LIPG2_ARATH
ID LIPG2_ARATH Reviewed; 558 AA.
AC Q9M8S2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Receptor-like kinase LIP2 {ECO:0000303|PubMed:23684977};
DE EC=2.7.11.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein LOST IN POLLEN TUBE GUIDANCE 2 {ECO:0000303|PubMed:23684977};
DE Short=AtLIP2 {ECO:0000303|PubMed:23684977};
GN Name=LIP2 {ECO:0000303|PubMed:23684977};
GN OrderedLocusNames=At3g02810 {ECO:0000312|Araport:AT3G02810};
GN ORFNames=F13E7.25 {ECO:0000312|EMBL:AAF26979.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF CYS-3 AND CYS-6, 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 SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=24963069; DOI=10.1104/pp.114.236133;
RA Dai X.R., Gao X.-Q., Chen G.H., Tang L.L., Wang H., Zhang X.S.;
RT "ABNORMAL POLLEN TUBE GUIDANCE1, an endoplasmic reticulum-localized
RT mannosyltransferase homolog of GLYCOSYLPHOSPHATIDYLINOSITOL10 in yeast and
RT PHOSPHATIDYLINOSITOL GLYCAN ANCHOR BIOSYNTHESIS B in human, is required for
RT Arabidopsis pollen tube micropylar guidance and embryo development.";
RL Plant Physiol. 165:1544-1556(2014).
RN [6]
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 ECO:0000269|PubMed:24963069}; Lipid-anchor
CC {ECO:0000305|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}.
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DR EMBL; AC018363; AAF26979.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73862.1; -; Genomic_DNA.
DR EMBL; BT004041; AAO42074.1; -; mRNA.
DR EMBL; BT004942; AAO50475.1; -; mRNA.
DR RefSeq; NP_186930.1; NM_111149.3.
DR AlphaFoldDB; Q9M8S2; -.
DR SMR; Q9M8S2; -.
DR IntAct; Q9M8S2; 1.
DR STRING; 3702.AT3G02810.1; -.
DR PaxDb; Q9M8S2; -.
DR PRIDE; Q9M8S2; -.
DR ProteomicsDB; 238560; -.
DR EnsemblPlants; AT3G02810.1; AT3G02810.1; AT3G02810.
DR GeneID; 821236; -.
DR Gramene; AT3G02810.1; AT3G02810.1; AT3G02810.
DR KEGG; ath:AT3G02810; -.
DR Araport; AT3G02810; -.
DR TAIR; locus:2075517; AT3G02810.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_0_1; -.
DR InParanoid; Q9M8S2; -.
DR OMA; HTHIEHI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9M8S2; -.
DR PRO; PR:Q9M8S2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8S2; baseline and differential.
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; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..558
FT /note="Receptor-like kinase LIP2"
FT /id="PRO_0000436435"
FT DOMAIN 64..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 70..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 138
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MUTAGEN 3
FT /note="C->S: Loss of membrane localization; when associated
FT with S-6."
FT /evidence="ECO:0000269|PubMed:23684977"
FT MUTAGEN 6
FT /note="C->S: Loss of membrane localization; when associated
FT with S-3."
FT /evidence="ECO:0000269|PubMed:23684977"
SQ SEQUENCE 558 AA; 62402 MW; D6E8DB2A957432DB CRC64;
MHCFPCFSSP KNKKSSTTNE TNDNNEPKPD DRRRAEETEE IEQSEGTSLK IFTFRELATA
TKNFRQECLL GEGGFGRVYK GTLKSTGQVV AVKQLDKHGL HGNKEFQAEV LSLGQLDHPN
LVKLIGYCAD GDQRLLVYDY ISGGSLQDHL HEPKADSDPM DWTTRMQIAY AAAQGLDYLH
DKANPPVIYR DLKASNILLD DDFSPKLSDF GLHKLGPGTG DKMMALSSRV MGTYGYSAPE
YTRGGNLTLK SDVYSFGVVL LELITGRRAL DTTRPNDEQN LVSWAQPIFR DPKRYPDMAD
PVLENKFSER GLNQAVAIAS MCVQEEASAR PLISDVMVAL SFLSMPTEDG IPTTVPILSF
KDKSMSIALS RHDSNLVSPP PELATEDDKS STSSGEESSL ESEKESVSKN EYKKKHEEED
SSMESDDESD SNSEHEKDQP PKPIDEKNQA QSLKIKYRYS WEDIDVNDER LSSKSSQKSN
DESTSSRYDS DRDQDEKGKE EEEEEEAEEK HTHIEHIDSS KTDDDQSVYF DNDDDSGDDN
GGSLHRIKSD VAIDSIKE
