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Database: UniProt
Entry: M4AQU5_XIPMA
LinkDB: M4AQU5_XIPMA
Original site: M4AQU5_XIPMA 
ID   M4AQU5_XIPMA            Unreviewed;      1021 AA.
AC   M4AQU5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSXMAP00000016840.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000016840.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000016840.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000016840.2};
RG   Ensembl;
RL   Submitted (NOV-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; M4AQU5; -.
DR   STRING; 8083.ENSXMAP00000016840; -.
DR   Ensembl; ENSXMAT00000016864.2; ENSXMAP00000016840.2; ENSXMAG00000016808.2.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000164552; -.
DR   HOGENOM; CLU_000288_7_40_1; -.
DR   InParanoid; M4AQU5; -.
DR   OMA; FGCLQLP; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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   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; 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; 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; 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; 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};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1021
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017387908"
FT   TRANSMEM        577..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..205
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          326..430
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          435..531
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          655..911
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          946..1010
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          523..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        68..187
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        104..114
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   1021 AA;  112495 MW;  D4C29FD16C08FF03 CRC64;
     MDACRTLAAL LWVLLLRRVQ VCQAEEVVLL NSKETQAELG WTSFPPNGWE EISGVDEKYK
     PIRTYQVCNV MEPTQQNNWL QTGWVARRGG QRIFVELQFT LRDCNSIPGV AGTCKETFNL
     LYVESDRDLG AVTREDRYSK IDTIAADESF TQGDLGERKM KLNTEVREIG HLNRKGFHLA
     FQDVGACVAL VAVRVYYKRC LATVQNLAVF PDTVAEAAFA TLVEVRGGCV NNSEVDSDSP
     PKMHCSAEGE WLVPIGKCSC SAGYEEGHSS CEACPPGSYK MSSRQQECFP CPANSVAEEE
     GSVVCVCEED HFRTPLDSPS TPCTRPPSPP RSLRFSLRQS SLVLDWAPPS DSGGRVDLTY
     SVGCRRCGPA RCEPCGPGVG FVPQQVGLTE RTVTVVNLLP NTNYTFSVEA LNGVSDLLPS
     KSFYTQVNVS TSLPPPSLIS ELRAEKVEEK SVTLVWREPP NPNSSRTEYE VKYYEKDQKD
     QSYSTVKTAA TRIIVNNLKP GTTYVFLIRP FLTPAPSSSL SSSALSSTSS TSASSSSSSS
     SSSSSTPPPI DYGAFSAPLE LQTLGELALA SSEQNPVVII VIVSVAALIM LLSMGAGLLL
     WRRQCGYSKA SQEGDEELYF QFKIPTRRTY IDPETCEDLL QAVHAFAKEL DNQSIKIERI
     VHTGDFGEVC RGCLKLPSKR ELPVAIRTLR AGCSDKQRRS FLSEAGILGQ FDHANIIRLE
     GVITTGNTMM IVEESMTNGA MDSFLRKHEG QLSVMQLMDM LTGVASGMKY LTEMGFVHKR
     LAAHKVLVNS NLTCKVSGFR PLQEEKIDSI YTTLHGGKSV VLWTAPEAIQ YRRFSSASDV
     WSFGIVMWEV MSYGERPYWD MGTQDVIKAI EDGFRLPAPV NCPPHLHQLM LDCWQKERAE
     RPGFSQIHSA LSKSVRSPDG IGSSTLARRT LSSSISLAER PLPSFPSFSS VGEWLDAVDM
     SRYKDNFTAA GYCYLESVAR MTVQDVLSLG VTSLDHQKLI LAAIQTLRAQ VIQMHGRGVQ
     V
//
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