ID FANK1_BOVIN Reviewed; 345 AA.
AC Q6B858; Q32L70;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Fibronectin type 3 and ankyrin repeat domains protein 1 {ECO:0000305};
DE AltName: Full=GV14 {ECO:0000303|PubMed:15803458};
GN Name=FANK1 {ECO:0000250|UniProtKB:Q8TC84};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=15803458; DOI=10.1002/mrd.20282;
RA Hwang K.-C., Park S.-Y., Park S.-P., Lim J.H., Cui X.-S., Kim N.-H.;
RT "Specific maternal transcripts in bovine oocytes and cleavaged embryos:
RT identification with novel DDRT-PCR methods.";
RL Mol. Reprod. Dev. 71:275-283(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Through the activation of JUN and AP-1-mediated
CC transcription, may regulate apoptosis. {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- SUBUNIT: Interacts with COPS5; regulates the phosphorylation of JUN and
CC the transcriptional activity of AP-1. Interacts with RYBP; may prevent
CC the ubiquitin-mediated proteasomal degradation of FANK1.
CC {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TC84}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8TC84}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9DAM9}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q9DAM9}.
CC -!- DEVELOPMENTAL STAGE: Detected in germinal vesicle (GV) stage oocytes
CC and in embryos up to the 8-cell stage, but not in morula or
CC blastocysts. {ECO:0000269|PubMed:15803458}.
CC -!- DOMAIN: The fibronectin type-III domain mediates interaction with COPS5
CC and RYBP. {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination leads to proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q8TC84}.
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DR EMBL; AY675079; AAT84372.1; -; mRNA.
DR EMBL; BC109735; AAI09736.1; -; mRNA.
DR RefSeq; NP_001003904.2; NM_001003904.3.
DR AlphaFoldDB; Q6B858; -.
DR SMR; Q6B858; -.
DR STRING; 9913.ENSBTAP00000057853; -.
DR PaxDb; 9913-ENSBTAP00000031105; -.
DR GeneID; 445423; -.
DR KEGG; bta:445423; -.
DR CTD; 92565; -.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q6B858; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR24183; FIBRONECTIN TYPE 3 AND ANKYRIN REPEAT DOMAINS PROTEIN 1; 1.
DR PANTHER; PTHR24183:SF1; FIBRONECTIN TYPE 3 AND ANKYRIN REPEAT DOMAINS PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50853; FN3; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cell projection; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..345
FT /note="Fibronectin type 3 and ankyrin repeat domains
FT protein 1"
FT /id="PRO_0000066989"
FT DOMAIN 11..108
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 109..139
FT /note="ANK 1"
FT REPEAT 143..172
FT /note="ANK 2"
FT REPEAT 176..205
FT /note="ANK 3"
FT REPEAT 209..238
FT /note="ANK 4"
FT REPEAT 243..273
FT /note="ANK 5"
FT REPEAT 277..306
FT /note="ANK 6"
FT CONFLICT 57
FT /note="H -> R (in Ref. 1; AAT84372)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="L -> M (in Ref. 1; AAT84372)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="R -> L (in Ref. 1; AAT84372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38426 MW; 9D893157A5C89DE3 CRC64;
MELQKIASSS KPHPPVVGKV THHSIELYWD LEKKAKRQGP QEQWFRFSIE EEDPKLHTYG
IIYTGYATKH VVEGLEPRTL YRFRLKVTSP SGEYAYSPVV SVSTTREPIS SEHLHRAVNV
NDEDLLVRIL QGGNVKVDVP NKFGFTALMV AAQRGYTRLV KILISHGTDV NLQNGSGKDS
LMLACYAGHL DVVKYLRRHG ASWDTRDLGG CTALHWAADG GHCNVIEWMI GDGCEVDAVD
AGSRWTPLMR VSAVSGNQEV ASLLIDAGAD VNVKDKDGKT PLMVAVLNNH EELVQLLLDR
GADASVKNEF GKGVLEMARV FDRQNVLSLL EERKRKQMRK KSSVR
//
