ID A0A176WR35_MARPO Unreviewed; 804 AA.
AC A0A176WR35;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE34762.1};
GN ORFNames=AXG93_2528s1280 {ECO:0000313|EMBL:OAE34762.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE34762.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE34762.1, 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:OAE34762.1};
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 -!- FUNCTION: Acts as a molecular chaperone for G protein-coupled
CC receptors, regulating their biogenesis and exit from the ER.
CC {ECO:0000256|ARBA:ARBA00037107}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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:OAE34762.1}.
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DR EMBL; LVLJ01000312; OAE34762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WR35; -.
DR OrthoDB; 20116at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR021832; ANKRD13.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR12447; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13; 1.
DR PANTHER; PTHR12447:SF25; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13C; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF11904; GPCR_chapero_1; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT REPEAT 72..104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 355..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 90662 MW; D9DB22272E1F02B3 CRC64;
MAVLSTEEIS KLSHSPAHIA IARRDHSALR RILASVPRPA KAGEVRTEAE SIIAEQRADE
ASAVIDRRDV PGRETPLHLA VRLGDADAVE MLMAAGADWS LQNEHGWSAL QEAVCAREDA
IAMIITRYYQ PMAWAKWCRR LPRLTAAMGR MRDFYMELTF HFESSVIPFI GRIAPSDTYR
IWKRGSNLRA DMTLAGFDGF RIHRSDQSFL FLGDGSEDGK LPAGSLCVLS HKEKEVMNAL
EGAGVQPSEA EIAQEVAAMS QTNMYRPGID VTQAELVSHL NWRRQERTEM VGAWKAKIFD
MHHVLVSVRS RRVPGAMTDE ELFAVEGDRQ EGGELDEDYA DLLTAEEKQQ LESALRRDNF
DDDGFDDSRP RPSKVGQANG NGSYDSFDEE LEAADEEYNF HPSPAVERIE THDANMASTN
SEKKGWFGWG RKSVKVDSKR GEERASSSHE PARRSTMKPP RATDAIAHRR SVDHRRSVDV
PDRRHSSVDV MVDRRGSVDR RPSSVRDEDL FMLRKGKEKS KKASKEPVRK RRTEANSESE
YKKGLRPVLW LTQDFPLKTE ELLPLLDILA NKVKAVRRLR ELLTTKLPNG TFPVKVAIPV
VPTIRVVITF TKFEELKSSE EFSTPLSSPG HFQDSKGKEG ELPNLSSASW FSWIRGSQNG
SSNGAVYLED HIEEEIDPFL IPADYTWVDM NEKKRRMKEK KGKRCRNGLV RTVTLESQRE
TAFDQRNCPE GLIFVDVSGI VLRAECNLKV GIVCNQTRYT LRGQQADVFA RTPVKKSEVL
GPYSSVYSDV TFLLPELMAI AFED
//