ID   FANK1_RAT               Reviewed;         344 AA.
AC   Q66H07;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Fibronectin type 3 and ankyrin repeat domains 1 protein {ECO:0000305};
GN   Name=Fank1 {ECO:0000312|RGD:1304756};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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: 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   -!- 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; BC082095; AAH82095.1; -; mRNA.
DR   RefSeq; NP_001008348.1; NM_001008347.1.
DR   AlphaFoldDB; Q66H07; -.
DR   SMR; Q66H07; -.
DR   STRING; 10116.ENSRNOP00000024751; -.
DR   PaxDb; Q66H07; -.
DR   GeneID; 309071; -.
DR   KEGG; rno:309071; -.
DR   UCSC; RGD:1304756; rat.
DR   CTD; 92565; -.
DR   RGD; 1304756; Fank1.
DR   VEuPathDB; HostDB:ENSRNOG00000018327; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   InParanoid; Q66H07; -.
DR   OMA; NFGHRLR; -.
DR   OrthoDB; 1514637at2759; -.
DR   PhylomeDB; Q66H07; -.
DR   TreeFam; TF106234; -.
DR   PRO; PR:Q66H07; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018327; Expressed in testis and 10 other tissues.
DR   ExpressionAtlas; Q66H07; baseline and differential.
DR   Genevisible; Q66H07; RN.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0097546; C:ciliary base; ISO:RGD.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
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; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
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..344
FT                   /note="Fibronectin type 3 and ankyrin repeat domains 1
FT                   protein"
FT                   /id="PRO_0000066992"
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"
SQ   SEQUENCE   344 AA;  38411 MW;  7C46279BA11ED36A CRC64;
     MEPKKIVPLL RPHPPVVGKV THHSIELYWD LEKREKRQGP QEQWLRFSIE EEDPKMHNYG
     VIYTGYATKH VVEGLEPRTL YRFRLKVTSP SGEYEYSPVV SVATTREPIS SEHFHRAVNV
     NDEDLLLRIL EGGHVMVDVP NKFGFTALMV AAQKGYTRLV KILISNGTDV NLKNGSGKDS
     LMLACYAGHL DVVKYLRKHG ASWDARDLGG CTALHWAADG GHCPVIDWMI KDGCEVDVVD
     TGSGWTPLMR VSAVTGSQKV ASLLIEAGAD VNVRDKDGKT PLMVAVLNNH EQLVQLLLDK
     GADATVKNEF GKGVLEMARV FDRQNVLSLL EERKKKMPRK SSVH