ID A0A176VF99_MARPO Unreviewed; 321 AA.
AC A0A176VF99;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=MIR domain-containing protein {ECO:0000259|PROSITE:PS50919};
GN ORFNames=AXG93_3756s1340 {ECO:0000313|EMBL:OAE19628.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19628.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19628.1, 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:OAE19628.1};
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:OAE19628.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVLJ01003810; OAE19628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VF99; -.
DR OrthoDB; 103242at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR PANTHER; PTHR46809:SF8; GH21273P; 1.
DR PANTHER; PTHR46809; STROMAL CELL-DERIVED FACTOR 2-LIKE PROTEIN; 1.
DR Pfam; PF02815; MIR; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 90..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..188
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 196..251
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 254..308
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 321 AA; 35873 MW; 463A6ABBBB8195AD CRC64;
MKGVNDRRVV DSVEWTRCEE GGKSVESSGV KSLTQRSRLV TGNSASGKER LELEQEAIRR
RDEHLRSVHQ KKKKEKQEQG GLLTYKELTF WALSGLGFLA VMGFLIFGVL LMVGFMKPFE
DSGPQSAWAA TGEGKEVTYG SVIKLQHDRT KYRLHSHEVP YGTGSGQQSV TGFPGGEDAN
SYWVVKPVSD SDARQGDLVS DGAIVRLFHT RTRKWLHSHL HASPITGNYE VSAFGADDQS
DTGDHWKLII EGKGKVWLRD QKVRFLHVDT GGYLHSHDKK YSRIVAGQQE VCGYLKKNSD
NLWFAAEGVY FPSRNEGKAS I
//
