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Database: UniProt
Entry: G3WV44_SARHA
LinkDB: G3WV44_SARHA
Original site: G3WV44_SARHA 
ID   G3WV44_SARHA            Unreviewed;      1272 AA.
AC   G3WV44;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=INSRR {ECO:0000313|Ensembl:ENSSHAP00000019299.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000019299.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000019299.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000019299.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; G3WV44; -.
DR   STRING; 9305.ENSSHAP00000019299; -.
DR   Ensembl; ENSSHAT00000019455.2; ENSSHAP00000019299.2; ENSSHAG00000016391.2.
DR   eggNOG; KOG1095; Eukaryota.
DR   eggNOG; KOG4258; Eukaryota.
DR   GeneTree; ENSGT00940000160437; -.
DR   HOGENOM; CLU_000288_166_0_1; -.
DR   InParanoid; G3WV44; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF351636; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:Ensembl.
DR   GO; GO:0030238; P:male sex determination; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00064; FU; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF338; INSULIN RECEPTOR-RELATED PROTEIN; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 2.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000620-
KW   2}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000620-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1272
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029698547"
FT   TRANSMEM        922..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          485..605
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          609..710
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          820..914
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          987..1226
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          669..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1234..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1264
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         997
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1021
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1068..1074
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1272 AA;  141792 MW;  CDA1D703DD2C5868 CRC64;
     MTAPSSWLWG SCLLMNFLPL GFGLDTPEVC PSLDIRTEVS ELRRLENCTV VEGYLQILLI
     FTATGEDFQG LSFPRLTQVT DYLLLFRVYG LESLRDLFPN LAVIRGTRLF FSYALVIFEM
     PHLRDVGLPG LGAILRGAVR VEKNQELCHL STVDWSLLQP TTDANHIVGN KLGEECADVC
     PGMLGTEEPC IRTTVNGRMD YRCWTSGHCQ RVCPCARGLA CTPRGECCHP ECLGGCSRPS
     DAQACVACRH FHFGGTCHSA CPQGTYQYEA WRCVTAEYCA SLRALPDLPG RGSDFVIHQG
     SCLAQCPPGY THNDSSIFCH KCEGLCPKEC KVGTKTIDSL QAAQELIGCT HLKGSLILNL
     RQGYNLETEL QRSLGLVETI TGFLKIKHSF ALISLGFFRN LKLIRGDFMV DGNYTLYVLD
     NQNLQQLGEW AEAGLSIPVG KIYFAFNPRL CLEHIYQLEE VTGTRGRQNK AEINPRTNGD
     RAACKTRPLR FVSNVTESDR ILLRWERYEP LEARDLLSFI VYYKESPFQN ATEHMGPDAC
     GAPNWNLLDV ELPLSRTQEP GVTLAPLKPW TQYAVFVRAI TLSMAEDSPH QGAQSPIIYL
     RTLPAAPTVP LDVMSTSNSS SHLLVRWKPP TQRNGNLTYY LVLWQRLAED ADLYLNDYCQ
     RGLRLPSSST DARFDQEERE PLAEAEPGCC PCRSPSPEQP QQPALEAHEA SFQKKFENFL
     HNAITLPRSP WKVTSINKNP QRDAGRYRRA AKAPGGGGNG SDFGIQDKVP RERAVLSGLR
     HFTEYRIDIH ACNHAAHTVG CSAATFVFAR TMPHREADSI PGKVAWKPAS KSSVLLHWPE
     PPDPNGLILK YEIKYRRLGE EATVLCVSRL RYAKFGGVHL ALLPPGNYTA RVRATSLAGN
     GSWTDGLPFY IPGPEEEESG GLHVLLTVTP VGLLLLVVLA ALGFFYSRKR NSDGYPNGTL
     YASVNPEYFS TSDMYVPDEW EVPREQISVM RELGQGSFGM VYEGLAQGLE EGEAPTPVAL
     KTVNELASLR ERIEFLKEAS VMKAFKCHHV VRLLGVVSQG QPVLVIMELM TRGDLKSHLR
     SLRPEAENNP GLPRPELGDM IQMADFGMTR DVYETDYYRK GGKGLLPVRW MAPESLKDGI
     FSTHSDVWSF GVVLWEIVTL AEQPYQGLSN EQVLRFVMDN GVLEEPEGCP PQLQELMSRC
     WQQNPRQRPT FLQILDSIKD ELRPSFRLLS FYYSPESRGG RGSLAPPDTD PDPHLSPEAP
     PDYSPPNGSL GH
//
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