PKHO1_DANRE
ID PKHO1_DANRE Reviewed; 520 AA.
AC A4IG55; A5A8K2; A8E7N4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Pleckstrin homology domain-containing family O member 1-A;
DE Short=PH domain-containing family O member 1-A;
DE AltName: Full=Casein kinase 2-interacting protein 1;
DE Short=CK2-interacting protein 1;
DE Short=CKIP-1;
GN Name=plekho1a; Synonyms=ckip, plekho1; ORFNames=si:dkey-200h23.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-520 (ISOFORM 1).
RX PubMed=18065431; DOI=10.1242/dev.009050;
RA Nagayoshi S., Hayashi E., Abe G., Osato N., Asakawa K., Urasaki A.,
RA Horikawa K., Ikeo K., Takeda H., Kawakami K.;
RT "Insertional mutagenesis by the Tol2 transposon-mediated enhancer trap
RT approach generated mutations in two developmental genes: tcf7 and
RT synembryn-like.";
RL Development 135:159-169(2008).
CC -!- FUNCTION: Plays a role in the regulation of the actin cytoskeleton
CC through its interactions with actin capping protein (CP).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4IG55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4IG55-2; Sequence=VSP_032043;
CC -!- PTM: C-terminal fragments could be released during apoptosis via
CC caspase-3-dependent cleavage. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571688; CAP09533.1; -; Genomic_DNA.
DR EMBL; BC134933; AAI34934.1; -; mRNA.
DR EMBL; AB303429; BAF62166.1; -; mRNA.
DR RefSeq; NP_001103933.1; NM_001110463.1. [A4IG55-2]
DR AlphaFoldDB; A4IG55; -.
DR SMR; A4IG55; -.
DR STRING; 7955.ENSDARP00000081436; -.
DR PaxDb; A4IG55; -.
DR PRIDE; A4IG55; -.
DR GeneID; 563283; -.
DR KEGG; dre:563283; -.
DR CTD; 563283; -.
DR ZFIN; ZDB-GENE-060503-433; plekho1a.
DR eggNOG; ENOG502RKBY; Eukaryota.
DR InParanoid; A4IG55; -.
DR PhylomeDB; A4IG55; -.
DR TreeFam; TF333115; -.
DR PRO; PR:A4IG55; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043448; PKHO1/2.
DR PANTHER; PTHR15871; PTHR15871; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..520
FT /note="Pleckstrin homology domain-containing family O
FT member 1-A"
FT /id="PRO_0000310427"
FT DOMAIN 20..131
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 141..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032043"
FT CONFLICT 230
FT /note="N -> V (in Ref. 3; BAF62166)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="E -> D (in Ref. 1; CAP09533)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="D -> N (in Ref. 3; BAF62166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58751 MW; 4D7C523A29D20F74 CRC64;
MKKSHLVKRG LQDANQPSSQ PDKVGWIRRF SGKGIFREIW RNRFVMLKGD HLFIFEKEMK
NNGKTHEVFD LVHYERSEEL RKAKSHSKKN HSKFTLLRCQ HPGNKSPNLV FLAVSPEEKE
SWINVLNTAI TRAKNRVLDE VTIEEESLLA HPTRDRAKIP LGRRLPTRGH LMAVGSASSD
GMLTLDLVNE EDAAMLDEDE WLKDHRASLD KLAPGRRRAG TDASRPPASN TEAQEKTSSL
PRKSEISWSQ EDHPRTPQNK KKFAQVRNRC ASMDDALSRG ERKPKKNIPS PTGHLQDLIT
QRLQRTQELL AQIQEQEPHR GRMGSYPYLR GIDSPRLRHL KGSDSPHSKG SSSPHSANSP
SVRAKDSPSS KSKESPHAKS KDSPRFKSSK NALRSKSIDS PDSKESSSLH MKCIDLTHIK
GSQSPLSTGS NSPHMKSTDF YQMSYSPNFR NMKGGDSPLG EALDWDSRRA AAERLLQEAI
SSWREAKEVL AEVKELQARQ RREELSKTGM ASQKLQQKSP
