ID U3JH97_FICAL Unreviewed; 789 AA.
AC U3JH97;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Receptor interacting serine/threonine kinase 4 {ECO:0000313|Ensembl:ENSFALP00000002151.1};
GN Name=RIPK4 {ECO:0000313|Ensembl:ENSFALP00000002151.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002151.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002151.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002151.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_005037240.1; XM_005037183.2.
DR AlphaFoldDB; U3JH97; -.
DR STRING; 59894.ENSFALP00000002151; -.
DR Ensembl; ENSFALT00000002163.2; ENSFALP00000002151.1; ENSFALG00000002070.2.
DR GeneID; 101814635; -.
DR KEGG; fab:101814635; -.
DR CTD; 54101; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159908; -.
DR HOGENOM; CLU_015188_0_0_1; -.
DR OMA; HSKENTC; -.
DR OrthoDB; 5295000at2759; -.
DR Proteomes; UP000016665; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR CDD; cd14025; STKc_RIP4_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF65; RECEPTOR-INTERACTING SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 10.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 22..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 436..468
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 469..501
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 502..534
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 535..567
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 568..601
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 602..634
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 635..667
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 668..700
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 701..723
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 733..765
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 347..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 789 AA; 87300 MW; 9C186BADC3C9ABAA CRC64;
MARDGGSPWA MGLLKTFEES EFSSWEKIGS GGFGQVYKVR HLHWKTWLAI KCSPSLHVDE
KERMELLEEA RKMEMAKFRY ILPVYGICRE PVGLVMEYME TGSLEKLLAS EPLPWELRFR
IIHETAVGMN FLHCMSPPLL HLDLKPANIL LDAHYHVKIS DFGLAKCNGL SHSHDISMDG
LCGTIAYLPP ERIKEKNRCF DTKHDVYSFS IVVWGVLTQK KPFAEENNIL HIMVKVVKGH
RPELPAVSKS RPHSCNNLIK LMQKCWQDDP GARPTFQEIT SETEALCEKP EDETKEMITQ
DLDTKNAPEQ QPEGICALSQ KKQEPALPSV KDYSLSELLS QLDSGISQTM EGPEDLSRSS
SESKLASSDK RLSGVSSVDS AFSSRGSLSL SFERESSDIG TTDIQKRKLT EAILSGDTSK
LMKILQPQDV DIVLDGNSSL LHLAVEAGQE ECVKWLLLYN ANPNLTNKKG STPLHIAIEK
KFKSIVELIM ARKINVNAKD EDQWTALHFA AQNGDDFSTK MLLDKNASLN EVDFEGRAPI
HIACQYGQEN IVRILLRRGV NVNARGKDDW VPLHYAAWQG HLPIVKLLAK QRGADVNVQT
LDGRTSLHLA AQRGHYRVAR LLIDLESDVN VRNGLLQTAL HIAAETGHTS TSRLLLKHGA
DIEAATAEGY TALHLASRSG HLATAKLLLD ERAGVLARGP ADRTALHLAA ENGHSEVLEE
LVSAENIDVP DSQGLTALHL AARGGHAKAV EVLLKHGART DVPRAKGQPL LPPARQSRKS
SPTVLLSDT
//
