GFS12_ARATH
ID GFS12_ARATH Reviewed; 1639 AA.
AC F4JY12; B5B8Z0; Q8VZH9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein GFS12 {ECO:0000303|PubMed:25618824};
DE EC=2.7.10.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=BEACH domain-containing protein D {ECO:0000303|PubMed:25618824};
DE AltName: Full=BEACH-domain homolog D {ECO:0000305};
DE AltName: Full=GREEN FLUORESCENT SEED 12 {ECO:0000303|PubMed:25618824};
GN Name=GFS12 {ECO:0000303|PubMed:25618824};
GN Synonyms=BCHD {ECO:0000303|PubMed:25618824};
GN OrderedLocusNames=At5g18525 {ECO:0000312|Araport:AT5G18525};
GN ORFNames=T28N17.10 {ECO:0000312|EMBL:AC069328};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000312|Proteomes:UP000006548};
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 IDENTIFICATION, AND NUCLEOTIDE SEQUENCE [MRNA] OF 737-1129.
RX PubMed=19392685; DOI=10.1111/j.1365-313x.2009.03900.x;
RA Saedler R., Jakoby M., Marin B., Galiana-Jaime E., Hulskamp M.;
RT "The cell morphogenesis gene SPIRRIG in Arabidopsis encodes a WD/BEACH
RT domain protein.";
RL Plant J. 59:612-621(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1052-1639.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY,
RP NOMENCLATURE, AND INTERACTION WITH BCHC1.
RX PubMed=25618824; DOI=10.1016/j.molp.2014.11.015;
RA Teh O.K., Hatsugai N., Tamura K., Fuji K., Tabata R., Yamaguchi K.,
RA Shingenobu S., Yamada M., Hasebe M., Sawa S., Shimada T.,
RA Hara-Nishimura I.;
RT "BEACH-domain proteins act together in a cascade to mediate vacuolar
RT protein trafficking and disease resistance in Arabidopsis.";
RL Mol. Plant 8:389-398(2015).
CC -!- FUNCTION: May act predominantly to suppress BCHC1, which itself is a
CC negative factor in protein storage vacuole (PSV) trafficking regulation
CC and plant effector triggered immunity (ETI). Required for ETI, but not
CC for cell death. {ECO:0000269|PubMed:25618824}.
CC -!- SUBUNIT: Interacts (via protein kinase 2 domain) with BCHC1 (via PH-
CC BEACH domain). {ECO:0000269|PubMed:25618824}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in the cotyledons of germinating
CC seedlings. Restricted to the vascular tissues of cotyledons. Detected
CC in root tips, apical meristem, young flower buds and receptacles.
CC {ECO:0000269|PubMed:25618824}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Accumulation of unprocessed
CC 12S globulin in the seeds. {ECO:0000269|PubMed:25618824}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL36064.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC069328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92575.1; -; Genomic_DNA.
DR EMBL; FM180203; CAQ77322.1; -; mRNA.
DR EMBL; AY064158; AAL36064.1; ALT_INIT; mRNA.
DR EMBL; AY143925; AAN28864.1; -; mRNA.
DR RefSeq; NP_974804.4; NM_203075.7.
DR AlphaFoldDB; F4JY12; -.
DR STRING; 3702.AT5G18525.1; -.
DR iPTMnet; F4JY12; -.
DR MetOSite; F4JY12; -.
DR PaxDb; F4JY12; -.
DR PRIDE; F4JY12; -.
DR ProteomicsDB; 224777; -.
DR EnsemblPlants; AT5G18525.1; AT5G18525.1; AT5G18525.
DR GeneID; 2745988; -.
DR Gramene; AT5G18525.1; AT5G18525.1; AT5G18525.
DR KEGG; ath:AT5G18525; -.
DR Araport; AT5G18525; -.
DR TAIR; locus:1006230455; AT5G18525.
DR eggNOG; KOG1786; Eukaryota.
DR HOGENOM; CLU_250373_0_0_1; -.
DR InParanoid; F4JY12; -.
DR OMA; NKMESCA; -.
DR OrthoDB; 101142at2759; -.
DR PRO; PR:F4JY12; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JY12; baseline and differential.
DR Genevisible; F4JY12; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR CDD; cd06071; Beach; 1.
DR Gene3D; 1.10.1540.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000409; BEACH_dom.
DR InterPro; IPR036372; BEACH_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02138; Beach; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01026; Beach; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR SUPFAM; SSF81837; SSF81837; 1.
DR PROSITE; PS50197; BEACH; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Kinase; Reference proteome; Repeat; Transferase; WD repeat.
FT CHAIN 1..1639
FT /note="Protein GFS12"
FT /id="PRO_0000434031"
FT DOMAIN 206..294
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255"
FT DOMAIN 336..608
FT /note="BEACH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT DOMAIN 715..788
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255"
FT REPEAT 1290..1333
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1336..1373
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1465..1499
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1511..1549
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1609..1639
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REGION 1377..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 978..984
FT /note="VRIGRLL -> GDYW (in Ref. 3; CAQ77322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1639 AA; 183399 MW; 2B71A76D1D035792 CRC64;
MRGEDSDLCF DCLDQRINSD FSDQIVFSYG VSDSPLPFGS SAVVKVSDSS EEFSASCSSC
ESTSSQFILE YLRKDEHGCL AKYVDKFVVK DREGNSNDAV ESDECLDCST SGSQATEDDD
TENITCGSVT CEHSGSFSCW RTVAALLPIA QIRKCSASEL QKLASSFHYE CPEDQILASL
HRLIDGKSSG QATHSFLCLL LGLPLLEEKS KLRCLRHPNL SPVLGLLTSS DCLVSVLPKA
PYTLENILYY SPSAIKSEWH RNFIIYQLLS ALAHLHGLKV SHGDIRPSNI LLSDSLWSWL
TIYSKPDLGS VDANSSASRR RWCVEGCYSY GLYADLKISS HLDWQTHFDK WWKGELSNFE
YLLVLNKLAG RRWGDHTFHP VMPWVIDFSK KPENDSDSGW RDLRKSKWRL AKGDEQLDFT
YSTFEFPHHV SDECLSELAV CSYKARRLPL SVLRKAVRSV YEPNEYPSDM QRLYDWTPDE
CIPEFYCDPR IFCSLHPSMS DLAVPPWASS PDEFIRLHRD ALESPHVSSL IHHWIDITFG
YKMSGHAAIT AKNVMLSSSE PTVPRSVGRR QLFFRPHPVR LGFSREKEQS RNELEMHTFH
GFGVDNKRSV ILLADEYLEE TEEASAFSDH ATHLCPKYHL RENLVESPLH VSYSENTKKV
NTSLPGTSKN KGLSSRISLN YLLEHMEVRD EASTELQELL QWRQDFCTGN ISKDIAGDIF
SIGCVLAELY LMKPLFNSVS LATYLEGGDL PELIKELPPP TQVIVEACIE QDWRRRPSAK
SLLDSPYFSA TVRSAHLFAA PLQLLAKGQT RLCYAASFAK QGVLKVMGTF VAEMCAVYCL
PLVTTPLSED ECELAYVLLK EFTKSLTPMA VQRLVLPSIQ KILLTTGYSH LKVSLLQDSF
VRELWNQIGK RVYLEMIHPL VISNLYNSPD KISASAASVL LIGSSEELGA PVTVHQTILP
LISYFGKGIC TDGIDVLVRI GRLLGVNFIV KQMLPLLEHV VCFCIDLSSM KKPEPVHSWC
SLALSDCLIT LDGLVALISD ELLIHELTKG RLCLHVRVLM QKNLELRVLQ FAATSLMSIC
QRIGQEMTAL HVLPQLKELF DEFAFSEKST DASDSLSWKI RTAEQKFHPE SPIKSRMDLV
LLLYPSFASL LGMEKLRQGC PTWLLLEQYL LKHHNWKWEY TGRSSRYNME ARPVLKQGPA
SKHTPKVLLN GSGRSVPQSQ GLRNSNHLKL HIHVPVEGQE AVLNPLVHEP WSWFPSPVTC
WDGLDIGRFG NPKDENRWKI RASVLSSARA HHGALRSLVV SEDECTVFTS GIDPGFKGSV
QKWELASLSC VSSYHAHEEV VNDIGILSST GKVASCDGTI HVWNSQTGKL ISLFSESPSD
QDQASSDPSS KNNSNPCNRH ASHGLSSGIF DENLYTCMHY LEYMDQLIVG TGFGALRFID
LARGQKLELW GGEAIESGFT SLVSALCSGG SQTKHGDGAS VSPSWIAAGF SSGQCRLFDL
RENGFISSWR AHDGYVTKLV APESHLLVSS SLDKTLRIWD LRKSWTPQPF VVKGHNDGVS
GFSIWGKDVI SISRNNIGIF SLAKSQDEEE QQQQRIIPQK LYMAEKGGRV KSDLSTICVL
PFSRLFIVGA HDGHLRICC
