LIPG1_ARATH
ID LIPG1_ARATH Reviewed; 636 AA.
AC Q1PDW3; Q9FFD4;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Receptor-like kinase LIP1 {ECO:0000303|PubMed:23684977};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein LOST IN POLLEN TUBE GUIDANCE 1 {ECO:0000303|PubMed:23684977};
DE Short=AtLIP1 {ECO:0000303|PubMed:23684977};
GN Name=LIP1 {ECO:0000303|PubMed:23684977};
GN OrderedLocusNames=At5g16500 {ECO:0000312|Araport:AT5G16500};
GN ORFNames=MQK4.24 {ECO:0000312|EMBL:BAB09618.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:ABE66160.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF CYS-7 AND CYS-10, AND PALMITOYLATION.
RX PubMed=23684977; DOI=10.1016/j.cub.2013.04.043;
RA Liu J., Zhong S., Guo X., Hao L., Wei X., Huang Q., Hou Y., Shi J.,
RA Wang C., Gu H., Qu L.J.;
RT "Membrane-bound RLCKs LIP1 and LIP2 are essential male factors controlling
RT male-female attraction in Arabidopsis.";
RL Curr. Biol. 23:993-998(2013).
RN [5]
RP INTERACTION WITH PRK6.
RX PubMed=26961657; DOI=10.1038/nature17413;
RA Takeuchi H., Higashiyama T.;
RT "Tip-localized receptors control pollen tube growth and LURE sensing in
RT Arabidopsis.";
RL Nature 531:245-248(2016).
CC -!- FUNCTION: Involved in pollen tube guidance into micropyle. Participates
CC in perception of the ovule-secreted peptide signal LURE1.
CC {ECO:0000269|PubMed:23684977}.
CC -!- SUBUNIT: Interacts with PRK6. {ECO:0000269|PubMed:26961657}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23684977};
CC Lipid-anchor {ECO:0000305|PubMed:23684977}. Cytoplasm
CC {ECO:0000269|PubMed:23684977}. Note=In pollen tubes, mainly located in
CC the plasma membrane to the tip region. {ECO:0000269|PubMed:23684977}.
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen and in germinating
CC pollen tubes. {ECO:0000269|PubMed:23684977}.
CC -!- PTM: Palmitoylated. {ECO:0000305|PubMed:23684977}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Lip1 and lip2 double
CC mutants have a reduced male transmission.
CC {ECO:0000269|PubMed:23684977}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09618.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005242; BAB09618.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92301.1; -; Genomic_DNA.
DR EMBL; DQ446955; ABE66160.1; -; mRNA.
DR RefSeq; NP_197154.2; NM_121655.3.
DR AlphaFoldDB; Q1PDW3; -.
DR SMR; Q1PDW3; -.
DR STRING; 3702.AT5G16500.1; -.
DR iPTMnet; Q1PDW3; -.
DR PaxDb; Q1PDW3; -.
DR PRIDE; Q1PDW3; -.
DR ProteomicsDB; 238383; -.
DR EnsemblPlants; AT5G16500.1; AT5G16500.1; AT5G16500.
DR GeneID; 831511; -.
DR Gramene; AT5G16500.1; AT5G16500.1; AT5G16500.
DR KEGG; ath:AT5G16500; -.
DR Araport; AT5G16500; -.
DR TAIR; locus:2171342; AT5G16500.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q1PDW3; -.
DR OMA; NTSMRIN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q1PDW3; -.
DR PRO; PR:Q1PDW3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDW3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Cytoplasm; Kinase; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..636
FT /note="Receptor-like kinase LIP1"
FT /id="PRO_0000436434"
FT DOMAIN 74..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..434
FT /evidence="ECO:0000255"
FT COMPBIAS 27..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 250
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MUTAGEN 7
FT /note="C->S: Loss of membrane localization; when associated
FT with S-10."
FT /evidence="ECO:0000269|PubMed:23684977"
FT MUTAGEN 10
FT /note="C->S: Loss of membrane localization; when associated
FT with S-7."
FT /evidence="ECO:0000269|PubMed:23684977"
SQ SEQUENCE 636 AA; 71552 MW; C76FD6B1A557487C CRC64;
MIIMMNCFPC FTSQKSRNAP CTTNETNDDN VEHDEFRPPV VATTKRTEER EPAEQQPPVK
TFNFRELATA TKNFRQECLL GEGGFGRVYK GTLQSTGQLV AVKQLDKHGL HGNKEFLAEV
LSLAKLEHPN LVKLIGYCAD GDQRLLVFEY VSGGSLQDHL YEQKPGQKPM DWITRMKIAF
GAAQGLDYLH DKVTPAVIYR DLKASNILLD AEFYPKLCDF GLHNLEPGTG DSLFLSSRVM
DTYGYSAPEY TRGDDLTVKS DVYSFGVVLL ELITGRRAID TTKPNDEQNL VAWAQPIFKD
PKRYPDMADP LLRKNFSERG LNQAVAITSM CLQEEPTARP LISDVMVALS FLSMSTEDGI
PATVPMESFR DKSMSIALSR HGSCSVTPFC ISRKDVGNKS SSSSDSEDEE EEKEQKAEKE
EESTSKKRQE QEETATDSDD ESDSNSEKDQ EEEQSQLEKA RESSSSSSDS GSERRSIDET
NATAQSLKIS YSNYSSEEED NEKLSSKSSC KSNEESTFSR YDSGRDHDDS SRNTSMRINS
LAHDDKEEDE EENHETRSYS DHDDSPRNTS MRINSLSHDD DEEEEEENHQ TRLEHIHSSK
SEDQSVYSDD DAGESGESSL HRIEAKEEEH ISSDHD
