ID A0A2K1KTB5_PHYPA Unreviewed; 680 AA.
AC A0A2K1KTB5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=BTB domain-containing protein {ECO:0000259|PROSITE:PS50097};
GN ORFNames=PHYPA_003993 {ECO:0000313|EMBL:PNR57000.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR57000.1};
RN [1] {ECO:0000313|EMBL:PNR57000.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c3_4210V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR57000.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c3_4210V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c3_4210V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000256|ARBA:ARBA00002668}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; ABEU02000003; PNR57000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1KTB5; -.
DR PaxDb; 3218-PP1S1_642V6-1; -.
DR EnsemblPlants; Pp3c3_4210V3.1; Pp3c3_4210V3.1; Pp3c3_4210.
DR EnsemblPlants; Pp3c3_4210V3.2; Pp3c3_4210V3.2; Pp3c3_4210.
DR Gramene; Pp3c3_4210V3.1; Pp3c3_4210V3.1; Pp3c3_4210.
DR Gramene; Pp3c3_4210V3.2; Pp3c3_4210V3.2; Pp3c3_4210.
DR InParanoid; A0A2K1KTB5; -.
DR OrthoDB; 1217388at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006727; Chromosome 3.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR038920; BTB/POZ_dom_prot.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR31060:SF3; OS04G0579700 PROTEIN; 1.
DR PANTHER; PTHR31060; OSJNBA0011J08.25 PROTEIN-RELATED; 1.
DR Pfam; PF00651; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 282..358
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 75305 MW; AB60EFE9213B5C93 CRC64;
MAVVSRPPAW QQLQPRKAYQ HQQARGRPTS GVLYGSSGNV DGAGGSADIL QQEWSSRAQG
SGRSGKGDMS KSGRSVEQSN VVYQGDDFDG GFGSWCGCMN RSGAVTPPPR GGGVRGGKGR
KGGKKGSGEV KSGDVGSMVK NFSGSFERSV STSGSSPVFR PRLSPGKVSP VVEVVPPPAS
ISAVPAAQHQ QTVTSAVFSM SNYNLTSAAK MQNSSSGVSS SPPVDKIKAS PTLFEMMTHE
QELGPKAVHT ISLSQQLTFQ EKMKSILSGT SPGNQFNATN TSDLKLILNN REGYSVTVNV
HRHILVTHSR FFAAKLSDRW SKQQRTNSNL IEITDIDDVE IYLETLRLMY CEDVKKSLMK
ENVSRVLGIL KLSAHIMFEG GVFACLEYLE AVPWADEEEE KVTALMGQLQ LESVGVAADV
MKRCSALEST NSEDVLVRLL QAVTKGTDDK ARREMKSLVS RMLRENMSQN KNTVDVSKES
LYRACHACLD SLLHLFMQSK SGDDRGMLIE ISRQADNLHW LVDILIDRRI ADDFVRMWAH
QAELANLHAK VPVMFRYEVS RLTARLCIAI GKGQVLSPKD VRFLLLQTWL QPLVDDFAWM
QRCCRSLDKK VVEEGISQTI LTLPLKQQQS ILLSWFDRFS SSGDDCPNLQ KAFEVWWRRT
FSRPCIEEDA CAERREFCER
//
