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Database: UniProt
Entry: A0A176WLV2_MARPO
LinkDB: A0A176WLV2_MARPO
Original site: A0A176WLV2_MARPO 
ID   A0A176WLV2_MARPO        Unreviewed;       834 AA.
AC   A0A176WLV2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-MAR-2018, entry version 7.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE34019.1};
GN   ORFNames=AXG93_4142s1040 {ECO:0000313|EMBL:OAE34019.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae;
OC   Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE34019.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE34019.1, 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:OAE34019.1};
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
RT   tip-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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAE34019.1}.
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DR   EMBL; LVLJ01000462; OAE34019.1; -; Genomic_DNA.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0016485; P:protein processing; IEA:InterPro.
DR   InterPro; IPR008710; Nicastrin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR21092; PTHR21092; 1.
DR   Pfam; PF05450; Nicastrin; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077202};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN      732    834       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   834 AA;  90363 MW;  421DC61CB4317F5F CRC64;
     MYQSVDGTAC VRLLSLDGEV GCAGPDRRAV LAPLQHFSDA NIQLSTKTTV VLPLSALHQF
     LNRTVNERSL AKHVAGVLVE HGGADGQNLS RGFSPDTRFP QAEFAPYKAE YVWNPPGSGV
     LQQRFEFPVF LLTPESTAAV RELTAGNEKR NFKYPLHVAE FDFVMQSTKS GTHDSESCLK
     EWACLPLGGY SVWSSLPAIN VTSPVENPIV LVMAAMDSAS FFRDATPGAD SPLSGLIAML
     AAADALSRVP DVDEFQKQIV FLALTGEAWG YLGSRRFISE LAGGNPALSG LSLSRIHQVL
     EIGSVGKAVD AGRATLYVHK QKDQVSSATN EMVEALQLSA TSLAGAQHVG AVEVKMASKL
     NPGVPPSSLM SFIQKNSSTA AIVLEEFDEV FKNTLYHSHL DDANNIDKNS IAGTAALIAR
     TVYLLGDSAA NATQLQSIEV NSSLVSELVD CLLRQSPGMV CDLVKGLITP TQQYANHYVG
     VLLGEPSFSP YLENVDDISR FVWNFLASRT GIVRNQQVKD GVAAGIKRAS ASSFEECAQK
     CSNIDEICVG ATGEHKGRCI MSTTRFVPAY SPRLQFEAAS WKVVAAEPGD IMSEMDPVWT
     ESFWKSISIW YFAVFRCLLN LPVPATSVVK EVEFWDAKNF SAHARALGFG FPVVGTRSSG
     RRRDGDTRRV AALNSLGTNP ERISSDRHDL GAMAARGALL RSFRRSTCQM TRTVASSSAT
     TRSHLAQVLK HDVALPLAPS FSATDHLPYV GYPPAFRPRL FSSHAAGSSS NVVLVSDDAH
     FQQSLKEVES SKSLGVVYFT AQWCGPCKQI APYIDELSRE FDDVTFLKID VDNV
//
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