ID A0A3B5AU30_9TELE Unreviewed; 959 AA.
AC A0A3B5AU30;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSSPAP00000017042.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000017042.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000017042.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B5AU30; -.
DR STRING; 144197.ENSSPAP00000017042; -.
DR Ensembl; ENSSPAT00000017306.1; ENSSPAP00000017042.1; ENSSPAG00000012696.1.
DR GeneTree; ENSGT00940000164552; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05064; PTKc_EphR_A10; 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; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF16; EPHRIN TYPE-A RECEPTOR 10; 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; 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 SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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; PS50011; PROTEIN_KINASE_DOM; 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}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 528..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..174
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 295..403
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 419..517
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 606..862
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 884..948
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT DISULFID 37..156
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 73..83
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 959 AA; 106074 MW; F95D653DECBAE6D9 CRC64;
SKETQAELGW TSYPPNGWEE ISGVDEKYKP IRTYQVCNVM EPTQQNNWLQ TGWVARRGGQ
RIFVELQFTL RDCNSIPGVA GTCKETFNLL YVESDRDLGG VTREDRYTKI DTIAADESFT
QGDLGERKMK LNTEVREIGH LNRKGFHLAF QDVGACVALV AVRVYYKRCL ATVQNLAVFP
DTVAEAAFAT LVEVRGACVN NSEVDTDSPP RMHCSAEGEW LVPIGKCSCS AGYEEGHSSC
EACPPGSYKM SSRQQECFPC PANSVAEEEG SVVCMCEEDH FRTPLDNPSA PCTRPPSPPR
DLVYTLKQST LILEWSAPSD SGGRVDLTYS VGCRRCVGRQ CEPCGASVGF VPQQVGLTER
TVTVVNLLPN TNYTFTVEAL NGVSELLPSK RFYTQVNVST SLPGESNSVF PDSAFFLSPP
AAPSLISELR AEKIEQKSIT LVWREPSYPN SSRTEYEVKY YEKEQKDQSY STVKTAATRI
SVNNLKPGTT YVFLIRPFST PAPSSSLSSS QLSSSSSSTS SSSSQSPVVI IVVVSVAALI
MLLSMGVGLL IWRRQCGYSK ASQEGDEELY FQFKIPTRRT YIDPETCEDL LQAVHAFAKE
LDNSSIKIER IVHTGDFGEV CRGCLKLPSK RELPVAIKTL RAGCSDKQRR SFLSEAGILG
QFDHANIIRL EGVITTGNTM MIIVESMSNG ALDSFLRKHE GQLSVMQLMD MLTGVASGMK
YLTEMGFVHK RLAAHKVLVN SNLGCKVSGF RPLQEDKIEA IYTTLHGGKS VVLWTAPEAI
QYHRFSSASD VWSFGIVMWE VMSYGERPYW DMGNQDVIKA IEDGFRLPAP VNCPPHLHQL
MLDCWQKERT ERPSFSQIHS ALSKSIRSPD GIGSSTLRPL PSFPSFSSVG EWLDAVDMGR
YKDNFTAAGY CYLESVARMT VQDVLSLGIT SLDHQKLILA AIQTLRAQVI QMHGRGVQV
//
