ID A0A2Y9G0E9_TRIMA Unreviewed; 964 AA.
AC A0A2Y9G0E9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=LOC101360928 {ECO:0000313|RefSeq:XP_012411204.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_012411204.1};
RN [1] {ECO:0000313|RefSeq:XP_012411204.1}
RP IDENTIFICATION.
RG RefSeq;
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_012411204.1; XM_012555750.2.
DR AlphaFoldDB; A0A2Y9G0E9; -.
DR STRING; 127582.A0A2Y9G0E9; -.
DR GeneID; 101360928; -.
DR InParanoid; A0A2Y9G0E9; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd10477; EphR_LBD_B2; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR CDD; cd09552; SAM_EPH-B2; 1.
DR CDD; cd00185; TNFRSF; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034238; EphB2_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF11; EPHRIN TYPE-B RECEPTOR 2; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_012411204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
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 TRANSMEM 520..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..179
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 301..411
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 412..507
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 599..862
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 891..955
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 724
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 605..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 39..161
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 74..84
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 964 AA; 107565 MW; 32E81CFBDF8B047B CRC64;
MDSTTATAEL GWIVHPPSGW EEVSGYDENM NTIRTYQVCN VFESSQNNWL RTKFIRRRGA
HRIHVEMKFS VRDCSSIPSV PGSCKETFNL YYYEADYDSA TKTFPSWMEN PWVKVDTIAA
DESFSQVDLG GRVMKINTEV RSFGPVSRNG FYLAFQDYGG CMSLIAVHVF YRKCPRVIQN
GAIFQETLSG AESTSLVAAR GSCIANAEEV DVPIKLYCNG DGEWLVPIGR CMCKAGFEAV
ENGTVCRGCP SGTFKANQGD EACTHCPINS RTTSEGATNC VCRNGYYRAD LDPLDMPCTT
IPSAPQAVIS SVNETSLMLE WTPPRDSGGR EDLVYNIICK SCGSGRGACT RCGDNVQYAP
RQLGLTEPRI YISDLLAHTQ YTFEIQAVNG VTDQSPFSPQ FASVNITTNQ AAPSAVSIMH
QVSRTVDSIT LSWSQPDQPN GVILDYELQY YEKELSEYNA TAIKSPTNTV TVQGLKAGAI
YVFQVRARTV AGYGRYSGKM YFQTMTEAEY QTSIQEKLPL IIGSSAAGLV FLIAVVVIAI
VCNRRRGFER ADSEYTDKLQ HYTSGHMTPG MKIYIDPFTY EDPNEAVREF AKEIDISCVK
IEQVIGAGEF GEVCSGHLKL PGKREIFVAI KTLKSGYTEK QRRDFLSEAS IMGQFDHPNV
IHLEGVVTKS TPVMIITEFM ENGSLDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLADMNY
VHRDLAARNI LVNSNLVCKV SDFGLSRFLE DDTSDPTYTS ALGGKIPIRW TAPEAIQYRK
FTSASDVWSY GIVMWEVMSY GERPYWDMTN QDVINAIEQD YRLPPPMDCP SALHQLMLDC
WQKDRNHRPK FGQIVNTLDK MIRNPNSLKA MAPLSSGINL PLLDRTIPDY TSFNTVDEWL
EAIKMGQYKE SFANAGFTSF DVVSQMMMED ILRVGVTLAG HQKKILNSIQ VMRAQMNQIQ
SVEV
//
