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Database: UniProt
Entry: Q9SR05
LinkDB: Q9SR05
Original site: Q9SR05 
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   24-JAN-2024, entry version 153.
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.Q9SR05; -.
DR   UniLectin; Q9SR05; -.
DR   GlyCosmos; Q9SR05; 5 sites, No reported glycans.
DR   iPTMnet; Q9SR05; -.
DR   PaxDb; 3702-AT3G04690-1; -.
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; AT3G04690; ANX1.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_42_4_1; -.
DR   InParanoid; Q9SR05; -.
DR   OMA; PEPSPMQ; -.
DR   OrthoDB; 465256at2759; -.
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:0090404; C:pollen tube tip; IDA:TAIR.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; OS07G0166700 PROTEIN; 1.
DR   PANTHER; PTHR27003:SF465; RECEPTOR-LIKE PROTEIN KINASE ANXUR1-RELATED; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
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