ID H2PLG9_PONAB Unreviewed; 1503 AA.
AC H2PLG9; A0A2J8RU65;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=LMTK2 isoform 1 {ECO:0000313|EMBL:PNJ12071.1};
DE SubName: Full=Lemur tyrosine kinase 2 {ECO:0000313|Ensembl:ENSPPYP00000019451.3};
GN Name=LMTK2 {ECO:0000313|Ensembl:ENSPPYP00000019451.3};
GN ORFNames=CR201_G0048461 {ECO:0000313|EMBL:PNJ12071.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019451.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019451.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ12071.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ12071.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000019451.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; NDHI03003648; PNJ12071.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000019451; -.
DR Ensembl; ENSPPYT00000020218.3; ENSPPYP00000019451.3; ENSPPYG00000017360.3.
DR eggNOG; ENOG502QSD2; Eukaryota.
DR GeneTree; ENSGT00940000158475; -.
DR HOGENOM; CLU_004618_0_0_1; -.
DR OMA; SHKSVSC; -.
DR OrthoDB; 2910608at2759; -.
DR TreeFam; TF332280; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070853; F:myosin VI binding; IEA:Ensembl.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0045022; P:early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IEA:Ensembl.
DR GO; GO:0001881; P:receptor recycling; IEA:Ensembl.
DR GO; GO:0033572; P:transferrin transport; IEA:Ensembl.
DR CDD; cd05086; PTKc_Aatyk2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24417; SERINE/THREONINE-PROTEIN KINASE LMTK1; 1.
DR PANTHER; PTHR24417:SF8; SERINE_THREONINE-PROTEIN KINASE LMTK2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158385"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..407
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 596..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1503 AA; 164922 MW; B02D013121B8917A CRC64;
MPGPPALRRR LLLLLLVLLI AGSAAAAPLP QTGAGEAPPA AEVSSSFVIL CVCSLIILIV
LIANCVSCCK DPEIDFKEFE DNFDDEIDFT PPAEDTPSVQ SPAEVFTLSV PNISLPAPSQ
FQPSVEGLKS QVARHSLNYI QEIGNGWFGK VLLGEIYTGT SVARVIVKEL KASASPKEQD
TFLKNGEPYY ILQHPNILQC VGQCVEAIPY LLVFEFCDLG DLKAYLRTEQ EHMRGDSQTM
LLQRMACEIA AGLAAMHKLH FLHSDLALRN CFLTSDLNVK VGDYGIGFSR YKEDYIETDD
KKVFPLRWTA PELVTSFQDR LLTADQTKYS NIWSLGVTLW ELFDNATQPY SNLSNLDVLN
QVIRERDTKL PKPQLEQPYS DRWYEVLQFC WLSPEKRPAA EDVHRLLTYL RLQSQRDSEV
DFEQQWNALK PNTNSRDSSN NAAFPILDHF ARDRLGREME EVLTVTETSQ GLSFEYVWEA
AKHDHFDERS QGHLDEALSY TSIFYPVEVF ESSLSDPGPG KQDDSGQDVP LRVPGVVPVF
DAHNLSVGSD YYIQLEEKSG SNLELDYPPA LLTTDMDNPE RTGPEPSQLT ALRSVELEES
STDEDFFQSS TDPKDSSVPG DLHMTSGPES PFNNIFNDLD KSEDLPSHQK IFDLMELNGV
QADFKPATLS SSLDNPKESV ITGHFEKEKP RKLFDSEPLC LSDNLMHQDN FDPLNVQELS
ENFLFLQEKN LLKGSLSSKE HINDLQTELK NAGFTEAMLE TSRRNSLDTE LQFAENKPGL
SLLQENISTK GDDTDVMLTG DTLSTSLQSS PEVQVPPTSF ETEETPRRVP PDSLPTQGET
QPTCLDVIVP EDCLCQDISP DAVTVPVEIL STDAKTHSLD DRSQDSPGES EETLQLTESN
SVLADDILAS RVSVGSSLPE LGQEVHNKPF SEDHHSHRQL EKNLEAVETL NRLNSKDAAK
EAGLVSALSS DSTSQDSLLE DSLSAPFPAS EPSLETPDSL ESVDVHEALL DSLGSHTPQK
LVPPDKPADS GYETENLESP EWTLHPAPEG TADSEPATAG DGGHSGLPPN PVIVISDAGD
GHRGTEVTPQ TFTAGSQGSY RDSAYFSDND SEPEKRSEEV PGTSPSALVL VQEQPLPEPV
LPEQSPAAQD SCLEARKSQP DESCLSALHN SSDLELRATP EPAQTGVAQQ VHPTEDEASS
PWSVLNAELS SGDDFETQDD HPCTLASTGT NTNELLAYTN SALDKSLSSH TEGLKLKEPD
IEGKYLGKLG VSGMLDLSED GMDADEEDEN SDDSDEDLRA FNLHSLSSES EDETEHPVPI
ILSNEDGRHL RSLLKPTAAD APDPLPEDWK KEKKAVTFFD DVTVYLFDQE TPTKELGPCG
GEACGPDLSS PAPASGSPYL SRCINSESST DEEGGGFEWD DDFSPDPFMS KTTSNLLSSK
PSLQTSKYFS PPPPARSTEQ SWPHLAPYSR FSISPANIAS FSLTHLTDSD IEQGGSSEDG
EKD
//
