RPK1_IPONI
ID RPK1_IPONI Reviewed; 1109 AA.
AC P93194; Q9AVV0; Q9AVV1; Q9AVV2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Receptor-like protein kinase;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=INRPK1;
OS Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=35883 {ECO:0000312|EMBL:AAB36558.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS INRPK1; INRPK1A; INRPK1B AND
RP INRPK1C), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Violet {ECO:0000312|EMBL:AAB36558.2};
RC TISSUE=Leaf {ECO:0000312|EMBL:AAB36558.2};
RX PubMed=10949373; DOI=10.1023/a:1006408011873;
RA Bassett C.L., Nickerson M.L., Cohen R.A., Rajeevan M.S.;
RT "Alternative transcript initiation and novel post-transcriptional
RT processing of a leucine-rich repeat receptor-like protein kinase gene that
RT responds to short-day photoperiodic floral induction in morning glory
RT (Ipomoea nil).";
RL Plant Mol. Biol. 43:43-58(2000).
CC -!- FUNCTION: Possible role in short-day photoperiod floral induction.
CC {ECO:0000303|PubMed:10949373}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: [Isoform INRPK1]: Cell membrane; Single-pass type
CC I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform INRPK1b]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform INRPK1c]: Cell membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=INRPK1 {ECO:0000269|PubMed:10949373};
CC IsoId=P93194-1; Sequence=Displayed;
CC Name=INRPK1a {ECO:0000269|PubMed:10949373};
CC IsoId=P93194-2; Sequence=VSP_050676;
CC Name=INRPK1b {ECO:0000269|PubMed:10949373};
CC IsoId=P93194-3; Sequence=VSP_050677, VSP_050678;
CC Name=INRPK1c;
CC IsoId=P93194-4; Sequence=VSP_018857;
CC -!- TISSUE SPECIFICITY: INRPK1 and INRPK1b are expressed in leaves,
CC cotyledons, shoot tips and roots from induced and vegetative plants.
CC The highest concentrations of INRPK1 are found in vegetative roots, and
CC the lowest concentrations in vegetative cotyledons. INRPK1b is more
CC abundant in roots than other tissues. INRPK1a is expressed in
CC vegetative roots. INRPK1c is expressed in cotyledons.
CC {ECO:0000269|PubMed:10949373}.
CC -!- MISCELLANEOUS: [Isoform INRPK1c]: Produced by alternative initiation at
CC Met-667 of isoform INRPK1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U77888; AAB36558.2; -; Genomic_DNA.
DR EMBL; U77888; AAG52992.2; -; Genomic_DNA.
DR EMBL; U77888; AAG52993.2; -; Genomic_DNA.
DR EMBL; U77888; AAG52994.1; -; Genomic_DNA.
DR PIR; T18536; T18536.
DR RefSeq; XP_019193281.1; XM_019337736.1. [P93194-1]
DR AlphaFoldDB; P93194; -.
DR SMR; P93194; -.
DR GeneID; 109187519; -.
DR KEGG; ini:109187519; -.
DR OrthoDB; 826997at2759; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; NAS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Alternative splicing; ATP-binding; Cell membrane;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Repeat; Secreted; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1109
FT /note="Receptor-like protein kinase"
FT /id="PRO_0000024382"
FT TOPO_DOM 21..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..1109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 69..92
FT /note="LRR 1"
FT REPEAT 93..115
FT /note="LRR 2"
FT REPEAT 117..140
FT /note="LRR 3"
FT REPEAT 141..162
FT /note="LRR 4"
FT /evidence="ECO:0000305"
FT REPEAT 165..187
FT /note="LRR 5"
FT REPEAT 189..209
FT /note="LRR 6"
FT REPEAT 213..236
FT /note="LRR 7"
FT REPEAT 237..258
FT /note="LRR 8"
FT REPEAT 261..284
FT /note="LRR 9"
FT REPEAT 309..331
FT /note="LRR 10"
FT REPEAT 333..355
FT /note="LRR 11"
FT REPEAT 357..378
FT /note="LRR 12"
FT REPEAT 381..404
FT /note="LRR 13"
FT REPEAT 405..427
FT /note="LRR 14"
FT REPEAT 429..451
FT /note="LRR 15"
FT REPEAT 453..476
FT /note="LRR 16"
FT REPEAT 477..499
FT /note="LRR 17"
FT REPEAT 500..523
FT /note="LRR 18"
FT REPEAT 524..546
FT /note="LRR 19"
FT REPEAT 548..569
FT /note="LRR 20"
FT REPEAT 572..595
FT /note="LRR 21"
FT REPEAT 596..618
FT /note="LRR 22"
FT REPEAT 620..642
FT /note="LRR 23"
FT REPEAT 643..666
FT /note="LRR 24"
FT REPEAT 667..689
FT /note="LRR 25"
FT REPEAT 690..710
FT /note="LRR 26"
FT DOMAIN 816..1096
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REPEAT 827..850
FT /note="LRR 27"
FT /evidence="ECO:0000305"
FT REPEAT 958..981
FT /note="LRR 28"
FT /evidence="ECO:0000305"
FT ACT_SITE 942
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 822..830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 845
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..666
FT /note="Missing (in isoform INRPK1c)"
FT /evidence="ECO:0000305"
FT /id="VSP_018857"
FT VAR_SEQ 130..591
FT /note="Missing (in isoform INRPK1a)"
FT /evidence="ECO:0000303|PubMed:10949373"
FT /id="VSP_050676"
FT VAR_SEQ 130..155
FT /note="GNIPDTLGALQNLRNLSLFFNSLIGP -> ARWKFTSWRYSTSGSFAGTEVI
FT KFEQ (in isoform INRPK1b)"
FT /evidence="ECO:0000303|PubMed:10949373"
FT /id="VSP_050677"
FT VAR_SEQ 156..1109
FT /note="Missing (in isoform INRPK1b)"
FT /evidence="ECO:0000303|PubMed:10949373"
FT /id="VSP_050678"
SQ SEQUENCE 1109 AA; 120765 MW; B7B7C50A4A0FAF29 CRC64;
MKVAVNTFLL FLCSTSSIYA AFALNSDGAA LLSLTRHWTS IPSDITQSWN ASDSTPCSWL
GVECDRRQFV DTLNLSSYGI SGEFGPEISH LKHLKKVVLS GNGFFGSIPS QLGNCSLLEH
IDLSSNSFTG NIPDTLGALQ NLRNLSLFFN SLIGPFPESL LSIPHLETVY FTGNGLNGSI
PSNIGNMSEL TTLWLDDNQF SGPVPSSLGN ITTLQELYLN DNNLVGTLPV TLNNLENLVY
LDVRNNSLVG AIPLDFVSCK QIDTISLSNN QFTGGLPPGL GNCTSLREFG AFSCALSGPI
PSCFGQLTKL DTLYLAGNHF SGRIPPELGK CKSMIDLQLQ QNQLEGEIPG ELGMLSQLQY
LHLYTNNLSG EVPLSIWKIQ SLQSLQLYQN NLSGELPVDM TELKQLVSLA LYENHFTGVI
PQDLGANSSL EVLDLTRNMF TGHIPPNLCS QKKLKRLLLG YNYLEGSVPS DLGGCSTLER
LILEENNLRG GLPDFVEKQN LLFFDLSGNN FTGPIPPSLG NLKNVTAIYL SSNQLSGSIP
PELGSLVKLE HLNLSHNILK GILPSELSNC HKLSELDASH NLLNGSIPST LGSLTELTKL
SLGENSFSGG IPTSLFQSNK LLNLQLGGNL LAGDIPPVGA LQALRSLNLS SNKLNGQLPI
DLGKLKMLEE LDVSHNNLSG TLRVLSTIQS LTFINISHNL FSGPVPPSLT KFLNSSPTSF
SGNSDLCINC PADGLACPES SILRPCNMQS NTGKGGLSTL GIAMIVLGAL LFIICLFLFS
AFLFLHCKKS VQEIAISAQE GDGSLLNKVL EATENLNDKY VIGKGAHGTI YKATLSPDKV
YAVKKLVFTG IKNGSVSMVR EIETIGKVRH RNLIKLEEFW LRKEYGLILY TYMENGSLHD
ILHETNPPKP LDWSTRHNIA VGTAHGLAYL HFDCDPAIVH RDIKPMNILL DSDLEPHISD
FGIAKLLDQS ATSIPSNTVQ GTIGYMAPEN AFTTVKSRES DVYSYGVVLL ELITRKKALD
PSFNGETDIV GWVRSVWTQT GEIQKIVDPS LLDELIDSSV MEQVTEALSL ALRCAEKEVD
KRPTMRDVVK QLTRWSIRSY SSSVRNKSK
