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Database: UniProt
Entry: A0A176VGH8_MARPO
LinkDB: A0A176VGH8_MARPO
Original site: A0A176VGH8_MARPO 
ID   A0A176VGH8_MARPO        Unreviewed;       386 AA.
AC   A0A176VGH8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE20004.1};
GN   ORFNames=AXG93_17s1030 {ECO:0000313|EMBL:OAE20004.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE20004.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE20004.1, 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:OAE20004.1};
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   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375, ECO:0000256|RuleBase:RU000488}.
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:OAE20004.1}.
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DR   EMBL; LVLJ01003721; OAE20004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VGH8; -.
DR   OrthoDB; 1215218at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   PANTHER; PTHR45667:SF17; -; 1.
DR   PANTHER; PTHR45667; S-ADENOSYLMETHIONINE MITOCHONDRIAL CARRIER PROTEIN; 1.
DR   Pfam; PF00153; Mito_carr; 2.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50920; SOLCAR; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}; Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000488}.
FT   REPEAT          14..100
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          110..261
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   386 AA;  41896 MW;  C752AD41C52CEEFF CRC64;
     MGLSPNAIEE SRKALFVRHG AAFVGAVATE TAFFYPIDTL KTLLQVNANA GRKLDVSAVV
     EGVSKSSGFT GLYGGVGWQL LGRLSSLGLR FGVYELMTAF YADGRSDSYV SLSESFLGGL
     TAGAVESLVS TPFDILKVRA QITSATTGVI KVQGETVKLN AHKAQPNLPT NIPDGPHWDR
     IRRSLSLLPS RSPDITADLR KYPWLATGSG QPPLVKDVGG LRGAVGLEGL NVLWRGLRPG
     LYRDAMYGGF FFCGWQFLDD LATEGRAYMM NPPPTSWDDV SPSSPWQLSI TAGIVASFAA
     TASHSFDSAK TRLQATVVPK YLTMERKMLK WKAPGSWFES IVGFSPFDRH FLRRGLGLRA
     LQHGCGTFAL VLTYHTAVQA AKIKKW
//
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