HTK7_HYDVU
ID HTK7_HYDVU Reviewed; 1477 AA.
AC Q25197;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative insulin-like peptide receptor;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=HTK7;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Steele R.E., Mai N.H., Lieu P., Shenk M.A.;
RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This receptor probably binds an insulin related protein and
CC has a tyrosine-protein kinase activity. {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in dividing epithelial cells.
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; M64612; AAA68205.1; -; mRNA.
DR PIR; T18534; T18534.
DR RefSeq; NP_001296700.1; NM_001309771.1.
DR AlphaFoldDB; Q25197; -.
DR SMR; Q25197; -.
DR PRIDE; Q25197; -.
DR GeneID; 100214733; -.
DR KEGG; hmg:100214733; -.
DR OrthoDB; 223327at2759; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0046777; P:protein autophosphorylation; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.20.20; -; 2.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000620; Insulin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50853; FN3; 3.
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 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Kinase; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1477
FT /note="Putative insulin-like peptide receptor"
FT /id="PRO_0000016714"
FT TOPO_DOM 25..980
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 652..750
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 780..869
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 880..971
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1044..1315
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1350..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1050..1058
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1077
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1201
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
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 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1477 AA; 168278 MW; 74ACDBA7C6DE1D41 CRC64;
MMRNVQSFYF LFLLIVLNFH VVLSAVCIGQ RATTTIWLNQ NGDCQDVGFC QYLQNCTCWH
GNLVVKSTKY YDEENFKPYF PKLREITGYL LISLCTLKFF HLFPGLTVIR GGDLILNYAL
VIYYNEIKEV YFPSLTAILN GGVHIGRNHR LCYVNTIRWK SIIKDIHQTG QYGIYLESNK
LNCDLGCLKG HCHPAPGHDG DPKAQYCWGP GPKKQQNKAQ CQRFCNTQCG PEGCLDGSDH
ICCHHECLGG CSAINSTNTC HACRKYRIKS TGQCVSKCPR KQYLVDKFLC QESCPYWSIN
STEYHHYLWQ GECVTKCPVN YISNNQTKKC EKCKSGMKCN TVCKYQDVMA DGTLYNGALI
RVPSDISKKG LVGCSVFEGS LTFQLQEGTG KAEDSLNELK SLKVLKGHLK IQKSSLKSLN
FLSSLEVIET PQNALLHNKY VMAVYENSQL SELWPGNESI IVSDGGIFFQ YNPRLCPLHI
RNLQDRIHYK NGSKVTGEVS LQNNGHKVLC DTQMLVMHVE EFIPPDLNME TDMTAIECNS
FKCVKVTWNF TMTSAYNNIL FYAIYFKELQ SNQEAVVQLD NECQNNDDWN VITVDIPKIE
SLEQSLFLQS KIISKLTPYT RYAFYIKEIV SKGEERSSHI HYINISQDLP SEPLGVEASF
LSENKILLKW RAPSKPNGII TAFKIYYNKP DYSFWEEQKV LDWCSRDASR DKNAKDVAGY
PVNKENYNQY CNISCVCDEE KENSKAIKAD REAHNFNVEF QTELMRVLFT KNKFSYRNKN
KSPPKIDFSK NISLILSNKI LTSTSTTVTQ AKIEIIEEPK VTVNGNIFSY VISGLDYFED
YELKVCGCTV VGCRRPSSTI NLDCGIVQAR TGVNLTADNL DSKMVRVQVQ LDSYNISWIA
PHKPNAVILK YEISIRYALD KDALVICRPG YLPTYIIRKS RFGNYVAKIR AISPAGNGSW
TEEIHFKVAE LSVTKNNNQL IIGIISAVSA VIVALLVFIL LYMFLHRKLE KDVQGVLYAS
VNPEYMNSKE VYIPDEWELN REKIELIREL GQGSFGMVFE GIAHGIGDHA ELRVAVKTTN
ENASIHDRIQ ILQEASIMKA FNCNHVVKLI GVVSQGQPTF VVMELMGRGD LKSYLKERRP
DDGGIPLMRQ EIYQMVAEIA DGMAYLAARK FVHCDLAARN CMVASDFTVK IGDFGMARDI
YERNYYRKDG KSLLPIRWMA PESLKDGIFS TASDVWSFGV VLWEICTLAS QPYQGKTNEQ
VLNFVLSNGH LDYPEGCDYQ LREFMSLCWH RDPKMRPSFL EIVHVLENEV DDDFVMVSFY
HEMKRKALED IYMKSESYIK SDAYTMSDGY TKGDGNMQNM LSRSQNRKSA IEKSKERLSI
SSLDSGTYVE KYDANDTPEE IPKKKKRPRS KRNSAVDSNA CETKPMLRVE SLYDNHDAFS
ENMQYGDTPV GKSDLMHPET NRELRLSEIF YGKPIPV
