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   25-MAY-2022, entry version 94.
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.ENSBTAP00000031105; -.
DR   PaxDb; Q6B858; -.
DR   GeneID; 445423; -.
DR   KEGG; bta:445423; -.
DR   CTD; 92565; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   InParanoid; Q6B858; -.
DR   OrthoDB; 1514637at2759; -.
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 transcription, DNA-templated; 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; -; 2.
DR   Gene3D; 2.60.40.10; -; 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   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF49265; SSF49265; 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