ID A0A1D2MZH3_ORCCI Unreviewed; 1334 AA.
AC A0A1D2MZH3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Insulin-like peptide receptor {ECO:0000313|EMBL:ODM98443.1};
GN ORFNames=Ocin01_08218 {ECO:0000313|EMBL:ODM98443.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM98443.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM98443.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM98443.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM98443.1}.
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DR EMBL; LJIJ01000353; ODM98443.1; -; Genomic_DNA.
DR STRING; 48709.A0A1D2MZH3; -.
DR OMA; AYKLEMT; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR CDD; cd06366; PBP1_GABAb_receptor; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
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 PANTHER; PTHR24416:SF489; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:ODM98443.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, 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..1334
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008904791"
FT TRANSMEM 895..919
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 960..1233
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1292..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 992
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1334 AA; 151180 MW; 89DF72214A772283 CRC64;
MLFRKHNLTN LIHLITIITG LVGHVTPKKC LEYVKAPRQF LQVEINNEIQ MWNLTLETSQ
ESLGHQLITH TFAIFLQEVL GYDAVQVVSY PIHYNLNSTT DILRRLSGTE LMVENGAVFM
SQLSNNTQKI PETMINVAVW LSPEMELEKW NTPGIFLENC GHLGFVGRFG WFIPKLPITD
KYPTVEYWRT FNINASLTEL FSLDDSDYQN ATTHLAWNPQ TERFYCQEAF CESGMYTPDV
CRNGFSSSGT SKCAMLLASY PESSMFLPEE ISSLGLRVMV IWLGPNLESF VRHLLSKYEQ
PESRTTTNRA VMFFSWDPTR LTSELDLISI SFPTCTGGVH CRYESLRLEK FVSSRLKEGA
KPAYEAAHRL SITYEEYRKM MEVYTNVSNE LQNEIDPDGS LTAMQVWNGG KSTSVVEHAA
CQWMKENKLV WESWEPKGGN GKVPLFIGGI FPITGSYTAR GILVAAQMAT IAVNRNDSVL
KDYDLRMHVY DGQCRADKVM KGFIDFIRLN TFPSMAGILG PACSDTAEPL AGVATHFKTV
VISYSAEGSS FSDRAKYPYF FRTIGENKQY QHVYLDLFRQ LSWTRVASLT EEGQKYAEYV
SSLQDLLQEN HIAFIANRKF PKDRPALNMS QYLQDLKSKK AKIIIGDFYD HAARAVMCEA
YHQKMTAREG FVWFLPVWFL KDWYDTNKHN QDSDENEKIP CNTTEMIQAI NGHLSLQYAY
FAPEDHIMQE SVNVSQWRHR YDQNCQNKNI STSDYAGYAY DAIWTYAYAL DKLLKQNHSH
ITNLHSDKTT NELVRIITET DFHGVSGHIK FVGGPSRIST IHVVQWFNRS TNIVGTWYPK
TSNQIDSSTP GHLALKKELI QWLTPDGSVP NDGSEPPPKC VLETLASALD VSCEVAIVIA
NVIGFGILGF ILVICFLVIK RRYDKKVQMT QDYFKALGID ILSATNVSAL DKWEVPRDRV
VINRKLGEGA FGTVYGGECF FDDRGWVAVA VKTLKVGSSC EQKLDFLGEA EVMKRFEHKN
IVRLLGVCTK NEPIYTIMEF MLYGDLKTYL LARRHLVNEK NCEESDEISS RRLTSMSLDV
ARALSYLAEL KYVHRDVACR NCLVNASRVV KLGDFGMTRP MYENDYYRFN RKGMLPVRWM
APESLALGIF TPMSDVWSFG VLLYEIITFG SFPFQGKSNN EVLDYVKSGN TVSIPSGVKL
QLEQLLKGCW SLDPPKRPAA AVIVEFLANN PRIISPSLDM PLASVQLEGT DQLEIQIPDR
IFNRKTGSTA VRNGGKGIPK VVREPRDMTG NNLSAFGEEN IPLTGQKTYG NRNQTQSSYV
SLHHEPSSVE ADLI
//
