AXL
entrez
558
canonical
uniprot
P30530
canonical
ensembl
ENSG00000167601
resolver
ensp
ENSP00000301178
resolver
ensp
ENSP00000351995
resolver
ensp
ENSP00000471497
resolver
enst
ENST00000593513
resolver
genesymbol
AXL
resolver
genesymbol_syn
UFO
resolver
hgnc
HGNC:905
resolver
uniprot
M0R0W6
resolver
uniprot
Q8N5L2
resolver
uniprot
Q9UD27
resolver
uniprot_entry
M0R0W6_HUMAN
resolver
uniprot_entry
UFO_HUMAN
resolver
uniprot_sec
Q8N5L2
resolver
uniprot_sec
Q9UD27
resolver
activity_regulation
ACTIVITY REGULATION: Activated by GAS6-binding and subsequent autophosphorylation. {ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:8621659}.
uniprot
proteins
amino_acid_sequence
MAWRCPRMGRVPLAWCLALCGWACMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSDDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWWYVLLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQPDPKDSCSCLTAAEVHPAGRYVLCPSTTPSPAQPADRGSPAAPGQEDGA
uniprot
proteins
disease_involvement
DISEASE: Note=AXL and its ligand GAS6 are highly expressed in thyroid carcinoma tissues, and might thus be involved in thyroid tumorigenesis. Overexpression of AXL and its ligand was also detected in many other cancers such as myeloproliferative disorders, prostatic carcinoma cells, or breast cancer.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: 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, AXL 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 TNS2. 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. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. {ECO:0000269|PubMed:10403904, ECO:0000269|PubMed:11484958, ECO:0000269|PubMed:12364394, ECO:0000269|PubMed:12490074, ECO:0000269|PubMed:15507525, ECO:0000269|PubMed:15733062, ECO:0000269|PubMed:1656220, ECO:0000269|PubMed:18840707}.; FUNCTION: (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. {ECO:0000269|PubMed:17005688, ECO:0000269|PubMed:21501828, ECO:0000269|PubMed:22156524, ECO:0000269|PubMed:25277499}.; FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope. {ECO:0000269|PubMed:22673088}.; FUNCTION: (Microbial infection) Promotes Zika virus entry in glial cells, Sertoli cells and astrocytes (PubMed:28076778, PubMed:29379210, PubMed:31311882). Additionally, Zika virus potentiates AXL kinase activity to antagonize type I interferon signaling and thereby promotes infection (PubMed:28076778). Interferon signaling inhibition occurs via an SOCS1-dependent mechanism (PubMed:29379210). {ECO:0000269|PubMed:28076778, ECO:0000269|PubMed:29379210, ECO:0000269|PubMed:31311882}.
uniprot
proteins
mass_dalton
98337
uniprot
proteins
mutagenesis
MUTAGEN 63; /note="E->R: Slightly reduced affinity for GAS6."; /evidence="ECO:0000269|PubMed:16362042"; MUTAGEN 66; /note="E->R: Reduced affinity for GAS6."; /evidence="ECO:0000269|PubMed:16362042"; MUTAGEN 84; /note="T->R: Reduced affinity for GAS6."; /evidence="ECO:0000269|PubMed:16362042"; MUTAGEN 567; /note="K->M: Catalytically inactive mutant."; /evidence="ECO:0000269|PubMed:28076778
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion. {ECO:0000269|PubMed:15958209}.; PTM: Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. {ECO:0000269|PubMed:18346204, ECO:0000269|PubMed:9178760}.
uniprot
proteins
protein_family
AXL/UFO subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10403904
uniprot
proteins
pubmed
11484958
uniprot
proteins
pubmed
12364394
uniprot
proteins
pubmed
12470648
uniprot
proteins
pubmed
12490074
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507525
uniprot
proteins
pubmed
15733062
uniprot
proteins
pubmed
15958209
uniprot
proteins
pubmed
16362042
uniprot
proteins
pubmed
1656220
uniprot
proteins
pubmed
17005688
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18346204
uniprot
proteins
pubmed
1834974
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18840707
uniprot
proteins
pubmed
19815557
uniprot
proteins
pubmed
21501828
uniprot
proteins
pubmed
22156524
uniprot
proteins
pubmed
2247464
uniprot
proteins
pubmed
22673088
uniprot
proteins
pubmed
25277499
uniprot
proteins
pubmed
28076778
uniprot
proteins
pubmed
29379210
uniprot
proteins
pubmed
29507355
uniprot
proteins
pubmed
31311882
uniprot
proteins
pubmed
7854420
uniprot
proteins
pubmed
7896447
uniprot
proteins
pubmed
8247543
uniprot
proteins
pubmed
8621659
uniprot
proteins
pubmed
9178760
uniprot
proteins
sequence_length
894
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28076778, ECO:0000269|PubMed:29379210, ECO:0000269|PubMed:7896447}; Single-pass type I membrane protein {ECO:0000269|PubMed:7896447}.
uniprot
proteins
transmembrane_region
TRANSMEM 452..472; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins