PKHO1_RAT
ID PKHO1_RAT Reviewed; 408 AA.
AC Q5BJM5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Pleckstrin homology domain-containing family O member 1;
DE Short=PH domain-containing family O member 1;
GN Name=Plekho1;
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=Spleen;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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: Cell membrane {ECO:0000250|UniProtKB:Q53GL0};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q53GL0}. Nucleus
CC {ECO:0000250|UniProtKB:Q53GL0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q53GL0}. Note=Predominantly localized to the
CC plasma membrane through the binding to phosphatidylinositol 3-
CC phosphate. In C2C12 cells, with the absence of growth factor, it is
CC found in the nucleus. It rapidly translocates to the plasma membrane
CC after insulin stimulation. In response to TNF, it translocates from the
CC plasma membrane to the cytoplasm and then to the nucleus accompanied by
CC cleavage by caspase-3. However, the subcellular location is highly
CC dependent of the cell type, and this explains why it is found
CC exclusively at the plasma membrane, in some type of cells.
CC {ECO:0000250|UniProtKB:Q53GL0}.
CC -!- PTM: C-terminal fragments could be released during apoptosis via
CC caspase-3-dependent cleavage. {ECO:0000250}.
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DR EMBL; BC091420; AAH91420.1; -; mRNA.
DR RefSeq; NP_001020290.1; NM_001025119.1.
DR AlphaFoldDB; Q5BJM5; -.
DR SMR; Q5BJM5; -.
DR STRING; 10116.ENSRNOP00000028747; -.
DR iPTMnet; Q5BJM5; -.
DR PhosphoSitePlus; Q5BJM5; -.
DR PaxDb; Q5BJM5; -.
DR GeneID; 310674; -.
DR KEGG; rno:310674; -.
DR UCSC; RGD:1311487; rat.
DR CTD; 51177; -.
DR RGD; 1311487; Plekho1.
DR eggNOG; ENOG502QSPU; Eukaryota.
DR HOGENOM; CLU_052292_0_0_1; -.
DR InParanoid; Q5BJM5; -.
DR OrthoDB; 929437at2759; -.
DR PhylomeDB; Q5BJM5; -.
DR TreeFam; TF333115; -.
DR PRO; PR:Q5BJM5; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q5BJM5; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036195; C:muscle cell projection membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISO:RGD.
DR GO; GO:0007520; P:myoblast fusion; ISO:RGD.
DR GO; GO:0051451; P:myoblast migration; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..408
FT /note="Pleckstrin homology domain-containing family O
FT member 1"
FT /id="PRO_0000310425"
FT DOMAIN 20..131
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 132..192
FT /note="Interaction with capping proteins (CPs)"
FT /evidence="ECO:0000250"
FT REGION 135..307
FT /note="Interaction with ATM, CKIP, IFP35 and NMI"
FT /evidence="ECO:0000250"
FT REGION 217..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..408
FT /note="Negative regulator of AP-1 activity"
FT /evidence="ECO:0000250"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 154
FT /note="Interacts with capping protein"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Interacts with capping protein"
FT /evidence="ECO:0000250"
FT SITE 309..310
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT SITE 344..345
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIY0"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
SQ SEQUENCE 408 AA; 46068 MW; 82A8781364A2C787 CRC64;
MKKSGSGKRG PPDGNHQSVA PEKVGWVRKF CGKGIFREIW KNRYVVLKGD QLYVSEKEVK
DEKNSQEVFD LSDYEKCEEL RKSKSRSKKN HSKFTLARCR QPGTTAPNLI FLAVSPEEKE
SWINALSSAI TRAKNRILDE VTVEEDSYLA HPTRDRAKIQ HSRRPPTRGH LMAVASTSTS
DGMLTLDLIQ EEDPSPEEPA SCAESFRVDL DKSVAQLAGS RRRADSDRIR PSSHRASSLS
RPWERPDKGA PYTPQALKKL PSTEKSRCAS LEEILSQRDT APAHPLHLQA EESPAPVPSQ
PGQLSRIQDL VARKLEKTQE LLAEVQGLGD GKWKAKDPPR SPPDSQSEQL LLETERLLGE
ASSNWSQAKR VLQEVRELRD LYRQMDLQTP DSHLRQTSQH SQYRKSLM
