ILK_CHICK
ID ILK_CHICK Reviewed; 452 AA.
AC Q9DF58;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Integrin-linked protein kinase {ECO:0000250|UniProtKB:Q13418};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q13418};
DE AltName: Full=59 kDa serine/threonine-protein kinase {ECO:0000250|UniProtKB:Q13418};
DE AltName: Full=Beta-integrin-linked kinase {ECO:0000250|UniProtKB:P57044};
DE AltName: Full=ILK-1 {ECO:0000250|UniProtKB:Q13418};
DE AltName: Full=ILK-2 {ECO:0000250|UniProtKB:Q13418};
DE AltName: Full=p59ILK {ECO:0000250|UniProtKB:Q13418};
GN Name=ILK {ECO:0000250|UniProtKB:Q13418};
GN Synonyms=ILK1 {ECO:0000250|UniProtKB:Q13418},
GN ILK2 {ECO:0000250|UniProtKB:Q13418};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:AAG18430.1};
RN [1] {ECO:0000312|EMBL:AAG18430.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gizzard {ECO:0000312|Proteomes:UP000000539};
RX PubMed=11278951; DOI=10.1074/jbc.m011634200;
RA Deng J.T., Van Lierop J.E., Sutherland C., Walsh M.P.;
RT "Ca2+-independent smooth muscle contraction. a novel function for integrin-
RT linked kinase.";
RL J. Biol. Chem. 276:16365-16373(2001).
RN [2] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3] {ECO:0000305}
RP INTERACTION WITH PXN.
RX PubMed=15817463; DOI=10.1074/jbc.m500752200;
RA LaLonde D.P., Brown M.C., Bouverat B.P., Turner C.E.;
RT "Actopaxin interacts with TESK1 to regulate cell spreading on
RT fibronectin.";
RL J. Biol. Chem. 280:21680-21688(2005).
CC -!- FUNCTION: Receptor-proximal protein kinase regulating integrin-mediated
CC signal transduction. May act as a mediator of inside-out integrin
CC signaling. {ECO:0000250|UniProtKB:Q13418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q13418};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13418};
CC -!- SUBUNIT: Interacts with PXN/PAXILLIN (via LD motif 4).
CC {ECO:0000269|PubMed:15817463}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q13418}. Cell membrane
CC {ECO:0000250|UniProtKB:Q13418}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13418}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q13418}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O55222}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:Q13418}.
CC -!- PTM: Autophosphorylated on serine residues.
CC {ECO:0000250|UniProtKB:Q13418}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF296130; AAG18430.1; -; mRNA.
DR EMBL; AADN05001070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989525.1; NM_204194.1.
DR AlphaFoldDB; Q9DF58; -.
DR SMR; Q9DF58; -.
DR STRING; 9031.ENSGALP00000027964; -.
DR Ensembl; ENSGALT00000081529; ENSGALP00000048764; ENSGALG00000031642.
DR GeneID; 374018; -.
DR KEGG; gga:374018; -.
DR CTD; 3611; -.
DR VEuPathDB; HostDB:geneid_374018; -.
DR GeneTree; ENSGT00940000155956; -.
DR HOGENOM; CLU_000288_7_5_1; -.
DR OMA; NMADAKF; -.
DR OrthoDB; 740146at2759; -.
DR PhylomeDB; Q9DF58; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000031642; Expressed in granulocyte and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0030030; P:cell projection organization; IEA:Ensembl.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0021675; P:nerve development; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR CDD; cd14057; PK_ILK; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035692; PK_ILK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cell junction; Cell membrane; Cell projection;
KW Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..452
FT /note="Integrin-linked protein kinase"
FT /id="PRO_0000451828"
FT REPEAT 33..62
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 66..95
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 99..128
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT DOMAIN 193..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 199..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 452 AA; 51518 MW; 99E5EE272F80F680 CRC64;
MDDIFTQCRE GNAVAVRLWL DNTENDLNQG DDHGFSPLHW ACREGRSNVV DMLIMRGARI
NVMNRGDDTP LHLAASHGHR DIVQKLIQFK ADINAVNEHG NTPLHYACFW GHDTVAEDLV
GNGALVSIAN KYSETPIDKA KMPLREILKE RAEKLGQNLT KIPYKDTFWK GTTRTRPRNG
TLNKLAGIDF KQLSLSQKLN ENQSGELWKG RWQGNDIVIK MLKIRDWTTR KSRDFNEEYP
KLRIFSHPNV LPVLGACQSP PAPHPIVISH WMPYGSLYNV LHEGTNFVVD QMQAVKFAFD
IARGMAFLHT LEPLIPRHHL NSRSIMIDED MTARISMADV KFSFQCPGRM YAPAWVAPEA
LQKKPEEINR RSADMWSFAV LLWELVTREV PFADLSNMEI GMKVALEGLR PTIPPGISPH
ICKLMKICMN EDPAKRPKFD MIVPILEKMQ DK
