ID A0A5N4CY85_CAMDR Unreviewed; 794 AA.
AC A0A5N4CY85;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Ephrin type-B receptor 4 {ECO:0000313|EMBL:KAB1263815.1};
GN ORFNames=Cadr_000023673 {ECO:0000313|EMBL:KAB1263815.1};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1263815.1, ECO:0000313|Proteomes:UP000299084};
RN [1] {ECO:0000313|EMBL:KAB1263815.1, ECO:0000313|Proteomes:UP000299084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1263815.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB1263815.1};
RX PubMed=30972949; DOI=.1111/1755-0998.13020;
RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA Burger P.A.;
RT "Improving Illumina assemblies with Hi-C and long reads: an example with
RT the North African dromedary.";
RL Mol. Ecol. Resour. 19:1015-1026(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB1263815.1}.
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DR EMBL; JWIN03000018; KAB1263815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N4CY85; -.
DR STRING; 9838.ENSCDRP00005021986; -.
DR Proteomes; UP000299084; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd10474; EphR_LBD_B4; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd09554; SAM_EPH-B4; 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; IPR037636; EPH-B4_SAM.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034290; EphB4_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; 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; 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 PRINTS; PR00014; FNTYPEIII.
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; 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; 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};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KAB1263815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000299084};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..794
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024418301"
FT TRANSMEM 538..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..202
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 323..432
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 436..529
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 714..778
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 774..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 86864 MW; 88BB0D8F000CB79E CRC64;
MELRALLCWA SLAAALEETL LNTKLETADL KWVTFPQEEG QWEELSGLDE EQHSVRTYEV
CDMQRAPGVA HWLRTGWVPR RGAVHVYATL RFTMLECLSL PQAGRSCKET FTVFYFESDA
DTATAHTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN IKTLRLGPLT KAGFYLAFQD
QGACMALLSL HLFYKKCAQL TVNLTRFPET VPRELVVPVA GSCVADAVPG PGPSPSLYCR
EDGQWAEQPV TGCSCAQGFE AAEGNTRCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSP
ICQCRIGYFR ARTDPRGAPC TTPPSAPRSV VPRLNGSSLR LEWSAPLESG GREDLTYALR
CRECRPGGSC TPCGGDLTFD PGPRDLVEPW VAIRGLRPDF TYTFEVTALN GVSSLASGPV
PFEAVNVTTD REVPPPVSDI RVTRSSPSSL SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS
SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE NESWREQLAL
IAGTAVVGVV LVLVVVVIAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
EAVREFAKEI DVSYVKIEEV IGADVLTQCF HLSFQVINAI EQDYRLPPPP DCPTSLHQLM
LDCWQKDRNA RPRFPQVVSA LDKMIRNPAS LKIVARENGG ASHPLLDQRQ PHYSAFGSVG
EWLRAIKMGR YEESFAAAGF GSFELVSQIS TEDLLRIGVT LAGHQKKILA SVQHMKSQAK
PGAPGGSAAP APQY
//
