GenomeNet

Database: UniProt
Entry: F1N381_BOVIN
LinkDB: F1N381_BOVIN
Original site: F1N381_BOVIN 
ID   F1N381_BOVIN            Unreviewed;       999 AA.
AC   F1N381;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 3.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=MERTK {ECO:0000313|Ensembl:ENSBTAP00000007664.5,
GN   ECO:0000313|VGNC:VGNC:31391};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000007664.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000007664.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007664.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000007664.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007664.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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   RefSeq; NP_001178953.2; NM_001192024.2.
DR   AlphaFoldDB; F1N381; -.
DR   SMR; F1N381; -.
DR   STRING; 9913.ENSBTAP00000007664; -.
DR   PaxDb; 9913-ENSBTAP00000007664; -.
DR   Ensembl; ENSBTAT00000007664.5; ENSBTAP00000007664.5; ENSBTAG00000005828.5.
DR   GeneID; 504429; -.
DR   KEGG; bta:504429; -.
DR   CTD; 10461; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005828; -.
DR   VGNC; VGNC:31391; MERTK.
DR   eggNOG; ENOG502QQQ3; Eukaryota.
DR   GeneTree; ENSGT00940000155669; -.
DR   HOGENOM; CLU_015796_0_0_1; -.
DR   InParanoid; F1N381; -.
DR   OMA; QETRFGN; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF317402; -.
DR   Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000005828; Expressed in milk and 103 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0051250; P:negative regulation of lymphocyte activation; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0097350; P:neutrophil clearance; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0032940; P:secretion by cell; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05749; IgI_2_Axl_Tyro3_like; 1.
DR   CDD; cd14204; PTKc_Mer; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF257; TYROSINE-PROTEIN KINASE MER; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..999
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018659411"
FT   TRANSMEM        502..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..186
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          197..277
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          286..381
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          386..483
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          587..858
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          967..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   999 AA;  110605 MW;  0077881C7C7B543D CRC64;
     MGRAVLLFLP WLFLSALWTR AIAEMKEGTI PNLPFSGSLP GSLQADHTPF FFAHTGRYQP
     TAVSPPIHPG TPDPGNVAFP RVTSARSELL PPLAFNHTIG HIILSEHKDV KFNCSINIPN
     MYQDSATISW WKDGKELLGA HHAITQFYPD KEVTAVIASF SITSVQRSDN GSYICKMKIN
     SEEIVSDPIY IEVQGLPYFT RQPESMNVTR NTAFNLTCQA VGPPEPVNIY WVQNSRRVNE
     LPERSPSVLT VPGLTKTTIF SCEAHNQKGL TVSKSVQINI KAIPSPPTEV RVHNSSAHSI
     LISWVPGFDG YSPLSDCRIQ VKEVEPLSHG SVRIFNTSGS AHVYQIEQLQ ALANYSISVS
     CMNEVGWSAI SPWILASTTE GAPSVAPLNV TMFLNKSSNK VAVRWIKPPI KRQDGDLVGY
     HISHVWQNAE TSKELSEEVG QNSSLAQLSV QVHNATCTVR IAAVTKGGVG PFSDPVKIFI
     PALGSIDFAP SSTPAPGNTD PVLIILGCFC GFILIGLVLY ISLAIRKRIQ ETKFGSAFTE
     EDSELVISYM AKQSFCRQVI ELTLQSLGVS EELQNKLEDV MIDRSLLILG KILGEGEFGS
     VMEGNLNQED GTSQKVAVKT MKLDNFSQRE IEEFLSEAAC MKDFNHPNVI RLLGVCIEMS
     PQGIPRPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL LKFMVDIAQG MEYLSNRNFL
     HRDLAARNCM LRDDMTVCVA DFGLSKKIYS GDYYRQGRIA KMPVKWIAIE SLADRVYTSK
     SDVWAFGVTM WEIATRGMTP YPGVQNHEMY DYLLHGQRLK QPEDCLDELY EIMHSCWRAE
     PLDRPPFSVL RLQLKKLLES LPAVGDNTEV IYVNTQFPES AEGRAEGSAL TQLDLSIHPD
     SIIASCMPSA TISVVTAEVH EHRPQEERYI LNGGNEGWEE PAMASPATGT AEKNRVLPED
     TLVRNGVSWS QSSTLPLETS GPDELLFADD ASEGSELLT
//
DBGET integrated database retrieval system