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Q00993

- UFO_MOUSE

UniProt

Q00993 - UFO_MOUSE

Protein

Tyrosine-protein kinase receptor UFO

Gene

Axl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TENC1. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response.2 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    Activated by GAS6-binding and subsequent autophosphorylation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei561 – 5611ATPPROSITE-ProRule annotation
    Active sitei666 – 6661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi536 – 5449ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylserine binding Source: Ensembl
    3. protein heterodimerization activity Source: MGI
    4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic cell clearance Source: UniProtKB
    2. blood vessel remodeling Source: MGI
    3. cell maturation Source: Ensembl
    4. cellular response to extracellular stimulus Source: MGI
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. cellular response to interferon-alpha Source: Ensembl
    7. cellular response to lipopolysaccharide Source: Ensembl
    8. dendritic cell differentiation Source: Ensembl
    9. enzyme linked receptor protein signaling pathway Source: MGI
    10. erythrocyte homeostasis Source: MGI
    11. forebrain cell migration Source: MGI
    12. inflammatory response Source: MGI
    13. innate immune response Source: UniProtKB-KW
    14. natural killer cell differentiation Source: MGI
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of dendritic cell apoptotic process Source: Ensembl
    17. negative regulation of interferon-gamma production Source: Ensembl
    18. negative regulation of lymphocyte activation Source: MGI
    19. negative regulation of neuron apoptotic process Source: MGI
    20. negative regulation of tumor necrosis factor production Source: MGI
    21. neuron migration Source: MGI
    22. organ regeneration Source: Ensembl
    23. ovulation cycle Source: MGI
    24. phagocytosis Source: MGI
    25. platelet activation Source: MGI
    26. positive regulation of cytokine-mediated signaling pathway Source: Ensembl
    27. positive regulation of natural killer cell differentiation Source: Ensembl
    28. positive regulation of protein kinase B signaling Source: UniProtKB
    29. protein kinase B signaling Source: MGI
    30. secretion by cell Source: MGI
    31. spermatogenesis Source: MGI
    32. substrate adhesion-dependent cell spreading Source: MGI
    33. vagina development Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Differentiation, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase receptor UFO (EC:2.7.10.1)
    Alternative name(s):
    Adhesion-related kinase
    Gene namesi
    Name:Axl
    Synonyms:Ark, Ufo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1347244. Axl.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular space Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 888870Tyrosine-protein kinase receptor UFOPRO_0000024482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi50 ↔ 111PROSITE-ProRule annotation
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi154 ↔ 199PROSITE-ProRule annotation
    Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Modified residuei697 – 6971Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei773 – 7731Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei815 – 8151Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei860 – 8601Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion By similarity.By similarity
    Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ00993.
    PRIDEiQ00993.

    PTM databases

    PhosphoSiteiQ00993.

    Miscellaneous databases

    PMAP-CutDBQ80YQ3.

    Expressioni

    Tissue specificityi

    In distinct substructures of a broad spectrum of developing tissues (in the late embryogenesis). In cells forming organ capsules as well as in connective tissue structures (in adult).

    Gene expression databases

    ArrayExpressiQ00993.
    BgeeiQ00993.
    CleanExiMM_AXL.
    GenevestigatoriQ00993.

    Interactioni

    Subunit structurei

    Heterodimer and heterotetramer with ligand GAS6 By similarity. Interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1 and TENC1. Part of a complex including AXL, TNK2 and GRB2, in which GRB2 promotes AXL recruitment by TNK2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204922. 1 interaction.
    IntActiQ00993. 2 interactions.
    STRINGi10090.ENSMUSP00000002677.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00993.
    SMRiQ00993. Positions 29-417, 485-836.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 445427ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini467 – 888422CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei446 – 46621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 12293Ig-like C2-type 1Add
    BLAST
    Domaini133 – 21684Ig-like C2-type 2Add
    BLAST
    Domaini221 – 325105Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini330 – 42293Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini530 – 801272Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 8668Interaction with GAS6By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108377.
    HOGENOMiHOG000231685.
    HOVERGENiHBG006346.
    InParanoidiQ80YQ3.
    KOiK05115.
    OMAiQVQGEPP.
    OrthoDBiEOG77DJ5C.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00060. FN3. 2 hits.
    SM00409. IG. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q00993-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRVPLAWWL ALCCWGCAAH KDTQTEAGSP FVGNPGNITG ARGLTGTLRC    50
    ELQVQGEPPE VVWLRDGQIL ELADNTQTQV PLGEDWQDEW KVVSQLRISA 100
    LQLSDAGEYQ CMVHLEGRTF VSQPGFVGLE GLPYFLEEPE DKAVPANTPF 150
    NLSCQAQGPP EPVTLLWLQD AVPLAPVTGH SSQHSLQTPG LNKTSSFSCE 200
    AHNAKGVTTS RTATITVLPQ RPHHLHVVSR QPTELEVAWT PGLSGIYPLT 250
    HCNLQAVLSD DGVGIWLGKS DPPEDPLTLQ VSVPPHQLRL EKLLPHTPYH 300
    IRISCSSSQG PSPWTHWLPV ETTEGVPLGP PENVSAMRNG SQVLVRWQEP 350
    RVPLQGTLLG YRLAYRGQDT PEVLMDIGLT REVTLELRGD RPVANLTVSV 400
    TAYTSAGDGP WSLPVPLEPW RPGQGQPLHH LVSEPPPRAF SWPWWYVLLG 450
    ALVAAACVLI LALFLVHRRK KETRYGEVFE PTVERGELVV RYRVRKSYSR 500
    RTTEATLNSL GISEELKEKL RDVMVDRHKV ALGKTLGEGE FGAVMEGQLN 550
    QDDSILKVAV KTMKIAICTR SELEDFLSEA VCMKEFDHPN VMRLIGVCFQ 600
    GSDREGFPEP VVILPFMKHG DLHSFLLYSR LGDQPVFLPT QMLVKFMADI 650
    ASGMEYLSTK RFIHRDLAAR NCMLNENMSV CVADFGLSKK IYNGDYYRQG 700
    RIAKMPVKWI AIESLADRVY TSKSDVWSFG VTMWEIATRG QTPYPGVENS 750
    EIYDYLRQGN RLKQPVDCLD GLYALMSRCW ELNPRDRPSF AELREDLENT 800
    LKALPPAQEP DEILYVNMDE GGSHLEPRGA AGGADPPTQP DPKDSCSCLT 850
    AADVHSAGRY VLCPSTAPGP TLSADRGCPA PPGQEDGA 888
    Length:888
    Mass (Da):98,191
    Last modified:July 27, 2011 - v2
    Checksum:iC5350E3A8995E975
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti394 – 3941A → R in CAA42158. (PubMed:1840679)Curated
    Sequence conflicti486 – 4861G → P in CAA42158. (PubMed:1840679)Curated
    Sequence conflicti566 – 5661A → V in CAA42158. (PubMed:1840679)Curated
    Sequence conflicti768 – 7681C → F in CAA45097. (PubMed:1320243)Curated
    Sequence conflicti774 – 7741A → S in CAA45097. (PubMed:1320243)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63535 mRNA. Translation: CAA45097.1.
    X59560 Genomic DNA. Translation: CAA42158.1.
    AK155567 mRNA. Translation: BAE33327.1.
    CH466593 Genomic DNA. Translation: EDL24236.1.
    BC046618 mRNA. Translation: AAH46618.1.
    BC050914 mRNA. Translation: AAH50914.1.
    CCDSiCCDS20996.1.
    PIRiS23065.
    S23251.
    RefSeqiNP_033491.2. NM_009465.4.
    XP_006540052.1. XM_006539989.1.
    XP_006540053.1. XM_006539990.1.
    UniGeneiMm.4128.

    Genome annotation databases

    EnsembliENSMUST00000002677; ENSMUSP00000002677; ENSMUSG00000002602.
    GeneIDi26362.
    KEGGimmu:26362.
    UCSCiuc009ftx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63535 mRNA. Translation: CAA45097.1 .
    X59560 Genomic DNA. Translation: CAA42158.1 .
    AK155567 mRNA. Translation: BAE33327.1 .
    CH466593 Genomic DNA. Translation: EDL24236.1 .
    BC046618 mRNA. Translation: AAH46618.1 .
    BC050914 mRNA. Translation: AAH50914.1 .
    CCDSi CCDS20996.1.
    PIRi S23065.
    S23251.
    RefSeqi NP_033491.2. NM_009465.4.
    XP_006540052.1. XM_006539989.1.
    XP_006540053.1. XM_006539990.1.
    UniGenei Mm.4128.

    3D structure databases

    ProteinModelPortali Q00993.
    SMRi Q00993. Positions 29-417, 485-836.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204922. 1 interaction.
    IntActi Q00993. 2 interactions.
    STRINGi 10090.ENSMUSP00000002677.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q00993.

    Proteomic databases

    PaxDbi Q00993.
    PRIDEi Q00993.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002677 ; ENSMUSP00000002677 ; ENSMUSG00000002602 .
    GeneIDi 26362.
    KEGGi mmu:26362.
    UCSCi uc009ftx.2. mouse.

    Organism-specific databases

    CTDi 558.
    MGIi MGI:1347244. Axl.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108377.
    HOGENOMi HOG000231685.
    HOVERGENi HBG006346.
    InParanoidi Q80YQ3.
    KOi K05115.
    OMAi QVQGEPP.
    OrthoDBi EOG77DJ5C.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    ChiTaRSi AXL. mouse.
    NextBioi 304223.
    PMAP-CutDB Q80YQ3.
    PROi Q00993.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00993.
    Bgeei Q00993.
    CleanExi MM_AXL.
    Genevestigatori Q00993.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00041. fn3. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00060. FN3. 2 hits.
    SM00409. IG. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The murine ufo receptor: molecular cloning, chromosomal localization and in situ expression analysis."
      Faust M., Ebensperger C., Schulz A.S., Schleithoff L., Hameister H., Bartram C.R., Janssen J.W.G.
      Oncogene 7:1287-1293(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
      Tissue: Heart.
    2. "A putative receptor tyrosine kinase with unique structural topology."
      Rescigno J., Mansukhani A., Basilico C.
      Oncogene 6:1909-1913(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Dendritic cell.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Eye.
    6. "The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases."
      Stitt T.N., Conn G., Gore M., Lai C., Bruno J., Radziejewski C., Mattsson K., Fisher J., Gies D.R., Jones P.F., Masiakowski P., Ryan T.E., Tobkes N.J., Chen D.H., DiStefano P.S., Long G.L., Basilico C., Goldfarb M.P.
      , Lemke G., Glass D.J., Yancopoulos G.D.
      Cell 80:661-670(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIGAND GAS6.
    7. "TAM receptors are pleiotropic inhibitors of the innate immune response."
      Rothlin C.V., Ghosh S., Zuniga E.I., Oldstone M.B., Lemke G.
      Cell 131:1124-1136(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.
    8. "Sertoli cell-initiated testicular innate immune response through toll-like receptor-3 activation is negatively regulated by Tyro3, Axl, and mer receptors."
      Sun B., Qi N., Shang T., Wu H., Deng T., Han D.
      Endocrinology 151:2886-2897(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.

    Entry informationi

    Entry nameiUFO_MOUSE
    AccessioniPrimary (citable) accession number: Q00993
    Secondary accession number(s): Q80YQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3