ID A0A3B5JUL6_TAKRU Unreviewed; 1079 AA.
AC A0A3B5JUL6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha-protein kinase 3 {ECO:0008006|Google:ProtNLM};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000048027.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000048027.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000048027.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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DR AlphaFoldDB; A0A3B5JUL6; -.
DR Ensembl; ENSTRUT00000052634.2; ENSTRUP00000048027.2; ENSTRUG00000004542.3.
DR GeneTree; ENSGT00940000158534; -.
DR InParanoid; A0A3B5JUL6; -.
DR OMA; YMESTRT; -.
DR Proteomes; UP000005226; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16973; Alpha_kinase_ALPK3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 63..154
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 657..745
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 773..1004
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 119405 MW; 26E47C20D9E38F4C CRC64;
MTSRRPMIRT YSSNGRTSSF SEEEGSSSNG RSESRNTYLS NVRPENRSTL CSVMAQLTED
IQPSFERTLK SKAVSENCNV KFTCVVSGYP APELKWYKDD REMDRYCGLP KYEIHRNGKT
HTLHIYNCTL DDAAIYQVSA SNSKGIVSCS GVLEVGDMNE YKIHQRFFSK LKQKAENKKK
NETEAQSKKT VDKENIQKAK QQISPERPPR KRHVPPPAPS PAIKEAAAVE QQGAAGEING
VSPEVMEAAQ MPFKDKETDK DEALSEKALA TKKMKISNGV DAEVDSDKME SSGEYLSQDN
SSVRLPQMAT VPVINVSCID PKQDEALSLD GHSSDGRKII ETPAAPAFVV PPISVTSHDG
ECALKPSTQN DSAETESTVT AMRVTKQNVD NAATEKSDKP QIRKQSHEEA TEKRSKESTL
SAMGDGFTPN VGSDGSSLNK TADDGVLPEN TEKKTHKEAK IENFVSVLDY QRNHPSVDRL
ASKPPTHPSL SPSSLRKFMS KAVQELDIEI SGGHQSDKPE DDLSGGSTPT LPLSCESSPR
MKRRDSLTLI RSATPEELAS GARRKIFMPR PKEDGEGTQD RKDSPYMSPS QARRAALLQC
PTGQSTPPME RRSPLVGRRM DMLAVPKFMD EPSTDEPDGT KKEEKQTQKK LDPLKAPQVI
RKIRAEPFPD ASGHLKLWCQ FFNVLLDSTI KWFRDEEEIL EMRRSGGDES QAALAIILAA
SQDCGVYGCS ISNEYGADTT DFLLSVDVLS QILLKDELEV GEEIEMTPLL FTKGLADWGS
WGEKYFGRIM TETLHVGSGC AHKASRVRVI YGLDPIFESG STCIVKVGNP VAYGTKPECS
LAERNGAITK QECKVQNTIR EYCKIFAAEA RVSENFGFLL EVIPQYLIYR PANSVPYATV
EADLKGQCLK HCTMDPKGKL ITQTASEVEQ KCSTFQHWIH QWTHGNLLVT QMEGVETKLT
NIRVVTKSKG YQGLTESGSP EVFEQFLTHH QCNYYCGLLG LIPLKTLESL QPPKAKGSRS
PLLNRKLGSS SPQMQRKGQS PQMSRKANSS PKVARKVQET EDDKSGGKSR LTETSVEMR
//
