GenomeNet

Database: UniProt
Entry: E9PSX9_RAT
LinkDB: E9PSX9_RAT
Original site: E9PSX9_RAT 
ID   E9PSX9_RAT              Unreviewed;       879 AA.
AC   E9PSX9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   05-JUN-2019, entry version 71.
DE   SubName: Full=Axl receptor tyrosine kinase {ECO:0000313|Ensembl:ENSRNOP00000028132};
GN   Name=Axl {ECO:0000313|Ensembl:ENSRNOP00000028132,
GN   ECO:0000313|RGD:620028};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000028132, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000028132, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028132,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000028132}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000028132};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; Evidence={ECO:0000256|SAAS:SAAS01168082};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|SAAS:SAAS00941529}.
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DR   EMBL; AABR07002708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07002709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07002710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; E9PSX9; -.
DR   PeptideAtlas; E9PSX9; -.
DR   PRIDE; E9PSX9; -.
DR   Ensembl; ENSRNOT00000028132; ENSRNOP00000028132; ENSRNOG00000020716.
DR   RGD; 620028; Axl.
DR   eggNOG; ENOG410IG6I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00940000160232; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020716; Expressed in 10 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; E9PSX9; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019838; F:growth factor binding; TAS:RGD.
DR   GO; GO:0032036; F:myosin heavy chain binding; IPI:RGD.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0030154; P:cell differentiation; IMP:RGD.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
DR   GO; GO:0001779; P:natural killer cell differentiation; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR   GO; GO:0030168; P:platelet activation; IBA:GO_Central.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IBA:GO_Central.
DR   GO; GO:0042246; P:tissue regeneration; TAS:RGD.
DR   GO; GO:0048771; P:tissue remodeling; TAS:RGD.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00600564};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
KW   Immunoglobulin domain {ECO:0000256|SAAS:SAAS00941986};
KW   Kinase {ECO:0000256|SAAS:SAAS00601152};
KW   Membrane {ECO:0000256|SAAS:SAAS00602125, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00600689};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:E9PSX9};
KW   Receptor {ECO:0000256|SAAS:SAAS00600436};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS00601608};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00600943,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00582553}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    879       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003245325.
FT   TRANSMEM    435    457       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    122       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      133    216       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      221    325       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      330    422       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      521    792       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   REGION      811    839       Disordered. {ECO:0000256|MobiDB-lite:
FT                                E9PSX9}.
FT   REGION      856    879       Disordered. {ECO:0000256|MobiDB-lite:
FT                                E9PSX9}.
SQ   SEQUENCE   879 AA;  97191 MW;  BEEF104A28017F06 CRC64;
     MGRVPLAWCV ALCCWGCAAP KDTQTEADSP FVGNPGNITG ARGLTGTLRC ELQVQGEPPE
     VMWLRDGQIL ELADNTQTQV PLGEDWQDEW KVVSQLRISA LQLSDAGEYQ CMVHLEGRTF
     VSQPGFVGLE GLPYFLEEPE DKAVPANTPF NLSCQAQGPP EPVTLLWLQD AVPLAPVAGY
     SFQHSLQAPG LNKTSSFSCE AHNAKGVTTS RTATITVLPQ RPHNLHVVSR HPTELEVAWI
     PSLSGIYPLT HCTLQAVLSD DGVGVWLGES DPPEEPLTVQ VSVPPHQLRL EKLLPHTPYH
     IRVSCTSSQG PSPWTHWLPV ETTEGVPLGP PENVSAMRNG SQALVRWQEP REPLQGTLLG
     YRLAYRGQDT PEVLMDIGLT REVTLELRGD RPVANLTVSV AAYTSAGDGP WSLPVPLEPW
     RPVSEPPPPA FSWPWWYVLL GALVAAACVL ILTLFLVHRR KKETRYGEVF EPTVERGELV
     VRYRARKSYS RRTTEATLNS LGISEELKEK LRDVMVDRHK VALGKTLGEG EFGAVMEGQL
     NQDDSILKVA VKTMKIAICT RSELEDFLSE AVCMKEFDHP NVMRLIGVCF QGSDREGFPE
     PVVILPFMKH GDLHSFLLYS RLGDQPVFLP TQMLVKFMAD IASGMEYLST KRFIHRDLAA
     RNCMLNENMS VCVADFGLSK KIYNGDYYRQ GRIAKMPVKW IAIESLADRV YTSKSDVWSF
     GVTMWEIATR GQTPYPGVEN SEIYDYLRQG NRLKQPLDCL DGLYALMSRC WELNPRDRPS
     FAELREDLEN TLKALPPAQE PDEILYVNMD EGGSHLEPRG AAGGADPPTQ PDPKDSCSCL
     TEADVHSAGR YVLCPSTAPG PTLSADRGCP APPGQEDGA
//
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