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Database: UniProt
Entry: A0A3P9C9T1_9CICH
LinkDB: A0A3P9C9T1_9CICH
Original site: A0A3P9C9T1_9CICH 
ID   A0A3P9C9T1_9CICH        Unreviewed;       208 AA.
AC   A0A3P9C9T1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Ephrin-A2 {ECO:0000313|Ensembl:ENSMZEP00005019043.1};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005019043.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005019043.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005019043.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-
CC       anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00884, ECO:0000256|RuleBase:RU004375}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00884}.
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DR   RefSeq; XP_004540248.1; XM_004540191.1.
DR   AlphaFoldDB; A0A3P9C9T1; -.
DR   STRING; 106582.ENSMZEP00005019043; -.
DR   Ensembl; ENSMZET00005019656.1; ENSMZEP00005019043.1; ENSMZEG00005014287.1.
DR   GeneID; 101485854; -.
DR   KEGG; mze:101485854; -.
DR   CTD; 30218; -.
DR   GeneTree; ENSGT00940000160040; -.
DR   OrthoDB; 2881104at2759; -.
DR   Proteomes; UP000265160; LG19.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR   CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR031328; Ephrin.
DR   InterPro; IPR034252; Ephrin-A_Ecto.
DR   InterPro; IPR019765; Ephrin_CS.
DR   InterPro; IPR001799; Ephrin_RBD.
DR   PANTHER; PTHR11304; EPHRIN; 1.
DR   PANTHER; PTHR11304:SF69; EPHRIN-A2; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00884}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004375};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..208
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017949066"
FT   TRANSMEM        186..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..168
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   DISULFID        68..108
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00884"
SQ   SEQUENCE   208 AA;  24222 MW;  A3684EFA83B7D23E CRC64;
     MSMMLCQLGQ KCVMEVVLLA ILSWVSVWAE EKIIFDRHAV YWNSSNPKFW HGEYRVAVNI
     NDYLDIYCPY YEGPPSHGRM ERYILFMVNH EGYTSCQHRM RGFKRWECNR PTGPDGPLRF
     SEKFQLFTPF SLGFEFRPGH EYYYISSPHP NHVGRACLKL KVYVRPPDGS GYDSPEPFLT
     DGSSSWRAGC MTLLAALASL FLGLFYWL
//
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