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Database: UniProt
Entry: A0A2D0QP17_ICTPU
LinkDB: A0A2D0QP17_ICTPU
Original site: A0A2D0QP17_ICTPU 
ID   A0A2D0QP17_ICTPU        Unreviewed;      1081 AA.
AC   A0A2D0QP17;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Inactive tyrosine-protein kinase 7 {ECO:0000313|RefSeq:XP_017320147.1};
GN   Name=ptk7b {ECO:0000313|RefSeq:XP_017320147.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017320147.1};
RN   [1] {ECO:0000313|RefSeq:XP_017320147.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017320147.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_017320147.1; XM_017464658.3.
DR   AlphaFoldDB; A0A2D0QP17; -.
DR   STRING; 7998.ENSIPUP00000028664; -.
DR   Ensembl; ENSIPUT00000029834; ENSIPUP00000028664; ENSIPUG00000019376.
DR   GeneID; 108263634; -.
DR   KEGG; ipu:108263634; -.
DR   CTD; 100150035; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000221080; Chromosome 3.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05046; PTK_CCK4; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR45080; CONTACTIN 5; 1.
DR   PANTHER; PTHR45080:SF21; INACTIVE TYROSINE-PROTEIN KINASE 7; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 7.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 7.
DR   SUPFAM; SSF48726; Immunoglobulin; 7.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 7.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000615-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000313|RefSeq:XP_017320147.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000615-2};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transferase {ECO:0000313|RefSeq:XP_017320147.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        716..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..147
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          157..236
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          245..331
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          354..420
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          425..511
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          520..601
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          606..681
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          807..1077
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        941
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         814..821
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         887..893
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         945
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         946
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1081 AA;  121062 MW;  53122F9A9E68B81F CRC64;
     MDISDTSDTL ARIATQHRGA SRSSTSFRNR RRWTLFPVRM NSLLAIIIFC TNVLCVQSLS
     LHFSKEPQSQ DALHGRSAML RCEVSEAAGV RYSWLQDGQP VQGSERRFIE DGSLKFTAVD
     RHLDTGNFQC VATSLTSGEV ATSTNASFNI KWLDSGPVTL KEPASVEEID DAEQIVLQCQ
     IDGHPRPNSK WYKDGVLLSV KERSITLRNP VPGDSGTYSC CARNGAGQLC SNSNFTLNII
     DKTIPRVVVA PEDQVVFRNE EAVFHCQFSA KPPPVIEWLH ESEPVINKPR VLVYDNGTLR
     ITQVKPRNTG RYTCVVRYGT DRQLNVEATL HIAEIEDMGG RLFRYFSANN MERISCVPPH
     GHPKPVVWWE KDGARVPTKG RVHQQDMDLI FNPAVVGDSG TYVCMAQNKA GQRRQEVTVT
     VAGPPEWVNR PQDTEMEEGQ PGYLHCRIQA TPPAQVTWYR NMQEISEEKS QYKLFPNGTL
     RINSVEVYDG LVYNCVCKTA SGILNGQAKV YVLEKLKFTP APQSPQCLQL DKEASVQCSA
     TGRETPTIHW TKADGSAIPA HVKQINGTLQ FEKVTRSDAG NFTCVASNRP QGEIRAYVSL
     TVGVYTEFKV EPEYTTVYQG HTATMHCQAT GDPQPYIQWI VKDKTLSVSN TRFQELPNGS
     LIIRDVTTAD TGKYTCIAGN SCGIRHRVAQ LYVVEKPKHD RDSDEGKTPY KMIQTIGLSV
     GAAVAYIIAV LGLMFYCKKR RNAKRLQKGQ DGEEPEMECL NGGAMQHNGQ TTAEIQEEVA
     LTNLETVSTA EKHHSNTDKF HFPRADLQTI TTLGKGEFGE VLLAKARGIE EGEEQTVVLV
     KSLLSRDELS QAEFRRQVDM FSKLNHTNIV RLLGLCKDTE PHYMILEYID LGDLKQFLRI
     SRSKDENLKP QPISTKTKVS ICAQVAAGME HLSNQRFVHK DLATRNCLIS GERHVKISAL
     GLSKDVYNSE YYHYRQNWIP LRWLPAESVF ENDFSTKSDV WAFGVLMWEV FSHGELPYSS
     LSHEDVLEGL QAGTLKLSAP EVCPSKVYKL MSRCWAPSLK ERPSFSELIQ VLGDIPLDSK
     V
//
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