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Growth arrest-specific protein 6 (GAS-6) (AXL receptor tyrosine kinase ligand)

 GAS6_HUMAN              Reviewed;         721 AA.
Q14393; B3KRQ7; B3KVL4; E9PBL7; Q6IMN1; Q7Z7N3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
22-NOV-2017, entry version 181.
RecName: Full=Growth arrest-specific protein 6;
Short=GAS-6;
AltName: Full=AXL receptor tyrosine kinase ligand;
Flags: Precursor;
Name=GAS6; Synonyms=AXLLG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=8336730; DOI=10.1128/MCB.13.8.4976;
Manfioletti G., Brancolini C., Avanzi G., Schneider C.;
"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.";
Mol. Cell. Biol. 13:4976-4985(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15108283; DOI=10.1002/humu.20025;
Munoz X., Sumoy L., Ramirez-Lorca R., Villar J., de Frutos P.G.,
Sala N.;
"Human vitamin K-dependent GAS6: gene structure, allelic variation,
and association with stroke.";
Hum. Mutat. 23:506-512(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Kidney, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-41; TYR-231;
MET-390; ARG-543; LEU-623; LYS-655 AND GLN-659.
SeattleSNPs variation discovery resource;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal lung, and Fetal spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
Maree A.O., Hillmann A., McRedmond J.P., Fitzgerald D.J.;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[8]
RECEPTOR INTERACTION.
PubMed=7854420; DOI=10.1038/373623a0;
Varnum B.C., Young C., Elliott G., Garcia A., Bartley T.D.,
Fridell Y.W., Hunt R.W., Trail G., Clogston C., Toso R.J.,
Yanagihara D., Bennett L., Silber M., Merewether L.A., Tseng A.,
Escobar E., Liu E.T., Yamane H.K.;
"Axl receptor tyrosine kinase stimulated by the vitamin K-dependent
protein encoded by growth-arrest-specific gene 6.";
Nature 373:623-626(1995).
[9]
RECEPTOR INTERACTION.
PubMed=7867073; DOI=10.1016/0092-8674(95)90520-0;
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.;
"The anticoagulation factor protein S and its relative, Gas6, are
ligands for the Tyro 3/Axl family of receptor tyrosine kinases.";
Cell 80:661-670(1995).
[10]
ALTERNATIVE SPLICING (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9326368; DOI=10.1016/S0014-5793(97)01094-6;
Marcandalli P., Gostissa M., Varnum B., Goruppi S., Schneider C.;
"Identification and tissue expression of a splice variant for the
growth arrest-specific gene gas6.";
FEBS Lett. 415:56-58(1997).
[11]
RECEPTOR INTERACTION.
PubMed=8939948; DOI=10.1074/jbc.271.47.30022;
Nagata K., Ohashi K., Nakano T., Arita H., Zong C., Hanafusa H.,
Mizuno K.;
"Identification of the product of growth arrest-specific gene 6 as a
common ligand for Axl, Sky, and Mer receptor tyrosine kinases.";
J. Biol. Chem. 271:30022-30027(1996).
[12]
RECEPTOR INTERACTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC
PROCESSING.
PubMed=9326369; DOI=10.1016/S0014-5793(97)01093-4;
Goruppi S., Yamane H., Marcandalli P., Garcia A., Clogston C.,
Gostissa M., Varnum B., Schneider C.;
"The product of a gas6 splice variant allows the release of the domain
responsible for Axl tyrosine kinase receptor activation.";
FEBS Lett. 415:59-63(1997).
[13]
FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
PubMed=12364394; DOI=10.1161/01.RES.0000036753.50601.E9;
D'Arcangelo D., Gaetano C., Capogrossi M.C.;
"Acidification prevents endothelial cell apoptosis by Axl
activation.";
Circ. Res. 91:E4-12(2002).
[14]
FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
PubMed=18840707; DOI=10.1182/blood-2008-05-157073;
Park I.K., Giovenzana C., Hughes T.L., Yu J., Trotta R.,
Caligiuri M.A.;
"The Axl/Gas6 pathway is required for optimal cytokine signaling
during human natural killer cell development.";
Blood 113:2470-2477(2009).
[15]
FUNCTION (MICROBIAL INFECTION).
PubMed=21501828; DOI=10.1016/j.chom.2011.03.012;
Morizono K., Xie Y., Olafsen T., Lee B., Dasgupta A., Wu A.M.,
Chen I.S.;
"The soluble serum protein Gas6 bridges virion envelope
phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate
viral entry.";
Cell Host Microbe 9:286-298(2011).
[16]
FUNCTION (MICROBIAL INFECTION).
PubMed=23084921; DOI=10.1016/j.chom.2012.08.009;
Meertens L., Carnec X., Lecoin M.P., Ramdasi R., Guivel-Benhassine F.,
Lew E., Lemke G., Schwartz O., Amara A.;
"The TIM and TAM families of phosphatidylserine receptors mediate
dengue virus entry.";
Cell Host Microbe 12:544-557(2012).
[17]
FUNCTION (MICROBIAL INFECTION).
PubMed=17005688; DOI=10.1128/JVI.01157-06;
Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K.,
Irimura T., Jones S., Feldmann H., Kawaoka Y.;
"Tyro3 family-mediated cell entry of Ebola and Marburg viruses.";
J. Virol. 80:10109-10116(2006).
[18]
PHOSPHORYLATION AT SER-71.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 261-721 (ISOFORM 2),
MUTAGENESIS OF PHE-530; LEU-663 AND TYR-703, AND INTERACTION WITH AXL.
PubMed=8621659; DOI=10.1074/jbc.271.16.9785;
Mark M.R., Chen J., Hammonds R.G., Sadick M., Godowski P.J.;
"Characterization of Gas6, a member of the superfamily of G domain-
containing proteins, as a ligand for Rse and Axl.";
J. Biol. Chem. 271:9785-9789(1996).
[20]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 322-721 IN COMPLEX WITH AXL,
SUBUNIT, GLYCOSYLATION AT ASN-463, AND MUTAGENESIS OF ARG-353 AND
LYS-355.
PubMed=16362042; DOI=10.1038/sj.emboj.7600912;
Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Goehring W.,
Ullrich A., Timpl R., Hohenester E.;
"Structural basis for Gas6-Axl signalling.";
EMBO J. 25:80-87(2006).
-!- 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. {ECO:0000269|PubMed:12364394,
ECO:0000269|PubMed:18840707}.
-!- FUNCTION: (Microbial infection) Can bridges virus envelope
phosphatidylserine to the TAM receptor tyrosine kinase Axl to
mediate viral entry by apoptotic mimicry (PubMed:21501828). Plays
a role in Dengue cell entry by apoptotic mimicry
(PubMed:23084921). Plays a role in Vaccinia virus cell entry by
apoptotic mimicry (PubMed:21501828). Plays a role in ebolavirus
and marburgvirus cell entry by apoptotic mimicry
(PubMed:17005688). {ECO:0000269|PubMed:17005688,
ECO:0000269|PubMed:21501828, ECO:0000269|PubMed:23084921}.
-!- SUBUNIT: Heterodimer and heterotetramer with AXL.
{ECO:0000269|PubMed:16362042}.
-!- INTERACTION:
P30530:AXL; NbExp=8; IntAct=EBI-2802811, EBI-2850927;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9326369}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=gas6SV;
IsoId=Q14393-1; Sequence=Displayed;
Name=2;
IsoId=Q14393-2; Sequence=VSP_010494;
Name=3;
IsoId=Q14393-3; Sequence=VSP_010492, VSP_010493, VSP_010494;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q14393-4; Sequence=VSP_043832, VSP_010494;
Name=5;
IsoId=Q14393-5; Sequence=VSP_045685;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Plasma. Isoform 1 and isoform 2 are widely
expressed. Isoform 1 is the predominant form in spleen.
{ECO:0000269|PubMed:8336730, ECO:0000269|PubMed:9326368}.
-!- PTM: Isoform 1 is proteolytically processed after secretion to
yield a N-terminal 36 kDa protein and a C-terminal 50 kDa protein
including the laminin G-like domains which activates AXL.
{ECO:0000269|PubMed:9326369}.
-!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
dependent carboxylation. These residues are essential for the
binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/gas6/";
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EMBL; L13720; AAA58494.1; -; mRNA.
EMBL; AY256843; AAO84057.1; -; Genomic_DNA.
EMBL; AY256830; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256831; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256832; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256833; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256834; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256835; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256836; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256837; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256838; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256839; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256840; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256841; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AY256842; AAO84057.1; JOINED; Genomic_DNA.
EMBL; AK092028; BAG52469.1; -; mRNA.
EMBL; AK122969; BAG53826.1; -; mRNA.
EMBL; AK126533; BAC86580.1; -; mRNA.
EMBL; AK290803; BAF83492.1; -; mRNA.
EMBL; EF631974; ABR09277.1; -; Genomic_DNA.
EMBL; BX072579; CAH71174.1; -; Genomic_DNA.
EMBL; BC038984; AAH38984.1; -; mRNA.
EMBL; AY170372; AAO41859.1; -; Genomic_DNA.
EMBL; BK001240; DAA01155.1; -; Genomic_DNA.
CCDS; CCDS45072.1; -. [Q14393-2]
PIR; B48089; B48089.
RefSeq; NP_000811.1; NM_000820.3. [Q14393-2]
UniGene; Hs.646346; -.
PDB; 1H30; X-ray; 2.20 A; A=261-721.
PDB; 2C5D; X-ray; 3.30 A; A/B=261-721.
PDB; 4RA0; X-ray; 3.07 A; A/B=322-721.
PDB; 5VXZ; X-ray; 2.30 A; A/B=324-718.
PDBsum; 1H30; -.
PDBsum; 2C5D; -.
PDBsum; 4RA0; -.
PDBsum; 5VXZ; -.
ProteinModelPortal; Q14393; -.
SMR; Q14393; -.
BioGrid; 108891; 32.
IntAct; Q14393; 13.
MINT; MINT-2735698; -.
iPTMnet; Q14393; -.
PhosphoSitePlus; Q14393; -.
BioMuta; GAS6; -.
DMDM; 48427995; -.
EPD; Q14393; -.
MaxQB; Q14393; -.
PeptideAtlas; Q14393; -.
PRIDE; Q14393; -.
Ensembl; ENST00000327773; ENSP00000331831; ENSG00000183087. [Q14393-2]
GeneID; 2621; -.
KEGG; hsa:2621; -.
UCSC; uc001vud.4; human. [Q14393-1]
CTD; 2621; -.
DisGeNET; 2621; -.
EuPathDB; HostDB:ENSG00000183087.14; -.
GeneCards; GAS6; -.
HGNC; HGNC:4168; GAS6.
HPA; HPA008275; -.
HPA; HPA056080; -.
MIM; 600441; gene.
neXtProt; NX_Q14393; -.
OpenTargets; ENSG00000183087; -.
PharmGKB; PA28582; -.
GeneTree; ENSGT00530000063339; -.
HOGENOM; HOG000065758; -.
HOVERGEN; HBG051702; -.
InParanoid; Q14393; -.
KO; K05464; -.
OMA; VIRLRFK; -.
OrthoDB; EOG091G034Z; -.
PhylomeDB; Q14393; -.
TreeFam; TF352157; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SignaLink; Q14393; -.
SIGNOR; Q14393; -.
ChiTaRS; GAS6; human.
EvolutionaryTrace; Q14393; -.
GeneWiki; GAS6; -.
GenomeRNAi; 2621; -.
PRO; PR:Q14393; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000183087; -.
CleanEx; HS_GAS6; -.
Genevisible; Q14393; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0043277; P:apoptotic cell clearance; IDA:UniProtKB.
GO; GO:0035754; P:B cell chemotaxis; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:UniProtKB.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0071307; P:cellular response to vitamin K; IDA:UniProtKB.
GO; GO:0097028; P:dendritic cell differentiation; IEP:UniProtKB.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; IEA:Ensembl.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:UniProtKB.
GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0010934; P:macrophage cytokine production; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:UniProtKB.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0050711; P:negative regulation of interleukin-1 secretion; IDA:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; IDA:UniProtKB.
GO; GO:1900142; P:negative regulation of oligodendrocyte apoptotic process; IDA:UniProtKB.
GO; GO:0033159; P:negative regulation of protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:2000533; P:negative regulation of renal albumin absorption; ISS:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; TAS:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043491; P:protein kinase B signaling; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006465; P:signal peptide processing; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB.
GO; GO:0019079; P:viral genome replication; IDA:UniProtKB.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR026823; cEGF.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
Pfam; PF12662; cEGF; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF12661; hEGF; 2.
Pfam; PF00054; Laminin_G_1; 1.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 4.
SMART; SM00179; EGF_CA; 4.
SMART; SM00069; GLA; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49899; SSF49899; 3.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
Glycoprotein; Growth regulation; Host-virus interaction;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 721 Growth arrest-specific protein 6.
/FTId=PRO_0000007589.
DOMAIN 53 94 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 116 154 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 156 196 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 197 237 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 238 278 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 341 513 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 520 713 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
METAL 372 372 Calcium.
METAL 374 374 Calcium; via carbonyl oxygen.
METAL 483 483 Calcium; via carbonyl oxygen.
METAL 699 699 Calcium.
MOD_RES 71 71 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 664 664 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63772}.
MOD_RES 680 680 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63772}.
MOD_RES 683 683 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q63772}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16362042}.
DISULFID 65 70 {ECO:0000250}.
DISULFID 120 133 {ECO:0000250}.
DISULFID 125 142 {ECO:0000250}.
DISULFID 144 153 {ECO:0000250}.
DISULFID 160 171 {ECO:0000250}.
DISULFID 167 180 {ECO:0000250}.
DISULFID 182 195 {ECO:0000250}.
DISULFID 201 212 {ECO:0000250}.
DISULFID 207 221 {ECO:0000250}.
DISULFID 223 236 {ECO:0000250}.
DISULFID 242 251 {ECO:0000250}.
DISULFID 247 260 {ECO:0000250}.
DISULFID 262 277
DISULFID 326 613
DISULFID 487 513
DISULFID 686 713
VAR_SEQ 1 342 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045685.
VAR_SEQ 1 273 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043832.
VAR_SEQ 1 54 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010492.
VAR_SEQ 55 94 EAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLD
-> MCMCQASPPPAALAGCLLSSCVQPAREHGGAFSKAEWL
SN (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010493.
VAR_SEQ 279 321 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8336730}.
/FTId=VSP_010494.
VARIANT 41 41 F -> L. {ECO:0000269|Ref.4}.
/FTId=VAR_038823.
VARIANT 231 231 S -> Y (in dbSNP:rs146159446).
{ECO:0000269|Ref.4}.
/FTId=VAR_038824.
VARIANT 390 390 V -> M. {ECO:0000269|Ref.4}.
/FTId=VAR_038825.
VARIANT 543 543 G -> R. {ECO:0000269|Ref.4}.
/FTId=VAR_038826.
VARIANT 623 623 S -> L. {ECO:0000269|Ref.4}.
/FTId=VAR_038827.
VARIANT 655 655 E -> K. {ECO:0000269|Ref.4}.
/FTId=VAR_038828.
VARIANT 659 659 R -> Q. {ECO:0000269|Ref.4}.
/FTId=VAR_038829.
MUTAGEN 353 353 R->E: Strongly reduced affinity for AXL.
Abolishes phosphorylation of AXL.
{ECO:0000269|PubMed:16362042}.
MUTAGEN 355 355 K->E: Strongly reduced affinity for AXL.
Abolishes phosphorylation of AXL.
{ECO:0000269|PubMed:16362042}.
MUTAGEN 530 530 F->A: Decreases activation of AXL.
{ECO:0000269|PubMed:8621659}.
MUTAGEN 663 663 L->A: Reduces affinity for AXL 15-fold
and decreases activation of AXL.
{ECO:0000269|PubMed:8621659}.
MUTAGEN 703 703 Y->A: Reduces affinity for AXL 3-fold.
{ECO:0000269|PubMed:8621659}.
CONFLICT 399 399 E -> K (in Ref. 3; BAG52469).
{ECO:0000305}.
HELIX 264 266 {ECO:0000244|PDB:1H30}.
STRAND 268 271 {ECO:0000244|PDB:1H30}.
TURN 272 275 {ECO:0000244|PDB:1H30}.
STRAND 276 278 {ECO:0000244|PDB:1H30}.
STRAND 337 339 {ECO:0000244|PDB:1H30}.
STRAND 350 353 {ECO:0000244|PDB:1H30}.
STRAND 356 358 {ECO:0000244|PDB:1H30}.
STRAND 363 370 {ECO:0000244|PDB:1H30}.
STRAND 373 382 {ECO:0000244|PDB:1H30}.
STRAND 386 394 {ECO:0000244|PDB:1H30}.
STRAND 397 404 {ECO:0000244|PDB:1H30}.
STRAND 407 416 {ECO:0000244|PDB:1H30}.
STRAND 419 421 {ECO:0000244|PDB:5VXZ}.
STRAND 423 429 {ECO:0000244|PDB:1H30}.
STRAND 431 438 {ECO:0000244|PDB:1H30}.
STRAND 441 447 {ECO:0000244|PDB:1H30}.
STRAND 452 456 {ECO:0000244|PDB:1H30}.
STRAND 459 461 {ECO:0000244|PDB:1H30}.
STRAND 463 468 {ECO:0000244|PDB:1H30}.
HELIX 473 475 {ECO:0000244|PDB:1H30}.
STRAND 476 478 {ECO:0000244|PDB:1H30}.
STRAND 486 493 {ECO:0000244|PDB:1H30}.
HELIX 500 506 {ECO:0000244|PDB:5VXZ}.
HELIX 509 511 {ECO:0000244|PDB:1H30}.
STRAND 512 516 {ECO:0000244|PDB:1H30}.
STRAND 518 523 {ECO:0000244|PDB:1H30}.
STRAND 529 531 {ECO:0000244|PDB:1H30}.
STRAND 550 561 {ECO:0000244|PDB:1H30}.
STRAND 563 570 {ECO:0000244|PDB:1H30}.
HELIX 571 573 {ECO:0000244|PDB:1H30}.
STRAND 575 584 {ECO:0000244|PDB:1H30}.
STRAND 588 590 {ECO:0000244|PDB:4RA0}.
STRAND 595 600 {ECO:0000244|PDB:1H30}.
STRAND 603 609 {ECO:0000244|PDB:1H30}.
HELIX 612 614 {ECO:0000244|PDB:5VXZ}.
STRAND 618 625 {ECO:0000244|PDB:1H30}.
STRAND 628 633 {ECO:0000244|PDB:1H30}.
STRAND 639 642 {ECO:0000244|PDB:1H30}.
HELIX 644 658 {ECO:0000244|PDB:1H30}.
STRAND 663 667 {ECO:0000244|PDB:1H30}.
STRAND 676 678 {ECO:0000244|PDB:1H30}.
STRAND 685 691 {ECO:0000244|PDB:1H30}.
HELIX 698 700 {ECO:0000244|PDB:1H30}.
STRAND 701 704 {ECO:0000244|PDB:1H30}.
STRAND 708 711 {ECO:0000244|PDB:5VXZ}.
SEQUENCE 721 AA; 79677 MW; E7B22B0E010930F9 CRC64;
MAPSLSPGPA ALRRAPQLLL LLLAAECALA ALLPAREATQ FLRPRQRRAF QVFEEAKQGH
LERECVEELC SREEAREVFE NDPETDYFYP RYLDCINKYG SPYTKNSGFA TCVQNLPDQC
TPNPCDRKGT QACQDLMGNF FCLCKAGWGG RLCDKDVNEC SQENGGCLQI CHNKPGSFHC
SCHSGFELSS DGRTCQDIDE CADSEACGEA RCKNLPGSYS CLCDEGFAYS SQEKACRDVD
ECLQGRCEQV CVNSPGSYTC HCDGRGGLKL SQDMDTCELE AGWPCPRHRR DGSPAARPGR
GAQGSRSEGH IPDRRGPRPW QDILPCVPFS VAKSVKSLYL GRMFSGTPVI RLRFKRLQPT
RLVAEFDFRT FDPEGILLFA GGHQDSTWIV LALRAGRLEL QLRYNGVGRV TSSGPVINHG
MWQTISVEEL ARNLVIKVNR DAVMKIAVAG DLFQPERGLY HLNLTVGGIP FHEKDLVQPI
NPRLDGCMRS WNWLNGEDTT IQETVKVNTR MQCFSVTERG SFYPGSGFAF YSLDYMRTPL
DVGTESTWEV EVVAHIRPAA DTGVLFALWA PDLRAVPLSV ALVDYHSTKK LKKQLVVLAV
EHTALALMEI KVCDGQEHVV TVSLRDGEAT LEVDGTRGQS EVSAAQLQER LAVLERHLRS
PVLTFAGGLP DVPVTSAPVT AFYRGCMTLE VNRRLLDLDE AAYKHSDITA HSCPPVEPAA
A


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