ID A7SIY5_NEMVE Unreviewed; 412 AA.
AC A7SIY5;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Ephrin RBD domain-containing protein {ECO:0000259|PROSITE:PS51551};
GN ORFNames=NEMVEDRAFT_v1g212995 {ECO:0000313|EMBL:EDO36327.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO36327.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO36327.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00884}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00884}.
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DR EMBL; DS469673; EDO36327.1; -; Genomic_DNA.
DR RefSeq; XP_001628390.1; XM_001628340.1.
DR AlphaFoldDB; A7SIY5; -.
DR STRING; 45351.A7SIY5; -.
DR EnsemblMetazoa; EDO36327; EDO36327; NEMVEDRAFT_v1g212995.
DR eggNOG; KOG3858; Eukaryota.
DR HOGENOM; CLU_667827_0_0_1; -.
DR InParanoid; A7SIY5; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; EPHRIN; 1.
DR PANTHER; PTHR11304:SF29; EPHRIN; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..124
FT /note="Ephrin RBD"
FT /evidence="ECO:0000259|PROSITE:PS51551"
FT REGION 135..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 45296 MW; 581EAA6893E31564 CRC64;
MNVAAMSKVK IVCPNPTSIV DKVQDDTPKE FLYENLWIVT EESYDKCNTT LSPRNKILLK
CDTPLSLKYY TVAFQQFSAT AQGLEFALGQ EYYFIATSDG TKSSLDKTSG GNCIKSNMRM
KFYICKSPQD PRCLPPTTAP PTTPSGCPTV PSTTQTPLPP KTNPTTEPTE SNEVPLLPTE
NSHTKSSLQS DDPKPTLRPS MAPAVTSIRP QVTKYSSQTE KEAIVREEPC SHDDDPRCLP
PTTAPPTTPS GCPTVPSTTQ TPLPPKTNPT TEPTESNEVP LLPTENSHTK SSLQSDDPKP
TLRPSMAPAV TSIRPQVTKY SSQTEKEAIV REEPCSHDHG IRPSWSIIIP LLIIIVLLIA
TNVFFVYQLK QIYTAKDSNI CESLDRRSER SKFTLASIGL GRRKDEASPV NV
//
