FBF1_CHICK
ID FBF1_CHICK Reviewed; 1132 AA.
AC Q5ZIB2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Fas-binding factor 1 homolog;
DE Short=FBF-1;
GN Name=FBF1; ORFNames=RCJMB04_28i8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Keratin-binding protein required for epithelial cell
CC polarization. Required for ciliogenesis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle pole. Cell junction {ECO:0000250}. Note=Localizes specifically
CC to the distal appendage region of the centriole, which anchors the
CC mother centriole to the plasma membrane. Localizes to the apical
CC junction complex (AJC) in epithelial cells (By similarity).
CC {ECO:0000250}.
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DR EMBL; AJ720872; CAG32531.1; -; mRNA.
DR RefSeq; NP_001108102.1; NM_001114630.1.
DR AlphaFoldDB; Q5ZIB2; -.
DR SMR; Q5ZIB2; -.
DR STRING; 9031.ENSGALP00000003408; -.
DR PaxDb; Q5ZIB2; -.
DR GeneID; 770159; -.
DR KEGG; gga:770159; -.
DR CTD; 85302; -.
DR VEuPathDB; HostDB:geneid_770159; -.
DR eggNOG; ENOG502QQFR; Eukaryota.
DR InParanoid; Q5ZIB2; -.
DR PhylomeDB; Q5ZIB2; -.
DR PRO; PR:Q5ZIB2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097539; C:ciliary transition fiber; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell junction; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..1132
FT /note="Fas-binding factor 1 homolog"
FT /id="PRO_0000297648"
FT REGION 18..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 576..727
FT /evidence="ECO:0000255"
FT COILED 769..882
FT /evidence="ECO:0000255"
FT COILED 918..1044
FT /evidence="ECO:0000255"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 126606 MW; EF10AEE731081A02 CRC64;
MATKSKSSVR GSIDDVLDDL LGYDDEGPAK SSQPAGVSSG RARGSSLQAS KKSFLEDDFF
SKLPAEDMEA AEGSSISDAD PQAVLQTLKE MDDMEADLLG MSKPSSGLGK AATKGPGKFS
TSEGAVKTSG KMPAPEKGES APEMDKKPLS SPPTSRQYRK FNFEDVDDPL AGLLSEEEQD
APRKPSPKGS ERRPERKTEL GKEKDPLPPQ TPLHTTAPAR RREELTFEDD DDDMMDVLGF
GDGQKGDQKH GKKAEEEEVR PARSKLDELL GRGSVAKILE RPGAGEHREF KLDKKYQKQP
EKEEGWDEED FVFGAYQPTV ATTPEGRPSR RQSVSRFSAE NSSEPKPDPH SKPPPAASQS
PARGSRAGGD WLGLKDEDFL DSEPPSPAKT SPVVSSQQLL AKEQATSKPN QLEEDNWLSA
ALSRKKAQAQ VKAQERGAVP LETTGKGLDP SPAVSQPATS TGAAAQAAAL QDKAASADSS
GHPVPWLSTV TQTSAHPPEP AKRDPLRDVS PSDPAASSPA EQGMQGPAPL AQVTMPSTPL
QAASQLQAES PPLGSVHERR PGAPTGQSYE DATGCRAALL SAQARVAELE SQVRMLELER
TQHKLLLESL QQRHQEDLDL LESAHRSRVK VVEETYGQRE ERLRREKEQL EAQLLSQSQD
AERARADLVA QHKQRVATLE QQSAQELERL RELQRSSVQE MLKDHEEQLQ RLKRLKDQEI
DAVTSATSHT RSLNGVIEQM ERFSSDLHSL SHKVEATHHT TSQELAMGAR QRDEQLKVLQ
DRLSQQQRDM EEERSRLQEV IAKMEARLSE QTRLLEQERW RVTAVQSKVE SLQRSLEEQR
RLMTQQLSME RAELERAKSA LLEEQKSVMQ KCSEERRKLA VEWAEFHTQQ QLSKERMERD
IDRALQLDSQ REGTIMSLAK EQAELKVRSR ELKVKEEQLA RDRLLLDEAW HELRLEKEKV
KGATLRIRQQ EEEIKNMSKL SAQKYEEGER ALQDACRIES EHQARLQVMQ QHLEQLKQQE
QHLQQERLSM AHQRRQLEQL HKKLPNNPTL LLTTDQDLSA STKGLSSTLS FPPPIRTLPG
HRSVGTTASM ELYAKLLVLK HRAQQDRNFL EDEQLFLETL KKASYNTSPL SV
