P55144 (TYRO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase receptor TYRO3
EC=2.7.10.1

Alternative name(s):
Etk2/tyro3
TK19-2
Tyrosine-protein kinase DTK
Tyrosine-protein kinase RSE
Tyrosine-protein kinase TIF

Gene names

Name:	Tyro3
Synonyms:	Dtk, Rse, Tif

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. Ref.14 Ref.18 Ref.19 Ref.20
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6. Interacts with PIK3R1; this interaction increases PI3-kinase activity By similarity. Ref.13 Ref.17
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Abundant in the brain and lower levels in other tissues.
Post-translational modification	Autophosphorylated By similarity.
Disruption phenotype	knockout mice are fertile, but male animals that lack all three receptors TYRO3, AXL and MERTK produce no mature sperm. Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily. Contains 2 fibronectin type-III domains. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.
Sequence caution	The sequence AAB26942.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA54995.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic cell clearance Inferred from genetic interaction PubMed 18159085. Source: UniProtKB forebrain cell migration Inferred from genetic interaction PubMed 18787040. Source: MGI natural killer cell differentiation Inferred from genetic interaction PubMed 16751775. Source: MGI negative regulation of inflammatory response Inferred from genetic interaction PubMed 18083102. Source: UniProtKB negative regulation of innate immune response Inferred from genetic interaction PubMed 18083102. Source: UniProtKB negative regulation of lymphocyte activation Inferred from genetic interaction PubMed 11452127. Source: MGI negative regulation of neuron apoptotic process Inferred from genetic interaction PubMed 18787040. Source: MGI negative regulation of toll-like receptor signaling pathway Inferred from genetic interaction PubMed 18083102. Source: UniProtKB neuron homeostasis Inferred from mutant phenotype Ref.18. Source: UniProtKB ovulation cycle Inferred from genetic interaction PubMed 18787040. Source: MGI platelet aggregation Inferred from mutant phenotype PubMed 20546121. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein kinase B signaling cascade Inferred from mutant phenotype Ref.18. Source: UniProtKB secretion by cell Inferred from mutant phenotype Ref.14. Source: MGI spermatogenesis Inferred from genetic interaction Ref.12. Source: UniProtKB substrate adhesion-dependent cell spreading Inferred from mutant phenotype Ref.14. Source: MGI vagina development Inferred from genetic interaction PubMed 18393392. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol 3-kinase binding Inferred from sequence or structural similarity. Source: UniProtKB protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: P55144-1)

Also known as: III;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P55144-2)

Also known as: II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MALRRSMGWPGLRPLLLAGLASLLLPGSAAA → MGCPAGDWKV...QGAGPAAPSG

Isoform 1 (identifier: P55144-3)

Also known as: I; B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MALRRSMGWPGLRPLLLAGLASLLLPGSAAA → MDDKLENTLGRWAGENGLSIGEYLAIK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 880

850

Tyrosine-protein kinase receptor TYRO3

PRO_0000024479

Regions

Topological domain

31 – 419

389

Extracellular Potential

Transmembrane

420 – 440

21

Helical; Potential

Topological domain

441 – 880

440

Cytoplasmic Potential

Domain

31 – 118

88

Ig-like C2-type 1

Domain

129 – 209

81

Ig-like C2-type 2

Domain

214 – 307

94

Fibronectin type-III 1

Domain

312 – 403

92

Fibronectin type-III 2

Domain

508 – 785

278

Protein kinase

Nucleotide binding

514 – 522

9

ATP By similarity

Sites

Active site

645

1

Proton acceptor By similarity

Binding site

540

1

ATP By similarity

Amino acid modifications

Modified residue

671

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

675

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

676

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

794

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

53

1

N-linked (GlcNAc...) Potential

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

181

1

N-linked (GlcNAc...) Ref.16

Glycosylation

220

1

N-linked (GlcNAc...) Potential

Glycosylation

230

1

N-linked (GlcNAc...) Potential

Glycosylation

283

1

N-linked (GlcNAc...) Potential

Glycosylation

356

1

N-linked (GlcNAc...) Potential

Glycosylation

370

1

N-linked (GlcNAc...) Potential

Disulfide bond

54 ↔ 107

By similarity

Disulfide bond

150 ↔ 193

By similarity

Natural variations

Alternative sequence

1 – 31

31

MALRR…GSAAA → MDDKLENTLGRWAGENGLSI GEYLAIK in isoform 1.

VSP_012548

Alternative sequence

1 – 31

31

MALRR…GSAAA → MGCPAGDWKVFGEGGAWPGA CPGSEAGPPQRQRSGQGAGP AAPSG in isoform 2.

VSP_012549

Experimental info

Sequence conflict

630

1

A → R in CAA54995. Ref.3

Sequence conflict

637 – 639

3

SSR → AIK in BAA19191. Ref.5

Sequence conflict

637 – 639

3

SSR → AIK in BAA19192. Ref.5

Sequence conflict

811

1

V → L in AAA19237. Ref.1

Sequence conflict

811

1

V → L in AAC52148. Ref.2

Sequence conflict

811

1

V → L in BAA19193. Ref.5

Sequence conflict

811

1

V → L in AAB26942. Ref.6

Sequence conflict

811

1

V → L in AAB26943. Ref.6

Secondary structure

1

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880

Helix Strand Turn

Details...

Beta strand

509 – 517

9

Beta strand

520 – 526

7

Beta strand

536 – 541

6

Helix

550 – 562

13

Beta strand

575 – 578

4

Beta strand

589 – 594

6

Helix

601 – 609

9

Helix

619 – 638

20

Helix

648 – 650

3

Beta strand

651 – 653

3

Beta strand

659 – 661

3

Helix

686 – 688

3

Helix

691 – 696

6

Helix

701 – 716

16

Turn

722 – 725

4

Helix

728 – 730

3

Helix

731 – 736

6

Helix

749 – 757

9

Helix

763 – 765

3

Helix

769 – 781

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (III) [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 2794316CB0034617	FASTA	880	96,208
	10 20 30 40 50 60 MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV KLNCSVEGME 70 80 90 100 110 120 DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS 130 140 150 160 170 180 VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL 190 200 210 220 230 240 NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD 250 260 270 280 290 300 GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG 310 320 330 340 350 360 DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD 370 380 390 400 410 420 ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWV 430 440 450 460 470 480 PVVLGVLTAL ITAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER 490 500 510 520 530 540 IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK 550 560 570 580 590 600 MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD 610 620 630 640 650 660 LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN CMLAEDMTVC 670 680 690 700 710 720 VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VHSDVWAFGV TMWEIMTRGQ 730 740 750 760 770 780 TPYAGIENAE IYNYLIGGNR LKQPPECMEE VYDLMYQCWS ADPKQRPSFT CLRMELENIL 790 800 810 820 830 840 GHLSVLSTSQ DPLYINIERA EQPTESGSPE VHCGERSSSE AGDGSGVGAV GGIPSDSRYI 850 860 870 880 FSPGGLSESP GQLEQQPESP LNENQRLLLL QQGLLPHSSC
	Isoform 2 (II) [UniParc]. Checksum: 4F45E58F5B466FEA	FASTA	894	97,343
	10 20 30 40 50 60 MGCPAGDWKV FGEGGAWPGA CPGSEAGPPQ RQRSGQGAGP AAPSGGLKLM GAPVKMTVSQ 70 80 90 100 110 120 GQPVKLNCSV EGMEDPDIHW MKDGTVVQNA SQVSISISEH SWIGLLSLKS VERSDAGLYW 130 140 150 160 170 180 CQVKDGEETK ISQSVWLTVE GVPFFTVEPK DLAVPPNAPF QLSCEAVGPP EPVTIYWWRG 190 200 210 220 230 240 LTKVGGPAPS PSVLNVTGVT QRTEFSCEAR NIKGLATSRP AIVRLQAPPA APFNTTVTTI 250 260 270 280 290 300 SSYNASVAWV PGADGLALLH SCTVQVAHAP GEWEALAVVV PVPPFTCLLR NLAPATNYSL 310 320 330 340 350 360 RVRCANALGP SPYGDWVPFQ TKGLAPARAP QNFHAIRTDS GLILEWEEVI PEDPGEGPLG 370 380 390 400 410 420 PYKLSWVQEN GTQDELMVEG TRANLTDWDP QKDLILRVCA SNAIGDGPWS QPLVVSSHDH 430 440 450 460 470 480 AGRQGPPHSR TSWVPVVLGV LTALITAAAL ALILLRKRRK ETRFGQAFDS VMARGEPAVH 490 500 510 520 530 540 FRAARSFNRE RPERIEATLD SLGISDELKE KLEDVLIPEQ QFTLGRMLGK GEFGSVREAQ 550 560 570 580 590 600 LKQEDGSFVK VAVKMLKADI IASSDIEEFL REAACMKEFD HPHVAKLVGV SLRSRAKGRL 610 620 630 640 650 660 PIPMVILPFM KHGDLHAFLL ASRIGENPFN LPLQTLVRFM VDIACGMEYL SSRNFIHRDL 670 680 690 700 710 720 AARNCMLAED MTVCVADFGL SRKIYSGDYY RQGCASKLPV KWLALESLAD NLYTVHSDVW 730 740 750 760 770 780 AFGVTMWEIM TRGQTPYAGI ENAEIYNYLI GGNRLKQPPE CMEEVYDLMY QCWSADPKQR 790 800 810 820 830 840 PSFTCLRMEL ENILGHLSVL STSQDPLYIN IERAEQPTES GSPEVHCGER SSSEAGDGSG 850 860 870 880 890 VGAVGGIPSD SRYIFSPGGL SESPGQLEQQ PESPLNENQR LLLLQQGLLP HSSC
	Isoform 1 (I) (B) [UniParc]. Checksum: 5C7813084CC59D56	FASTA	876	96,042
	10 20 30 40 50 60 MDDKLENTLG RWAGENGLSI GEYLAIKGLK LMGAPVKMTV SQGQPVKLNC SVEGMEDPDI 70 80 90 100 110 120 HWMKDGTVVQ NASQVSISIS EHSWIGLLSL KSVERSDAGL YWCQVKDGEE TKISQSVWLT 130 140 150 160 170 180 VEGVPFFTVE PKDLAVPPNA PFQLSCEAVG PPEPVTIYWW RGLTKVGGPA PSPSVLNVTG 190 200 210 220 230 240 VTQRTEFSCE ARNIKGLATS RPAIVRLQAP PAAPFNTTVT TISSYNASVA WVPGADGLAL 250 260 270 280 290 300 LHSCTVQVAH APGEWEALAV VVPVPPFTCL LRNLAPATNY SLRVRCANAL GPSPYGDWVP 310 320 330 340 350 360 FQTKGLAPAR APQNFHAIRT DSGLILEWEE VIPEDPGEGP LGPYKLSWVQ ENGTQDELMV 370 380 390 400 410 420 EGTRANLTDW DPQKDLILRV CASNAIGDGP WSQPLVVSSH DHAGRQGPPH SRTSWVPVVL 430 440 450 460 470 480 GVLTALITAA ALALILLRKR RKETRFGQAF DSVMARGEPA VHFRAARSFN RERPERIEAT 490 500 510 520 530 540 LDSLGISDEL KEKLEDVLIP EQQFTLGRML GKGEFGSVRE AQLKQEDGSF VKVAVKMLKA 550 560 570 580 590 600 DIIASSDIEE FLREAACMKE FDHPHVAKLV GVSLRSRAKG RLPIPMVILP FMKHGDLHAF 610 620 630 640 650 660 LLASRIGENP FNLPLQTLVR FMVDIACGME YLSSRNFIHR DLAARNCMLA EDMTVCVADF 670 680 690 700 710 720 GLSRKIYSGD YYRQGCASKL PVKWLALESL ADNLYTVHSD VWAFGVTMWE IMTRGQTPYA 730 740 750 760 770 780 GIENAEIYNY LIGGNRLKQP PECMEEVYDL MYQCWSADPK QRPSFTCLRM ELENILGHLS 790 800 810 820 830 840 VLSTSQDPLY INIERAEQPT ESGSPEVHCG ERSSSEAGDG SGVGAVGGIP SDSRYIFSPG 850 860 870 GLSESPGQLE QQPESPLNEN QRLLLLQQGL LPHSSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo, is expressed at high levels in the brain." Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J. J. Biol. Chem. 269:10720-10728(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[2]	"Isolation of a receptor tyrosine kinase (DTK) from embryonic stem cells: structure, genetic mapping and analysis of expression." Crosier P.S., Lewis P.M., Hall L.R., Vitas M.R., Morris C.M., Beier D.R., Wood C.R., Crosier K.E. Growth Factors 11:125-136(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[3]	"Structure, expression, and activity of Tyro 3, a neural adhesion-related receptor tyrosine kinase." Lai C., Gore M., Lemke G. Oncogene 9:2567-2578(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Strain: C57BL/6.
[4]	"brt, a mouse gene encoding a novel receptor-type protein-tyrosine kinase, is preferentially expressed in the brain." Fujimoto J., Yamamoto T. Oncogene 9:693-698(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c. Tissue: Brain and Liver.
[5]	"Cloning of the cDNA for a novel receptor tyrosine kinase, Sky, predominantly expressed in brain." Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T. Oncogene 9:699-705(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1). Strain: BALB/c. Tissue: Brain.
[6]	"Isolation and expression analysis of tyro3, a murine growth factor receptor tyrosine kinase preferentially expressed in adult brain." Schulz N., Paulhiac C., Lee L., Zhou R. Brain Res. Mol. Brain Res. 28:273-280(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). Strain: BALB/c. Tissue: Brain.
[7]	"Structure and expression of a murine homologue of sky receptor tyrosine kinase." Sasaki M., Enami J. J. Biochem. 120:264-270(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3). Strain: BALB/c. Tissue: Brain.
[8]	"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: C57BL/6J. Tissue: Cerebellum.
[9]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[10]	"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.
[11]	"Identification of alternative exons, including a novel exon, in the tyrosine kinase receptor gene Etk2/tyro3 that explain differences in 5' cDNA sequences." Biesecker L.G., Giannola D.M., Emerson S.G. Oncogene 10:2239-2242(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92 (ISOFORMS 1; 2 AND 3). Strain: 129/Sv. Tissue: Liver.
[12]	"Tyro-3 family receptors are essential regulators of mammalian spermatogenesis." Lu Q., Gore M., Zhang Q., Camenisch T., Boast S., Casagranda F., Lai C., Skinner M.K., Klein R., Matsushima G.K., Earp H.S., Goff S.P., Lemke G. Nature 398:723-728(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[13]	"Transforming activity of receptor tyrosine kinase tyro3 is mediated, at least in part, by the PI3 kinase-signaling pathway." Lan Z., Wu H., Li W., Wu S., Lu L., Xu M., Dai W. Blood 95:633-638(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIK3R1.
[14]	"Role of Gas6 receptors in platelet signaling during thrombus stabilization and implications for antithrombotic therapy." Angelillo-Scherrer A., Burnier L., Flores N., Savi P., DeMol M., Schaeffer P., Herbert J.M., Lemke G., Goff S.P., Matsushima G.K., Earp H.S., Vesin C., Hoylaerts M.F., Plaisance S., Collen D., Conway E.M., Wehrle-Haller B., Carmeliet P. J. Clin. Invest. 115:237-246(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PLATELET ACTIVATION.
[15]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-675, MASS SPECTROMETRY. Tissue: Brain.
[16]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181, MASS SPECTROMETRY.
[17]	"Tubby and tubby-like protein 1 are new MerTK ligands for phagocytosis." Caberoy N.B., Zhou Y., Li W. EMBO J. 29:3898-3910(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TULP1.
[18]	"Protein S protects neurons from excitotoxic injury by activating the TAM receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway through its sex hormone-binding globulin-like region." Zhong Z., Wang Y., Guo H., Sagare A., Fernandez J.A., Bell R.D., Barrett T.M., Griffin J.H., Freeman R.S., Zlokovic B.V. J. Neurosci. 30:15521-15534(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NEURON PROTECTION.
[19]	"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 IMMUNE RESPONSE INHIBITION.
[20]	"Protein S blocks the extrinsic apoptotic cascade in tissue plasminogen activator/N-methyl D-aspartate-treated neurons via Tyro3-Akt-FKHRL1 signaling pathway." Guo H., Barrett T.M., Zhong Z., Fernandez J.A., Griffin J.H., Freeman R.S., Zlokovic B.V. Mol. Neurodegener. 6:13-13(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U05683 mRNA. Translation: AAA19237.1.
U18933 mRNA. Translation: AAC52148.1.
X78103 mRNA. Translation: CAA54995.1. Different initiation.
U18342 mRNA. Translation: AAB26942.1. Different initiation.
U18343 mRNA. Translation: AAB26943.1.
AB000826 Genomic DNA. Translation: BAA19191.1.
AB000827 mRNA. Translation: BAA19192.1.
AB000828 mRNA. Translation: BAA19193.1.
AK141198 mRNA. Translation: BAE24581.1.
AL844896 Genomic DNA. Translation: CAM22049.1.
BC066058 mRNA. Translation: AAH66058.1.
BC082325 mRNA. Translation: AAH82325.1.
U23721, U23718 Genomic DNA. Translation: AAC52215.1.
U23721, U23719 Genomic DNA. Translation: AAC52216.1.
U23721, U23720 Genomic DNA. Translation: AAC52217.1.

IPI

IPI00126146.
IPI00136714.
IPI00421186.

PIR

B53743.
I48862.
I49152.

RefSeq

NP_062265.2. NM_019392.2.

UniGene

Mm.2901.
Mm.424496.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QUP	X-ray	1.90	A	485-800	[»]
4FEQ	X-ray	2.20	A	485-800	[»]
4FF8	X-ray	2.40	A	485-800	[»]

ProteinModelPortal

P55144.

SMR

P55144. Positions 37-365, 499-785.

ModBase

Search...

PTM databases

PhosphoSite

P55144.

Proteomic databases

PaxDb

P55144.

PRIDE

P55144.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028763; ENSMUSP00000028763; ENSMUSG00000027298.
ENSMUST00000110783; ENSMUSP00000106410; ENSMUSG00000027298.

GeneID

22174.

KEGG

mmu:22174.

Organism-specific databases

CTD

7301.

MGI

MGI:104294. Tyro3.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00550000074361.

HOVERGEN

HBG006346.

KO

K05116.

OMA

HAGQQGP.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Gene expression databases

ArrayExpress

P55144.

Bgee

P55144.

CleanEx

MM_TYRO3.

Genevestigator

P55144.

GermOnline

ENSMUSG00000027298. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF00041. fn3. 2 hits.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

SMART

SM00060. FN3. 2 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.
SSF56112. Kinase_like. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

TYRO3. mouse.

NextBio

302127.

SOURCE

Search...

Entry information

Entry name

TYRO3_MOUSE

Accession

Primary (citable) accession number: P55144
Secondary accession number(s): O09070 , O09080, P70285, Q60752, Q62482, Q62483, Q62484, Q6NZM6, Q78E85, Q78E87

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program