ID   ANR54_RAT               Reviewed;         299 AA.
AC   Q566C8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ankyrin repeat domain-containing protein 54;
GN   Name=Ankrd54;
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=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: Plays an important role in regulating intracellular signaling
CC       events associated with erythroid terminal differentiation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
CC       domain) in an activation-independent status of LYN. Forms a
CC       multiprotein complex with LYN and HCLS1 (By similarity). Interacts with
CC       TSN2, VAV1, DBNL AND LASP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Midbody {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm
CC       during the cell cycle. EPO stimulation induces nuclear accumulation (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; BC093616; AAH93616.1; -; mRNA.
DR   RefSeq; NP_001020456.1; NM_001025285.1.
DR   AlphaFoldDB; Q566C8; -.
DR   SMR; Q566C8; -.
DR   STRING; 10116.ENSRNOP00000014413; -.
DR   iPTMnet; Q566C8; -.
DR   PhosphoSitePlus; Q566C8; -.
DR   PaxDb; Q566C8; -.
DR   PRIDE; Q566C8; -.
DR   GeneID; 362957; -.
DR   KEGG; rno:362957; -.
DR   UCSC; RGD:1309552; rat.
DR   CTD; 129138; -.
DR   RGD; 1309552; Ankrd54.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_072816_0_0_1; -.
DR   InParanoid; Q566C8; -.
DR   OrthoDB; 1559479at2759; -.
DR   PRO; PR:Q566C8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019887; F:protein kinase regulator activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; ISO:RGD.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:1902531; P:regulation of intracellular signal transduction; ISS:UniProtKB.
DR   GO; GO:0045859; P:regulation of protein kinase activity; ISO:RGD.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; ANK repeat; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NXT1"
FT   CHAIN           2..299
FT                   /note="Ankyrin repeat domain-containing protein 54"
FT                   /id="PRO_0000274495"
FT   REPEAT          108..137
FT                   /note="ANK 1"
FT   REPEAT          141..170
FT                   /note="ANK 2"
FT   REPEAT          174..203
FT                   /note="ANK 3"
FT   REPEAT          207..239
FT                   /note="ANK 4"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..240
FT                   /note="LYN-binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           98..116
FT                   /note="Nuclear localization signal (NLS)"
FT                   /evidence="ECO:0000250"
FT   MOTIF           282..292
FT                   /note="Nuclear export signal (NES)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NXT1"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NXT1"
SQ   SEQUENCE   299 AA;  32492 MW;  07F248F4575F000A CRC64;
     MAATGGGAED ESRSGRSSSE GECAVAPEPL AEAGGLFSFA DLGAALGSGA GLPGRAVGRA
     QSPLRYLQVL WQQDVEPRDE LRCKIPAGRL RRAARPHRRL GPTGKEVHAL KRLRDSANAN
     DIETVQQLLE DGADPCAADD KGRTALHFAS CNGNDQIVQL LLDHGADPNQ QDGLGNTPLH
     LAACTNHVPV ITTLLRGGAR VDALDRAGRT PLHLAKSKLN ILQEGHSQCL EAVRLEVKQI
     IHMLREYLER LGRHEQRERL DDLCTRLQMT STKEQVDEVT DLLASFTSLS LQMQSMEKR