FBF1_MOUSE
ID FBF1_MOUSE Reviewed; 1173 AA.
AC A2A870; A2A871; B2RQ77; Q8BSP0; Q99MZ9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fas-binding factor 1;
DE Short=FBF-1;
GN Name=Fbf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND POSSIBLE INTERACTION WITH FAS.
RC TISSUE=Thymus;
RX PubMed=10978533; DOI=10.1016/s0167-4781(00)00163-9;
RA Schmidt T., Karsunky H., Frass B., Baum W., Denzel A., Moeroey T.;
RT "A novel protein (Fbf-1) that binds to CD95/APO-1/FAS and shows sequence
RT similarity to trichohyalin and plectin.";
RL Biochim. Biophys. Acta 1493:249-254(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Keratin-binding protein required for epithelial cell
CC polarization. Involved in apical junction complex (AJC) assembly via
CC its interaction with PARD3. Required for ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q8TES7}.
CC -!- SUBUNIT: Interacts with PARD3 (By similarity). May interact with FAS
CC cytoplasmic domain (By similarity). Interacts with TRAPPC14 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8TES7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000269|PubMed:10978533}. Cell junction
CC {ECO:0000250}. Note=Localizes specifically to the distal appendage
CC region of the centriole, which anchors the mother centriole to the
CC plasma membrane. Localizes to the apical junction complex (AJC) in
CC epithelial cells (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A870-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A870-2; Sequence=VSP_027324;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:10978533}.
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DR EMBL; AF241249; AAK28326.1; -; mRNA.
DR EMBL; AK031140; BAC27275.1; -; mRNA.
DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055689; AAH55689.1; -; mRNA.
DR EMBL; BC137794; AAI37795.1; -; mRNA.
DR CCDS; CCDS25659.1; -. [A2A870-1]
DR RefSeq; NP_766159.3; NM_172571.3. [A2A870-1]
DR RefSeq; XP_006533155.1; XM_006533092.3. [A2A870-1]
DR RefSeq; XP_006533156.1; XM_006533093.3. [A2A870-1]
DR RefSeq; XP_006533157.1; XM_006533094.3.
DR RefSeq; XP_011247250.1; XM_011248948.2. [A2A870-1]
DR AlphaFoldDB; A2A870; -.
DR SMR; A2A870; -.
DR BioGRID; 229891; 8.
DR IntAct; A2A870; 2.
DR MINT; A2A870; -.
DR STRING; 10090.ENSMUSP00000099320; -.
DR iPTMnet; A2A870; -.
DR PhosphoSitePlus; A2A870; -.
DR MaxQB; A2A870; -.
DR PaxDb; A2A870; -.
DR PRIDE; A2A870; -.
DR ProteomicsDB; 267576; -. [A2A870-1]
DR ProteomicsDB; 267577; -. [A2A870-2]
DR Antibodypedia; 80115; 93 antibodies from 21 providers.
DR Ensembl; ENSMUST00000103031; ENSMUSP00000099320; ENSMUSG00000020776. [A2A870-1]
DR Ensembl; ENSMUST00000106435; ENSMUSP00000102043; ENSMUSG00000020776. [A2A870-1]
DR GeneID; 217335; -.
DR KEGG; mmu:217335; -.
DR UCSC; uc007mkf.1; mouse. [A2A870-2]
DR UCSC; uc007mkg.2; mouse. [A2A870-1]
DR CTD; 85302; -.
DR MGI; MGI:1922033; Fbf1.
DR VEuPathDB; HostDB:ENSMUSG00000020776; -.
DR eggNOG; ENOG502QQFR; Eukaryota.
DR GeneTree; ENSGT00720000108861; -.
DR HOGENOM; CLU_008480_0_0_1; -.
DR InParanoid; A2A870; -.
DR OMA; DKEDPWG; -.
DR OrthoDB; 399859at2759; -.
DR PhylomeDB; A2A870; -.
DR TreeFam; TF328742; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 217335; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fbf1; mouse.
DR PRO; PR:A2A870; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A870; protein.
DR Bgee; ENSMUSG00000020776; Expressed in dorsal pancreas and 230 other tissues.
DR ExpressionAtlas; A2A870; baseline and differential.
DR Genevisible; A2A870; MM.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097539; C:ciliary transition fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR InterPro; IPR033561; FBF1.
DR PANTHER; PTHR33689; PTHR33689; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1173
FT /note="Fas-binding factor 1"
FT /id="PRO_0000297647"
FT REGION 17..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 617..742
FT /evidence="ECO:0000255"
FT COILED 808..917
FT /evidence="ECO:0000255"
FT COILED 975..1057
FT /evidence="ECO:0000255"
FT COMPBIAS 247..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TES7"
FT CROSSLNK 1002
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TES7"
FT VAR_SEQ 1..784
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027324"
FT CONFLICT 17
FT /note="M -> V (in Ref. 1; AAK28326)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="M -> I (in Ref. 1; AAK28326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1173 AA; 130138 MW; 2332B34E71672160 CRC64;
MTGQCCEELQ RAPKPRMALR TKKGLKGSIE DVLGDLLGDD TTPPEKPAEP ASHAKDTASS
PQWQASKAKF LPKDSVEGLA GADAEASSVS DADPQVFLQN MKDLDSMDDD LFGRMKSHQP
SGKGAAKGPG KEGPSNHKPA GTLTANEKGY TMPTKKPPPS SSKTGLQYKK FSFEDFEDPL
AGLLSDEEEE TATKLPAVER KPAPKSPGAA AGQGPSVPLT PGDTPIRKKE LLFDEGDDIM
TTLGFEDSPK AERKKTGDQE GPLPARSKLD ELLGRGTAAK LLTRPGTGER REFQLDKKYQ
KMGGEESVPA RDKEDSWDDE TLTFGAYKPT VASSEGRQSR RQSVSRFLGE GGPDPKGESL
GFKQSSPPAS SPIHPRKGGA DWLGLKDNDL DLLSPSPVQK AQQEDSPMTP SLLPPTNQPS
APEPQSAPTG LPSAAKPPAK GARPSLKASQ ASSPKASEEK EDDWLSHVIS QKKSQNLARE
ERAGPPKDLA SLGSLGQTPS GSLPVAQVLE QAPAGEASKP TTQGMAAVRP GVTGSSMSWS
QATTVLPVDD PKKGAASASG DFSSREPAVY IPHSQEPTGL SVPIQTLLPE SMMQSLLPGS
GYQKQLLAAQ GQLQSSTAQL QVELLQSQTK LSELEAQVRK LELERAQHRM LLESLQQRHQ
ADLELIEDAH RSRIKVLETS YQQREEQLRR EKEVLSAQHA SYCREAEQAR AELVAQHQRQ
MAMAEQERDQ EVARLRELQQ ASILEMRKDH EHQLQRLKML KDQEIDAVTS ATSHTRSLNG
IIEQMEKFSS SLNTLSSRVE ASHLTTSQQR ELGIRQQDEQ LRALQERLGR QQRDMEEERN
RLQEVIGKME VRLSEQSRLL EQERWRVAAE KTKAESAQRT LEEQRKIMVQ QIAMEREELE
RAKSALLEEQ KSVMNKCGEE RRRLAAEWAE YFTQQKLSKE RAEREAERAM HADSQREGTI
ISLTKEQAEL TVRACELRAK EEKLLAEREA LERERQELRL EKDRLHKASL RLQARAQEVE
HMSKVASKKY EEGEQALQEA QQMQNEQQGR LQVVQRQQEW LRQQEQRVHQ EHLSLAQQRL
QLDRVRQEVP ASLPGLPPRV QGPAASSRDA VQAPASSSPQ CSQPAAAQVP THLLAKLLLL
KHTAEEDHDF LENEQFFLET LKKAPYNMAY HSA
