WBC30_ARATH
ID WBC30_ARATH Reviewed; 1082 AA.
AC Q9SJK6; F4IPY4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative white-brown complex homolog protein 30;
DE AltName: Full=Putative non-intrinsic ABC protein 12;
DE AltName: Full=WBC-related protein 1;
GN Name=WBC30; Synonyms=NAP12; OrderedLocusNames=At2g37010; ORFNames=T1J8.19;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31586.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006922; AAD31586.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09334.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61200.1; -; Genomic_DNA.
DR PIR; D84787; D84787.
DR RefSeq; NP_001323430.1; NM_001336618.1.
DR RefSeq; NP_181238.4; NM_129257.4.
DR AlphaFoldDB; Q9SJK6; -.
DR SMR; Q9SJK6; -.
DR STRING; 3702.AT2G37010.1; -.
DR PaxDb; Q9SJK6; -.
DR PRIDE; Q9SJK6; -.
DR ProteomicsDB; 242639; -.
DR EnsemblPlants; AT2G37010.1; AT2G37010.1; AT2G37010.
DR EnsemblPlants; AT2G37010.2; AT2G37010.2; AT2G37010.
DR GeneID; 818275; -.
DR Gramene; AT2G37010.1; AT2G37010.1; AT2G37010.
DR Gramene; AT2G37010.2; AT2G37010.2; AT2G37010.
DR KEGG; ath:AT2G37010; -.
DR Araport; AT2G37010; -.
DR TAIR; locus:2057921; AT2G37010.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_0_1; -.
DR InParanoid; Q9SJK6; -.
DR OrthoDB; 1022017at2759; -.
DR PRO; PR:Q9SJK6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJK6; baseline and differential.
DR Genevisible; Q9SJK6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1082
FT /note="Putative white-brown complex homolog protein 30"
FT /id="PRO_0000250663"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 484..726
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 832..1029
FT /note="ABC transmembrane type-2"
FT REGION 329..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518..525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1082 AA; 120579 MW; 735E1E7EA4B38B13 CRC64;
MRVRVDVCWT QHIFLFFVFG LSFMSFALSL DGDDYSKTGN PKALVSVTNL IYTRLQNLKT
VLKADVDRDL GYCIKNLKGD WNEAFNFDKN LDFLSNCVKK NDGDLTLRLC SAAEIKFYFS
SFVRRDEATT VHVKPNINCN LAKWVSGCEP GWSCNADDEK RFDLNNGKIL PSRTRKCQPC
CEGFFCPQGL ACMIPCPLGA YCPLAKLNKT TGFCEPYNYQ IPPGKLNHTC GSADSWVDAE
SSGDMFCSPG SYCPTTIRKV TCSSGHYCRQ GSTSQKPCFK LATCNPNTAN QNIHAYGAIL
IASLSLLMIM VYNCSDQVLA TREKRQAKSR EAAARHAKET TQARERWKTA KGVAKNQKMG
LSAQLSQTFS RMKSARKDAT PVKASGKSKD KKKEPSNLTK MMKSMEENPS NNEGFNVGTG
SKPGKKPQAP KGKQLHTQSQ IFKYAYGQIE KEKAMEQNNK NLTFSGVISM ATDTEMRTRP
VIEVAFKDLT LTLKGKHKHI LRSVTGKIMP GRVSAVMGPS GAGKTTFLSA LAGKATGCTR
TGLILINGRN DSINSYKKIT GFVPQDDVVH GNLTVEENLR FSARCRLSAY MSKADKVLII
ERVIESLGLQ HVRDSLVGTI EKRGISGGQR KRVNVGVEMV MEPSLLILDE PTTGLDSASS
QLLLRALRRE ALEGVNICMV VHQPSYTMYK MFDDMIILAK GGLTVYHGSV KKIEEYFADI
GITVPDRVNP PDHYIDILEG IVKPDGDITI EQLPVRWMLH NGYPVPHDML KFCDGLPSSS
TGSAQEDSTH NSFSNDLWQD VKTNVEITKD QLQHNYSNSH DNSNRVTPTV GRQYRYFVGR
VGKQRLREAR LQALDFLILL VAGACLGTLA KVNDETIDTL GYTYTIIAVS LLCKISALRS
FSVDKLQYWR ESAAGISSLA HFMAKDTMDH LNTIMKPLVY LSMFYFFNNP RSSFEDNYIV
LVCLVYCVTG MAYIFAILYS PSAAQLLSVL VPVVMTLIAN QDKESMVLKY LGSFCYPKWT
LEAFVLSNAQ RYSGVWVVTR CSSLSQNGYD LSDWILCLIV LVLMGLICRF IAYFCMVTFQ
KK
