ANX2_ARATH
ID ANX2_ARATH Reviewed; 858 AA.
AC Q3E8W4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Receptor-like protein kinase ANXUR2;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=ANX2; OrderedLocusNames=At5g28680; ORFNames=F4I4.60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19646876; DOI=10.1016/j.cub.2009.06.064;
RA Miyazaki S., Murata T., Sakurai-Ozato N., Kubo M., Demura T., Fukuda H.,
RA Hasebe M.;
RT "ANXUR1 and 2, sister genes to FERONIA/SIRENE, are male factors for
RT coordinated fertilization.";
RL Curr. Biol. 19:1327-1331(2009).
RN [4]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-414, AND GLYCOSYLATION AT
RP ASN-133; ASN-293; ASN-303 AND ASN-331.
RX PubMed=29388293; DOI=10.1002/pro.3381;
RA Du S., Qu L.J., Xiao J.;
RT "Crystal structures of the extracellular domains of the CrRLK1L receptor-
RT like kinases ANXUR1 and ANXUR2.";
RL Protein Sci. 27:886-892(2018).
CC -!- FUNCTION: Receptor-like protein kinase that controls pollen tube
CC behavior by directing rupture at proper timing to release the sperm
CC cell. {ECO:0000269|PubMed:19646876}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19646876};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19646876}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen, but not in pistils or
CC seedlings. {ECO:0000269|PubMed:19646876}.
CC -!- DISRUPTION PHENOTYPE: No effect on male fertility and pollen
CC germination, but siliques slightly shorter. Anx1 and anx2 double
CC mutants show defects in male gametophytes due to premature pollen tube
CC rupture. {ECO:0000269|PubMed:19646876}.
CC -!- MISCELLANEOUS: Male paralog of FERONIA, a female factor expressed in
CC synergid cells that controls pollen tube behavior.
CC -!- MISCELLANEOUS: Named Anxur after the husband of the Etruscan goddess of
CC fertility Feronia.
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; AF272705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93826.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68270.1; -; Genomic_DNA.
DR RefSeq; NP_001318669.1; NM_001344080.1.
DR RefSeq; NP_198220.1; NM_122751.2.
DR PDB; 5Y92; X-ray; 2.00 A; A=28-414.
DR PDB; 6A5C; X-ray; 1.68 A; A=21-450.
DR PDB; 6FIH; X-ray; 1.08 A; A=27-431.
DR PDBsum; 5Y92; -.
DR PDBsum; 6A5C; -.
DR PDBsum; 6FIH; -.
DR AlphaFoldDB; Q3E8W4; -.
DR SMR; Q3E8W4; -.
DR BioGRID; 18248; 1.
DR IntAct; Q3E8W4; 1.
DR STRING; 3702.AT5G28680.1; -.
DR iPTMnet; Q3E8W4; -.
DR PaxDb; Q3E8W4; -.
DR PRIDE; Q3E8W4; -.
DR ProteomicsDB; 244432; -.
DR EnsemblPlants; AT5G28680.1; AT5G28680.1; AT5G28680.
DR EnsemblPlants; AT5G28680.2; AT5G28680.2; AT5G28680.
DR GeneID; 832975; -.
DR Gramene; AT5G28680.1; AT5G28680.1; AT5G28680.
DR Gramene; AT5G28680.2; AT5G28680.2; AT5G28680.
DR KEGG; ath:AT5G28680; -.
DR Araport; AT5G28680; -.
DR TAIR; locus:2148830; AT5G28680.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_1_1; -.
DR InParanoid; Q3E8W4; -.
DR OMA; MTIRYDD; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q3E8W4; -.
DR PRO; PR:Q3E8W4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E8W4; baseline and differential.
DR Genevisible; Q3E8W4; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 3D-structure; ATP-binding; Cell membrane; Fertilization; Glycoprotein;
KW Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..858
FT /note="Receptor-like protein kinase ANXUR2"
FT /id="PRO_0000385332"
FT TOPO_DOM 28..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 521..794
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 800..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 527..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y92"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y92"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y92"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y92"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6A5C"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6FIH"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5Y92"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6A5C"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6A5C"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6A5C"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 302..313
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:6FIH"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 370..379
FT /evidence="ECO:0007829|PDB:6FIH"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:6FIH"
SQ SEQUENCE 858 AA; 94297 MW; D83B1371D545EA1F CRC64;
MNEKLRILFS FLCFFYVLLV SPSQSNGQDI SLSCGASEPA VDQDKKKWEP DTKFLKTPNT
VHAPATYQDP SLLSTVPYMT SRIFTAPATY EIPVKGDKRH MLRLHFYPST YTGLNILDSY
FSVAANDLTL LSNFSAAITC QALTQAYLVR EYSLAPSEKD VLSIIFTPSD KHPKAFAFIN
GIEVIPMPEL FDTASLVGFS DQTSDTKTAN LQTMFRLNVG GQDIPGSQDS GGLTRTWYND
APYIFSAGLG VTLQASNNFR IDYQKMPVST APADVYKTAR SQGPNGDINM KSNLTWMFQV
DTNFTYIMRL HFCEFQLAKI NQKVFNIFIN NRTAQGDTNP ADILGWTGGK GIPTYKDYAI
YVDANTGGGG EEISLQMTPS TFGQPEYYDS QLNGLEIFKI DTMKNLAGPN PKPSPMQANE
DVKKDFQGDK RITAFVIGSA GGVAAVLFCA LCFTMYQRKR KFSGSDSHTS SWLPIYGNSH
TSATKSTISG KSNNGSHLSN LAAGLCRRFS LSEIKHGTHN FDESNVIGVG GFGKVYKGVI
DGGTKVAIKK SNPNSEQGLN EFETEIELLS RLRHKHLVSL IGYCDEGGEM CLIYDYMSLG
TLREHLYNTK RPQLTWKRRL EIAIGAARGL HYLHTGAKYT IIHRDVKTTN ILLDENWVAK
VSDFGLSKTG PNMNGGHVTT VVKGSFGYLD PEYFRRQQLT EKSDVYSFGV VLFEVLCARP
ALNPSLSKEQ VSLGDWAMNC KRKGTLEDII DPNLKGKINP ECLKKFADTA EKCLSDSGLD
RPTMGDVLWN LEFALQLQET ADGSRHRTPS NGGGSVDLGG GGGGVTVNIS AGESDLGDDL
SSEENSGIFS QIVNPKGR
