PTK7_CHICK
ID PTK7_CHICK Reviewed; 1051 AA.
AC Q91048;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Inactive tyrosine-protein kinase 7;
DE AltName: Full=Kinase-like protein;
DE AltName: Full=Protein-tyrosine kinase 7;
DE AltName: Full=Pseudo tyrosine kinase receptor 7;
DE AltName: Full=Tyrosine-protein kinase-like 7;
DE Flags: Precursor;
GN Name=PTK7; Synonyms=KLG;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=1711213; DOI=10.1073/pnas.88.11.4897;
RA Chou Y.-H., Hayman M.J.;
RT "Characterization of a member of the immunoglobulin gene superfamily that
RT possibly represents an additional class of growth factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4897-4901(1991).
CC -!- FUNCTION: Inactive tyrosine kinase involved in Wnt signaling. pathway
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, spleen, bursa, thymus and
CC brain. Weakly expressed in fibroblasts. Also expressed in embryonic
CC liver. {ECO:0000269|PubMed:1711213}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; M63437; AAA48933.1; -; mRNA.
DR PIR; A39712; A39712.
DR RefSeq; NP_001026206.1; NM_001031035.1.
DR AlphaFoldDB; Q91048; -.
DR SMR; Q91048; -.
DR STRING; 9031.ENSGALP00000014004; -.
DR PaxDb; Q91048; -.
DR GeneID; 421257; -.
DR KEGG; gga:421257; -.
DR CTD; 5754; -.
DR VEuPathDB; HostDB:geneid_421257; -.
DR eggNOG; KOG1026; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; Q91048; -.
DR OrthoDB; 530072at2759; -.
DR PhylomeDB; Q91048; -.
DR PRO; PR:Q91048; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 7.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1051
FT /note="Inactive tyrosine-protein kinase 7"
FT /id="PRO_0000016749"
FT TOPO_DOM 23..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..1051
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 115..204
FT /note="Ig-like C2-type 2"
FT DOMAIN 213..298
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..388
FT /note="Ig-like C2-type 4"
FT DOMAIN 393..472
FT /note="Ig-like C2-type 5"
FT DOMAIN 487..566
FT /note="Ig-like C2-type 6"
FT DOMAIN 573..661
FT /note="Ig-like C2-type 7"
FT DOMAIN 777..1048
FT /note="Protein kinase; inactive"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 326..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 414..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 505..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 594..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1051 AA; 116366 MW; 1752442AEA4CB702 CRC64;
MAALRALLLL LAVGAQAAIR FAKEPYSQDA LHGRSAILRC EVEEPAHVEF EWLQNGLPIQ
DTEQRFKEGS NLQFAAVDRH RDAGSFQCVA RNVQTGEEAR TANASFNIKW METGSVVLKQ
PASAAEIQPS STVVLRCHID GHPRPTWQWF RDGAPLPDGR GTYSVSSKER TLTLRGAGPD
DNGLYYCSAR PRAVGSVCSQ DNFTLNIIDE SFPQAVVVPE DLIVTKNEEA MFDCQFAAVP
PPTQEWLFED SPITNRSKTT VFANGSLLIT QVKARSTGVY KCIGHGQKGK ALVLKATLRL
AEIEEMAPFS PKVLTANQGH RVSCACPRGV PTPQVWWERN QERVPTAGRV YQEAEQLVFT
SITEADAGIY TCHAANKAGE KKQELSITVA TVPKWVEMPK DSQLEESKPG YLHCLSKASL
KPTVTWYRNG VSISEDSRFE ISENGTLRIN NVEVYDGTMY KCVSSTPAGS IEGYARVHVL
EKLKFTPPPQ PLQCMEFNKE VTVSCSATGR EKPTIQWTKT DGSSLPSHVS HRAGILSFHK
VSRSDSGNYT CIASNSPQGE IRATVQLVVA VYVTFKLEPE PTTVYQGHTA MFQCQAEGDP
VPHIQWKGKD KILDPSKLLP RIQIMPNGSL VIYDVTTEDS GKYTCIAGNS CNIKHREAFL
YVVDKPAAEE DEGPSSHTPY KMIQTIGLSV GAAVAYIIIV LGLMFYCKKR RKAKRLKKHP
EGEEPEMECL NGGTLLQNGQ TTAEIQEEVA LTNLGSSSGA SKRHSARDKM HFPRSNLQTI
TTLGRGEFGE VFLAKAKGAE DAEGEALVLV KSLQTRDEQL QLDFRREAEM FGKLNHVNVV
RLLGLCREAE PHYMVLEYVD LGDLKQFLRI SKSKDESLKP QPLSTKHKVS LCTQVALGME
HLSNGRFVHR DLAARNCLVS AQRQVKVSAL SLSKDVYNSE YYHFRQAWIP LRWMPPEAVL
EDEFSTKSDV WSFGVLMWEV FTQGEMPYAP LADDEVLAGL KSGKTKLPQP EGCPSRLTKL
MQRCWAPSPK DRPSFSELAA ALGDSPADSK A
