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Database: UniProt
Entry: A0A2K6FHB7_PROCO
LinkDB: A0A2K6FHB7_PROCO
Original site: A0A2K6FHB7_PROCO 
ID   A0A2K6FHB7_PROCO        Unreviewed;      2630 AA.
AC   A0A2K6FHB7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   Name=ROS1 {ECO:0000313|Ensembl:ENSPCOP00000013373.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000013373.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000013373.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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         ECO:0000256|RuleBase:RU000312};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   STRING; 379532.ENSPCOP00000013373; -.
DR   Ensembl; ENSPCOT00000023976.1; ENSPCOP00000013373.1; ENSPCOG00000018293.1.
DR   GeneTree; ENSGT00940000160831; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0010966; P:regulation of phosphate transport; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 6.
DR   CDD; cd05044; PTKc_c-ros; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF527; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF63825; YWTD domain; 2.
DR   PROSITE; PS50853; FN3; 7.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..2630
FT                   /note="Tyrosine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014401927"
FT   TRANSMEM        2144..2165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..187
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          188..276
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          881..991
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1229..1324
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1325..1432
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1839..1937
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1940..2033
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2227..2501
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          2568..2589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2630 AA;  294768 MW;  ABB094EE79200F26 CRC64;
     MKNIYWLNLK LVNFATLGCL WISLGQCTVL NNCLKSCVTN LGRQLDTGTP YNLSEPCIQG
     CHFWNSVHQE NCALKCVMAD GKWKEELKNA DVPTAPFASS IGSHSVTLRW KSANISGVKY
     IVQWKYAQLL GSWTYTETVS KPSYMAEPLH PFTTYVFRVV WIFTAQLQLY SPPSPSYRTH
     PYGVPETAPF IRNIESSSPD TVEVSWAPPQ FPGGPILGYN LRLISKNQKL DSGTQRTSFQ
     FYSTLPNTTY RFSVAAVNEV GEGPEAESSI TTPSPAVQEE EQWLFLSRKT SLRKRSLQHL
     VDEAHCLQSD AVHHNVTGQC IREMIPWCEK KDPEFPEEXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXTPP SLIAPQKIVV DSYNGYVFYL LRDGIYRADL PVPSGREAQA MRIVESCTLK
     DFAVKPQSKR IIYFNDTAQV FMSTFLDGSA SHLVLPHVPF ANVKSFTCEN NDFLVTDGKA
     VFQQDALSFN EFIVGCDLSH IEEFGFGNLV IFGLSTQLHP LPGCPQELSV LFGSHQALVQ
     WKPPALAIGA SECAIPRVVT GPSAWQNWTY EVKVSTQDLP EISHVFSNIS GTTLNVPELQ
     SATKYKVSVR ASSPKGPGPW SEPSVGTTLV PATEPPFIMA VKEDGLWSKP LNSFGPGEFL
     SSDIGNVSDM DWYNNSLYYS DMKGDIYVWL LNGTDISENY HIPNIAGAGA LAFEWLGHFL
     YWAGKTYVIQ RQSVLTGHTD IVTHVKLLVN DMVVDSVGGY LYWTTLYSVE STRLNGESFL
     ILQAQPCSVG DTIITEFAAW STSEISQNAL MYYSGRLFWI NGFRIITTQE IGQRTSVSVL
     EAAKFNQFTI IQTSLKPLPG NFSFTPKVIP DSVQVSSFRI EGNASSFQVL WDAPPVVDWG
     AVFYSVEFSA HSKFLASEQQ PLPVFTVEGL EPYALFNLSV TPYTYWGKGP KTSLSLRAPE
     TVPSAPENPR IFALPSGKYH KKNEVVVEFR WDKPKHENGV LTRFEIFYQI SNQSDTNKTF
     EDWIAVNVTP SVMSFQLEGM SPRCLVAFQV RVFTSKGPGP FSDIVKSTIS EINPFPYLIT
     LLGNKIVFLD MDQNQVVWTF SGEREISAVG YTADDEMGYY AEGNSLFLLD VHNRSSSELL
     RDALAFDITV ITIDWISRHL YFALKESQNG MQIFDVDLEH KVKYPRELKI CNRNSTIISF
     SVYPLLSRLY WTEVSDLGYQ MSYYSIINHT LHRILQPTAT NHQNGRSQCS CNVTEFELSG
     AMTIDTSDLE KPLIYFAKAQ EIWAMDLEGC QCWRVIMVPA VLAGKTLVSL TVDGEFIYWI
     ITAKASTQIY QAKKRNGAIL SQVKTLRSKH ILAYSSFMQP FPDKAFLSLA SDIEEPTILN
     ATNISLTIKL PLAKTNLTGY GITSPTPTYL VYYTEVNEKR NSSDLKYRML EFQDSIALIE
     DLQPFSTYMI QIAVKNYYSD PLEHFPLGKE IWGKTKSGVP EAVWLINTTV RSDTSLIISW
     RESHKPNGPK ESVRYQLAIL HLALIPETPL RQSEFPNERL TLLVTRLSGG NLYVLKVLAC
     HSEEMWCAES HPVTVETFDT PEKPYTLVPE NTSLQLHWKA PSNVNLIRFW FELQKWKYSE
     FYHTEASCSQ GPAYVCNITD LQPYTSYSVR VVVVYVTGEN STSLPESFKT QAGVPTKPGI
     PKLLEGSKNS IQWEKAEDSG NRLMYYILEI RYVTSNDSQD LNLRWKMTFN GSCSSICTWK
     SKNLKGIFQF RVVAANNLGF GEYSGISENI ILVGDGFGIP ETSFIFTIIV GIFLIVTIPL
     TFVWHRRLKN QKPPKEGPAV LVNEDKEMAE LQGLAAGVGL ANACYAIHTL PTQEEIENLP
     AFPREKLTLR LLLGSGAFGE VYEGTAVDIL GVGSGELKVA VKTLKKGSTD QEKIEFLKEA
     HLMSKFNHPN ILKQLGVCLL NEPQYIILEL MEGGDLLTYL RKARMTTFHG PLLTLVDLVD
     LCVDISKGCV YLEQMHFIHR DLAARNCLVS VKDYTSPSRI VKIGDFGLAR DIYKNDYYRK
     RGEGLLPVRW MAPESLMDGI FTTQSDVWSF GILIWEILTL GHQPYPAHSN LDVLNYVQTG
     GRLEPPRNCP DDLWNLMIHC WAQEPDQRPT FHRIQDQLQL FRNFSLNSVS QCRDEANTSG
     VINEGFEGEG GNMICVNSSD VMSIALMETK NQEGLNYMVL ATECSQGEKN SEGLPGSQES
     ESCGLRKEEK EPHADKDFCQ EKQVAYCPPG KPEGLNYACL AHSGCGDGSD
//
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