KANK2_BOVIN
ID KANK2_BOVIN Reviewed; 858 AA.
AC Q1LZH7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=KN motif and ankyrin repeat domain-containing protein 2;
DE AltName: Full=Ankyrin repeat domain-containing protein 25;
GN Name=KANK2; Synonyms=ANKRD25;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in transcription regulation by sequestering in the
CC cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3
CC (By similarity). Involved in regulation of caspase-independent
CC apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria
CC (By similarity). Pro-apoptotic stimuli can induce its proteasomal
CC degradation allowing the translocation of AIFM1 to the nucleus to
CC induce apoptosis (By similarity). Involved in the negative control of
CC vitamin D receptor signaling pathway (By similarity). Involved in actin
CC stress fibers formation through its interaction with ARHGDIA and the
CC regulation of the Rho signaling pathway (By similarity). May thereby
CC play a role in cell adhesion and migration, regulating for instance
CC podocytes migration during development of the kidney (By similarity).
CC Through the Rho signaling pathway may also regulate cell proliferation
CC (By similarity). {ECO:0000250|UniProtKB:Q63ZY3,
CC ECO:0000250|UniProtKB:Q8BX02}.
CC -!- SUBUNIT: Interacts (non-phosphorylated form) with NCOA1; NCOA2 AND
CC NCOA3 (By similarity). Interacts with AIFM1 (By similarity). Interacts
CC with ARHGDIA; the interaction is direct and may regulate the
CC interaction of ARHGDIA with RHOA, RAC1 and CDC42 (By similarity).
CC Interacts (via ANK repeats 1-5) with KIF21A (By similarity).
CC {ECO:0000250|UniProtKB:Q63ZY3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63ZY3}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q63ZY3}.
CC -!- PTM: Phosphorylated by casein kinase II upon estrogen stimulation (By
CC similarity). Phosphorylation induces the release by KANK2 of NCOA1 and
CC its translocation to the nucleus where NCOA1 can activate gene
CC transcription (By similarity). {ECO:0000250|UniProtKB:Q63ZY3}.
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DR EMBL; BC115992; AAI15993.1; -; mRNA.
DR RefSeq; NP_001069999.1; NM_001076531.1.
DR AlphaFoldDB; Q1LZH7; -.
DR SMR; Q1LZH7; -.
DR STRING; 9913.ENSBTAP00000012586; -.
DR PaxDb; Q1LZH7; -.
DR PRIDE; Q1LZH7; -.
DR Ensembl; ENSBTAT00000012586; ENSBTAP00000012586; ENSBTAG00000009568.
DR GeneID; 767586; -.
DR KEGG; bta:767586; -.
DR CTD; 25959; -.
DR VEuPathDB; HostDB:ENSBTAG00000009568; -.
DR VGNC; VGNC:30390; KANK2.
DR eggNOG; KOG0514; Eukaryota.
DR GeneTree; ENSGT00940000161012; -.
DR InParanoid; Q1LZH7; -.
DR OMA; HQRSLQF; -.
DR OrthoDB; 98668at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000009568; Expressed in trachea and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0072073; P:kidney epithelium development; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0070563; P:negative regulation of vitamin D receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0090521; P:podocyte cell migration; ISS:UniProtKB.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR021939; KN_motif.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF12075; KN_motif; 1.
DR SMART; SM00248; ANK; 5.
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 ANK repeat; Apoptosis; Coiled coil; Cytoplasm; Methylation; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..858
FT /note="KN motif and ankyrin repeat domain-containing
FT protein 2"
FT /id="PRO_0000240839"
FT REPEAT 621..658
FT /note="ANK 0; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT REPEAT 673..703
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 707..740
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 745..774
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 778..808
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 812..842
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="Interaction with AIFM1"
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..842
FT /note="Interaction with NCOA1"
FT /evidence="ECO:0000250"
FT COILED 183..234
FT /evidence="ECO:0000255"
FT COILED 282..313
FT /evidence="ECO:0000255"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 105
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX02"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
FT MOD_RES 559
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZY3"
SQ SEQUENCE 858 AA; 91957 MW; 4DA5AFA0A770ECF2 CRC64;
MAQVLHVSAP FPGTPGPASP PAFPSKEPDV PYSVETPYGY RLDLDFLKYV DDIEKGHTLR
RVAVQRRPRL GSLPRGPGSW WTSTESLCSN ASGDSRHSAY SYCGRGFYPQ YGALETRGGF
NPRVERTLLD ARRRLEDQAA APAGLGSLTP SAAGSTSSLV GVGLPPPTPR GSGLSTPVPP
SAGHLAHVRE QMAGALRKLR QLEEQVKLIP VLQVKLSVLQ EEKRQLTVQL KSQKFLGHPA
GARGRGELCL DLPEAPEDPV TLETRSVGTW VRERDLGMPD GEAALAAKVA VLETQLKKAL
QELQAAQARQ ADLPPQAWPP PDSPVRVDTV RVVQGPREVE VAASTAAGAP AQRAQSLEPY
GAGLRALATS NGAESPPVFR SHEVMETVFP APTASTSNVH QVKKISITER SCDGAAGHPQ
APAESSLSPP ESEGATQAQP EKNTGQVPAH DDTTIKEPIR QAACHESEFE EAGGAGGAQA
GLRSIMKQKE EPTDPEAHRR SLQFVGVNGS ISPRYESSSE DSSTAENFSD NESTENEAPE
PEERVPSVAE APQLRPKETA KAKTSREESQ LPQESLHTPT AEGASGSSAK DEIRMELSPD
LISACLALEK YLENPKALTE RELKVAYTTV LQEWLRLACR SDAHPELVRR HLVTFRAMSA
RLLDYVVNIA DSNGNTALHY SVSHANFPVV QQLLDSGVCQ VDKQNRAGYS PIMLTALATL
KTQDDIQTIL QLFRLGDVNA KASQAGQTAL MLAVSHGRVD VVKALLACEA DVNVQDDDGS
TALMCACEHG HKEITALLLA VPSCDISITD RDGSTALMVA LDAGHSEIAS MLYSRMNIKC
SFAPMSDDES PASSSAEE
