ID W5N6J9_LEPOC Unreviewed; 571 AA.
AC W5N6J9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=PX domain containing serine/threonine kinase like {ECO:0000313|Ensembl:ENSLOCP00000016258.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016258.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016258.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01029316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015203482.1; XM_015347996.1.
DR AlphaFoldDB; W5N6J9; -.
DR STRING; 7918.ENSLOCP00000016258; -.
DR Ensembl; ENSLOCT00000016288.1; ENSLOCP00000016258.1; ENSLOCG00000013200.1.
DR GeneID; 102692946; -.
DR KEGG; loc:102692946; -.
DR CTD; 54899; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000017669; -.
DR HOGENOM; CLU_036868_0_0_1; -.
DR InParanoid; W5N6J9; -.
DR OMA; FTQYAST; -.
DR OrthoDB; 50529at2759; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000013200; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0045022; P:early endosome to late endosome transport; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0043271; P:negative regulation of monoatomic ion transport; IBA:GO_Central.
DR GO; GO:0006622; P:protein targeting to lysosome; IBA:GO_Central.
DR CDD; cd06871; PX_MONaKA; 1.
DR CDD; cd22062; WH2_DdVASP-like; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037903; MONaKA_PX.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR22999:SF40; PX DOMAIN-CONTAINING PROTEIN KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR22999; PX SERINE/THREONINE KINASE PXK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 14..126
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 149..443
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 542..561
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 436..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 64252 MW; DFEA3986976569D1 CRC64;
MAFMEKPSAG KILLDDTVPL TAVIEASQSL QSHTEYIIRV QRGVSTENSW QVIRRYSDFD
MLNNSLLISG LSLPLPPKKL IGNMDREFIA ERQKGLQTYL NFITTHHILS SCELVKKFLD
TSNYSANYTE IALQQVSMFF RSDPKWEVVE PLKDIGWRIR KRFFLIKNKD QPKERQVLNW
ADLGPDKFLS DKDLQSTMKL LPTVSHPFIC PVTFATASES SALVIRMFGE KGTLRDHICK
AKPKEPFLKK YCNPKKIQGL ELQQIRTFGR QILEVLKFLH DKGFPYGHLH ASNILLDGDT
CKLLDIENTL LGLPSYYRPH ATQFRKINTT EDIDVYSFGH LLYEMTYGRP PDAVPVDCFP
PAPSTSIVSV LQSILSTEAC KAGMPAVSQL LQNPLFSDIL LFNSERPQFK ISTKLKDALK
SAKENLERRL QEEQKMIHQH RRLTRAQSHH GSEEEKKKRK ILARKKSRQS AYENEEDLSM
KCNNSNNSGS GASSPLTSPS SPTPPPTAGV PPAPPPPPPP PPPPLNEPGL CQSPLLPVSD
PGRGALLGSI QNFAKGRLRK AEIKDRSNPL I
//
