PKHO1_BOVIN
ID PKHO1_BOVIN Reviewed; 409 AA.
AC A4IFK0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Pleckstrin homology domain-containing family O member 1;
DE Short=PH domain-containing family O member 1;
GN Name=PLEKHO1;
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=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the regulation of the actin cytoskeleton
CC through its interactions with actin capping protein (CP). May function
CC to target CK2 to the plasma membrane thereby serving as an adapter to
CC facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears
CC to target ATM to the plasma membrane. Also implicated in PI3K-regulated
CC muscle differentiation, the regulation of AP-1 activity (plasma
CC membrane bound AP-1 regulator that translocates to the nucleus) and the
CC promotion of apoptosis induced by tumor necrosis factor TNF. When bound
CC to PKB, it inhibits it probably by decreasing PKB level of
CC phosphorylation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer or homodimer. Interacts with CK2 and actin capping
CC subunits (capping protein CP-alpha and CP-beta). CKIP1 and CK2 together
CC inhibit the activity of actin capping protein at the barbed ends of
CC actin filaments. Interacts with ATM, IFP35, JUN, JUND, NMI and PI3K.
CC Interacts with AKT1, AKT2 and AKT3 (each isozyme of PKB),
CC PtdIns(3,5)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm {ECO:0000250}.
CC -!- PTM: C-terminal fragments could be released during apoptosis via
CC caspase-3-dependent cleavage. {ECO:0000250}.
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DR EMBL; BC134615; AAI34616.1; -; mRNA.
DR RefSeq; NP_001077266.1; NM_001083797.1.
DR AlphaFoldDB; A4IFK0; -.
DR STRING; 9913.ENSBTAP00000006381; -.
DR PaxDb; A4IFK0; -.
DR GeneID; 788251; -.
DR KEGG; bta:788251; -.
DR CTD; 51177; -.
DR eggNOG; ENOG502QSPU; Eukaryota.
DR InParanoid; A4IFK0; -.
DR OrthoDB; 929437at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036195; C:muscle cell projection membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR GO; GO:1901739; P:regulation of myoblast fusion; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR028452; CKIP-1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043448; PKHO1/2.
DR PANTHER; PTHR15871; PTHR15871; 1.
DR PANTHER; PTHR15871:SF1; PTHR15871:SF1; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..409
FT /note="Pleckstrin homology domain-containing family O
FT member 1"
FT /id="PRO_0000310422"
FT DOMAIN 21..132
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..193
FT /note="Interaction with capping proteins (CPs)"
FT /evidence="ECO:0000250"
FT REGION 136..308
FT /note="Interaction with ATM, CKIP, IFP35 and NMI"
FT /evidence="ECO:0000250"
FT REGION 218..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..409
FT /note="Negative regulator of AP-1 activity"
FT /evidence="ECO:0000250"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 155
FT /note="Interacts with capping protein"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Interacts with capping protein"
FT /evidence="ECO:0000250"
FT SITE 310..311
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 345..346
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJM5"
SQ SEQUENCE 409 AA; 46395 MW; 49CF7C311172D51C CRC64;
MMKKNNSTKR GPQDGNHQCA PPEKVGWVRK FCGKGIFREI WKNRYVVLKG DQLYISEKEV
KDEKNIQEVF DLSDYEKCEE LRKSKSRSKK NHSKFTLAHS KQPGNTAPNL IFLAVSPEEK
ESWINALNSA ITRAKNRVLD EVTVEEDSYL AHPTRDRAKI QHSRRPPTRG HLMAVASTST
SDGMLTLDLI QEEDPSPEEP TSCAESFRVD LDKSVAQLAG SRRRADSDRI QPSSDRASGL
PRLWEKPDKG ATYTPQAPKK LTATEKSRCA SLEEILSQRD AVPAHTLQRR AEDPPTPIPH
APGQLSRIQD LVARKLEKTQ ELLAEVQGLG DGKRKAKEPP RSPPDSESEQ LLLETERLLG
EASSNWSQAK RVLQEVRELR DLYRQMDLQT PDSHLRQTTQ HSQYRKSLM
