ANX1_ARATH
ID ANX1_ARATH Reviewed; 850 AA.
AC Q9SR05;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Receptor-like protein kinase ANXUR1;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=ANX1; OrderedLocusNames=At3g04690; ORFNames=F7O18.16;
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, 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 (1.80 ANGSTROMS) OF 27-410, AND GLYCOSYLATION AT
RP ASN-114; ASN-132; ASN-292 AND ASN-302.
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:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AC011437; AAF04910.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74120.1; -; Genomic_DNA.
DR RefSeq; NP_187120.1; NM_111341.3.
DR PDB; 5Y96; X-ray; 1.80 A; A=27-410, B=28-410.
DR PDB; 6A5A; X-ray; 2.94 A; A/B=26-410.
DR PDB; 6FIG; X-ray; 1.48 A; A/B=26-429.
DR PDBsum; 5Y96; -.
DR PDBsum; 6A5A; -.
DR PDBsum; 6FIG; -.
DR AlphaFoldDB; Q9SR05; -.
DR SMR; Q9SR05; -.
DR STRING; 3702.AT3G04690.1; -.
DR UniLectin; Q9SR05; -.
DR iPTMnet; Q9SR05; -.
DR PaxDb; Q9SR05; -.
DR PRIDE; Q9SR05; -.
DR ProteomicsDB; 244468; -.
DR EnsemblPlants; AT3G04690.1; AT3G04690.1; AT3G04690.
DR GeneID; 819627; -.
DR Gramene; AT3G04690.1; AT3G04690.1; AT3G04690.
DR KEGG; ath:AT3G04690; -.
DR Araport; AT3G04690; -.
DR TAIR; locus:2084953; AT3G04690.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_4_1; -.
DR InParanoid; Q9SR05; -.
DR OMA; HFYPSEY; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SR05; -.
DR PRO; PR:Q9SR05; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR05; baseline and differential.
DR Genevisible; Q9SR05; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..850
FT /note="Receptor-like protein kinase ANXUR1"
FT /id="PRO_0000385331"
FT TOPO_DOM 27..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..850
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 517..790
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 796..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 641
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 523..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y96"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y96"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y96"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29388293,
FT ECO:0007744|PDB:5Y96"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6FIG"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6A5A"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5Y96"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 301..312
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6FIG"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 352..362
FT /evidence="ECO:0007829|PDB:6FIG"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 388..397
FT /evidence="ECO:0007829|PDB:6FIG"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:6A5A"
SQ SEQUENCE 850 AA; 94048 MW; 3168704E7338820A CRC64;
MSGKTRILFF LTCLSFLLVF PTRSNGQDLA LSCGTSEASA DQDKKKWEPD TKFLKTGNSI
HATATYQDPS LLSTVPYMTA RIFTAPATYE IPIKGDKRHL LRLYFYPSTY TGLNISNSYF
TVEANDVTLL SNFSAAITCQ ALTQAYLVKE YSLAPTDKDV LSIKFTPSDK YRDAFAFING
IEVIQMPELF DTAALVGFTD QTMDAKTANL QSMFRLNVGG QDIPGSQDSG GLTRTWYNDA
PYIFSAGLGV TLQASNNFRI NYQNMPVSIA PADIYKTARS QGPNGDINLK SNLTWMFQID
KNFTYILRLH FCEFQLSKIN QKVFNIYINN RTAQADTTPA DIIGWTGEKG IPMYKDYAIY
VDANNGGEEI TLQMTPSTFG QPEYYDSSLN GLEIFKMDTM KNLAGPNPEP SPMQAEEEVK
KEFKNEKRHA FIIGSAGGVL AVLIGALCFT AYKKKQGYQG GDSHTSSWLP IYGNSTTSGT
KSTISGKSNN GSHLSNLAAG LCRRFSLPEI KHGTQNFDDS NVIGVGGFGK VYKGVIDGTT
KVAVKKSNPN SEQGLNEFET EIELLSRLRH KHLVSLIGYC DEGGEMCLVY DYMAFGTLRE
HLYNTKKPQL TWKRRLEIAI GAARGLHYLH TGAKYTIIHR DVKTTNILVD ENWVAKVSDF
GLSKTGPNMN GGHVTTVVKG SFGYLDPEYF RRQQLTEKSD VYSFGVVLFE ILCARPALNP
SLPKEQVSLG DWAMNCKRKG NLEDIIDPNL KGKINAECLK KFADTAEKCL NDSGLERPTM
GDVLWNLEFA LQLQETADGT RHRTPNNGGS SEDLGRGGMA VNVAGRDDVS DLSSEDNTEI
FSQIVNPKGR
