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Q61592 (GAS6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth arrest-specific protein 6

Short name=GAS-6
Alternative name(s):
AXL receptor tyrosine kinase ligand
Gene names
Name:Gas6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. 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. Ref.3

Subunit structure

Heterodimer and heterotetramer with AXL.

Subcellular location

Secreted By similarity.

Post-translational modification

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium By similarity.

Miscellaneous

GAS6 deficient mice show protection against thrombosis, but no spontaneous bleeding.

Sequence similarities

Contains 4 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 2 laminin G-like domains.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

activation of protein kinase B activity

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic cell clearance

Inferred from direct assay PubMed 18159085. Source: MGI

blood coagulation

Inferred from mutant phenotype PubMed 15184064. Source: MGI

cell-substrate adhesion

Inferred from mutant phenotype PubMed 18188450. Source: MGI

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from direct assay Ref.1. Source: MGI

cellular response to interferon-alpha

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to starvation

Inferred from direct assay Ref.1. Source: MGI

cellular response to vitamin K

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

enzyme linked receptor protein signaling pathway

Inferred from genetic interaction PubMed 9395235. Source: MGI

extracellular matrix assembly

Inferred from sequence or structural similarity. Source: UniProtKB

fusion of virus membrane with host plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic stem cell migration to bone marrow

Inferred from sequence or structural similarity. Source: UniProtKB

macrophage cytokine production

Inferred from mutant phenotype PubMed 18188450. Source: MGI

negative regulation of apoptotic process

Inferred from direct assay PubMed 16723520. Source: UniProtKB

negative regulation of biomineral tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of dendritic cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-1 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of oligodendrocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of renal albumin absorption

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neuron migration

Inferred from genetic interaction PubMed 18787040. Source: MGI

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of TOR signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dendritic cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of natural killer cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from mutant phenotype PubMed 18188450. Source: MGI

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

receptor-mediated virion attachment to host cell

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from sequence or structural similarity. Source: UniProtKB

viral genome replication

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 18188450. Source: MGI

   Molecular_functionbinding, bridging

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylserine binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor agonist activity

Inferred from direct assay PubMed 9395235. Source: MGI

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 674647Growth arrest-specific protein 6
PRO_0000007590

Regions

Domain50 – 9142Gla
Domain113 – 15139EGF-like 1; calcium-binding Potential
Domain153 – 19341EGF-like 2; calcium-binding Potential
Domain194 – 23441EGF-like 3; calcium-binding Potential
Domain235 – 27541EGF-like 4; calcium-binding Potential
Domain295 – 467173Laminin G-like 1
Domain474 – 666193Laminin G-like 2

Sites

Metal binding3261Calcium By similarity
Metal binding3281Calcium; via carbonyl oxygen By similarity
Metal binding4371Calcium; via carbonyl oxygen By similarity
Metal binding6521Calcium By similarity

Amino acid modifications

Modified residue6091Phosphothreonine By similarity
Modified residue6141Phosphoserine By similarity
Modified residue6171Phosphothreonine By similarity
Modified residue6331Phosphothreonine By similarity
Modified residue6361Phosphotyrosine By similarity
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 67 By similarity
Disulfide bond117 ↔ 130 By similarity
Disulfide bond122 ↔ 139 By similarity
Disulfide bond141 ↔ 150 By similarity
Disulfide bond157 ↔ 168 By similarity
Disulfide bond164 ↔ 177 By similarity
Disulfide bond179 ↔ 192 By similarity
Disulfide bond198 ↔ 209 By similarity
Disulfide bond204 ↔ 218 By similarity
Disulfide bond220 ↔ 233 By similarity
Disulfide bond239 ↔ 248 By similarity
Disulfide bond244 ↔ 257 By similarity
Disulfide bond259 ↔ 274 By similarity
Disulfide bond280 ↔ 566 By similarity
Disulfide bond441 ↔ 467 By similarity
Disulfide bond639 ↔ 666 By similarity

Experimental info

Sequence conflict5301Missing in CAA42507. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61592 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 7C41F7693903F401

FASTA67474,610
        10         20         30         40         50         60 
MPPPPGPAAA LGTALLLLLL ASESSHTVLL RAREAAQFLR PRQRRAYQVF EEAKQGHLER 

        70         80         90        100        110        120 
ECVEEVCSKE EAREVFENDP ETEYFYPRYQ ECMRKYGRPE EKNPDFAKCV QNLPDQCTPN 

       130        140        150        160        170        180 
PCDKKGTHIC QDLMGNFFCV CTDGWGGRLC DKDVNECVQK NGGCSQVCHN KPGSFQCACH 

       190        200        210        220        230        240 
SGFSLASDGQ TCQDIDECTD SDTCGDARCK NLPGSYSCLC DEGYTYSSKE KTCQDVDECQ 

       250        260        270        280        290        300 
QDRCEQTCVN SPGSYTCHCD GRGGLKLSPD MDTCEDILPC VPFSMAKSVK SLYLGRMFSG 

       310        320        330        340        350        360 
TPVIRLRFKR LQPTRLLAEF DFRTFDPEGV LFFAGGRSDS TWIVLGLRAG RLELQLRYNG 

       370        380        390        400        410        420 
VGRITSSGPT INHGMWQTIS VEELERNLVI KVNKDAVMKI AVAGELFQLE RGLYHLNLTV 

       430        440        450        460        470        480 
GGIPFKESEL VQPINPRLDG CMRSWNWLNG EDSAIQETVK ANTKMQCFSV TERGSFFPGN 

       490        500        510        520        530        540 
GFATYRLNYT RTSLDVGTET TWEVKVVARI RPATDTGVLL ALVGDDDVVP ISVALVDYHS 

       550        560        570        580        590        600 
TKKLKKQLVV LAVEDVALAL MEIKVCDSQE HTVTVSLREG EATLEVDGTK GQSEVSTAQL 

       610        620        630        640        650        660 
QERLDTLKTH LQGSVHTYVG GLPEVSVISA PVTAFYRGCM TLEVNGKILD LDTASYKHSD 

       670 
ITSHSCPPVE HATP 

« Hide

References

« Hide 'large scale' references
[1]"The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade."
Manfioletti G., Brancolini C., Avanzi G., Schneider C.
Mol. Cell. Biol. 13:4976-4985(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
[3]"Deficiency or inhibition of Gas6 causes platelet dysfunction and protects mice against thrombosis."
Angelillo-Scherrer A., de Frutos P., Aparicio C., Melis E., Savi P., Lupu F., Arnout J., Dewerchin M., Hoylaerts M., Herbert J., Collen D., Dahlback B., Carmeliet P.
Nat. Med. 7:215-221(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59846 mRNA. Translation: CAA42507.1.
BC005444 mRNA. Translation: AAH05444.1.
PIRA48089.
RefSeqNP_062394.2. NM_019521.2.
UniGeneMm.3982.

3D structure databases

ProteinModelPortalQ61592.
SMRQ61592. Positions 46-672.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033828.

Proteomic databases

PaxDbQ61592.
PRIDEQ61592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033828; ENSMUSP00000033828; ENSMUSG00000031451.
GeneID14456.
KEGGmmu:14456.
UCSCuc009kya.1. mouse.

Organism-specific databases

CTD2621.
MGIMGI:95660. Gas6.

Phylogenomic databases

eggNOGNOG149502.
GeneTreeENSGT00530000063339.
HOGENOMHOG000065758.
HOVERGENHBG051702.
InParanoidQ61592.
KOK05464.
OMAVDYHSTK.
OrthoDBEOG7F5119.
PhylomeDBQ61592.
TreeFamTF352157.

Gene expression databases

BgeeQ61592.
CleanExMM_GAS6.
GenevestigatorQ61592.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamPF07645. EGF_CA. 1 hit.
PF00594. Gla. 1 hit.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSPR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 3 hits.
SM00069. GLA. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 3 hits.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGAS6. mouse.
NextBio286080.
PROQ61592.
SOURCESearch...

Entry information

Entry nameGAS6_MOUSE
AccessionPrimary (citable) accession number: Q61592
Secondary accession number(s): Q99K57
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot