ID A0A176VPR4_MARPO Unreviewed; 553 AA.
AC A0A176VPR4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN ORFNames=AXG93_3491s1220 {ECO:0000313|EMBL:OAE22281.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE22281.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE22281.1, 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:OAE22281.1};
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 -!- 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:OAE22281.1}.
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DR EMBL; LVLJ01003243; OAE22281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VPR4; -.
DR OrthoDB; 448980at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR PANTHER; PTHR47104; SEC14P-LIKE PHOSPHATIDYLINOSITOL TRANSFER FAMILY PROTEIN; 1.
DR PANTHER; PTHR47104:SF1; SEC14P-LIKE PHOSPHATIDYLINOSITOL TRANSFER FAMILY PROTEIN; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..408
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60958 MW; F07D1391A17FED4A CRC64;
MGLDGTALMR ERESDGSRGA RGWWAGRDRE TRKPRKKSGG GPEGPVGVDD GETGRSSTKS
ERRRRSSSSG EDDDDDARRE RSGGERCKDT SGGSQQCVAA CAAATATPVL LASAAVVATT
PARSGGDPYV VIVCECGGRG AAAAAAASAV GNPPEDYEFS QSTLGHRKQF RRDYVRRLVC
LKILVHIAVI VYWGWLTFPT WLEFCDDACV ERYLKARGYN VRRAAKLLKA TLAWRENFDV
DYLIADEFTA ELASGVSYVA GHDNEGRPVV IVRRKNFTYG AWSQKQYLRY LIFTMEVAVA
SMGPGVDQWV LVIDMGHAKL TSPSSSTILG TLRILNEHYP ERLAKAYVVD SPSVLYFLWK
SICPFVDYGT KGKVTFASSK DHALSEAVAA TSNRNSTQDK DGRSSLRRLL QESPSFRALR
PERNTSNESA LVNSPHCRSL SFSTPGTAFN TPALRGKEFS SFRADRNSWI PGLLSGNHSR
KLKAGEGHSF RLGRRPELQP GGAEQREKSP NSFRQYWKFF RAEYNESAYR ATMKPPHGGL
KSIIGFSMKN NLT
//
