG DEEDELFKGA TLKVPRPTAQ PEEEDEDEVS MKGRPPPTPL
FGDDDDDDDD DIGWLG


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