ID A0A176VTF7_MARPO Unreviewed; 1480 AA.
AC A0A176VTF7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PGG domain-containing protein {ECO:0000259|Pfam:PF13962};
GN ORFNames=AXG93_2752s1030 {ECO:0000313|EMBL:OAE24089.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24089.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE24089.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24089.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE24089.1}.
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DR EMBL; LVLJ01002675; OAE24089.1; -; Genomic_DNA.
DR OrthoDB; 5476624at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR026961; PGG_dom.
DR PANTHER; PTHR24186:SF38; ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR PANTHER; PTHR24186; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13962; PGG; 2.
DR SMART; SM00248; ANK; 16.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1121..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1162..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1195..1218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1339..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1409..1430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1450..1476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 200..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 324..356
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 449..481
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 484..516
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 773..795
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 951..983
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1054..1187
FT /note="PGG"
FT /evidence="ECO:0000259|Pfam:PF13962"
FT DOMAIN 1342..1474
FT /note="PGG"
FT /evidence="ECO:0000259|Pfam:PF13962"
FT REGION 38..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 164410 MW; 2F30113D519519D1 CRC64;
MSKMKPDYKK LNYLDLHRPF EQVVKRLEEL DLAKEIRNGS DTAPSFDTEK VTTSPSSRSH
HDESAQSERL MRHAAGAGYL NFEKRFVKRL PEEDLFLKIK EGDLEGVKKI LQAGSGDPLR
CTEDGLNCWH LAARYGRHLI LGLLIEQTPS ENLPPILERK STESPFRTAL HYAADNVNTE
VINLLVPHQT IDVLNDVDGD GNTGLMIACD RSSGGEQAVE ILLQKGAAVS TQNDQGYNCL
MIAASRGNVA LVQRFMFSDV GIRYLREKRL IGMTEPQPHQ MFVNASADVT NETALHRAAA
RNYWKVLQLL KNDHNIIVDA RDWLDRTPLM IAAVEGNLSA VQILLMCHAD VNLLDKSKRS
SLHAAASQGR SKVLFELLMV DDLDVGGKDK DGDTALDIAC QLGYIEAVRQ IVDSIKLRIE
RESSTKVARR SSQMTGPRAK LRAACSHEDG RNCLHIAASH GRAEVIQTLV GYRGLLDIDS
QDRQGNTALI LAAESGHTAA FQMLVQSGAN VFLLNDNGYN CVHVAAKSCQ NDLLEAFLID
EDSAEFLGSE LLEGKEALCP TIPRFGTDWM PKDGPLGHAW NVARLELLEK TGGEKKYTPL
HLAGMATENS NSQKTQILLM WSYLILALKV RGFSNQYFYL TRDDEFQSLV REQLAAMYEE
KELRDLASTH QSRYTVLWFS MKLRWFWRDR PSTFFRVNKI SGGAVDNLLI KEFVEAFIQS
LNYCNAGDED NTTVLHYVAN RTTQSREPDE KYKSFVERLL KYPAIDATVV DSSSETPLHL
AMKSGNVCVV RQILEMVEKA HITPLILTAE NSSKQTPCSI AFDRWQANAK AARRHGRSPD
PNAEYSVSLE LLETFVIEKY LEQEDAINSA QSGCKEAMST LLHCLAVILR DRLRRDKKSP
AGGDALFQTT GTDDYGLTLV HYVAYRGSSQ LLVSLLKRHE YQNLVNKKCT SGYTPLHFAV
VMVNYEVVRV LLKGPASTEH NDRAGKAELA WRVRTTEEDG SGETPLEKVG KLKAESELPA
AKDRLSHIEQ MLLNESDVRE YVDKLYRDRQ VYVDASNAML VGAAVIASVT FAGWLQPPLG
YAEYSQYPVS DSAPSDGVRF ESYAAVQQHP SVQTFWVFNS LSFFFAVAAV VCGAGASLQM
QLSQEASNSF AIKGEVKRIR KWLAVTSLLM AGAIVCVLGA FGTAGYVVLP PEMKFRAGMI
VTLCIGIPIC VASLYWFFRS SGIVKPKSLH FAVHMVNYAV VRVLLRGPAS TEHNDRASEA
VRAWRVRTTE EDGSGYSPQP KTQAELPAAK DRESQGQDRS PAAVPQADRR DRLSHIEQML
LNESDVREYV DKLYRDRQVY VDASNAMLVG AAVIASVTFA GWLQPPLGYA EYSQYPVSDS
APSDGVRFES YAAVQQHPSV QTFWVFNSLS FFFAVAAVVC GAGASLQMQL SHEASNSFAI
KGEVKRIRKW LVVTSLLMAG AIVSFLGAFG TAGYLFCPRK
//
