GenomeNet

Database: UniProt
Entry: A0A176WHX2_MARPO
LinkDB: A0A176WHX2_MARPO
Original site: A0A176WHX2_MARPO 
ID   A0A176WHX2_MARPO        Unreviewed;       534 AA.
AC   A0A176WHX2;
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=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN   ORFNames=AXG93_107s1100 {ECO:0000313|EMBL:OAE32727.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE32727.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE32727.1, 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:OAE32727.1};
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 fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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:OAE32727.1}.
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; LVLJ01000744; OAE32727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WHX2; -.
DR   OrthoDB; 294339at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:UniProt.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProt.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProt.
DR   CDD; cd03506; Delta6-FADS-like; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353:SF88; DELTA(5) FATTY ACID DESATURASE FAT-4; 1.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
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        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..137
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  60569 MW;  AAD1BAB132213BB1 CRC64;
     MASSTTTAVK QSSGGLWSKW GTGSNLSFVS RKEQQQQQQQ SSPEASTPAA QQEKSISRES
     IPEGFLTVEE VSKHDNPSDC WIVINDKVYD VSAFGKTHPG GPVIFTQAGR DATDSFKVFH
     SAKAWQFLQD LYIGDLYNAE PVSELVKDYR DLRTAFMRSQ LFKSSKMYYV TKCVTNFAIL
     AASLAVIAWS QTYLAVLCSS FLLALFWQQC GWLSHDFLHH QVTENRSLNT YFGGLFWGNF
     AQGYSVGWWK TKHNVHHAAT NECDDKYQPI DPDIDTVPLL AWSKEILATV DDQFFRSIIS
     VQHLLFFPLL FLARFSWLHS SWAHASNFEM PRYMRWAEKA SLLGHYGASI GAAFYILPIP
     QAICWLFLSQ LFCGALLSIV FVISHNGMDV YNDPRDFVTA QVTSTRNIEG NFFNDWFTGG
     LNRQIEHHLF PSLPRHNLAK VAPHVKALCA KHGLHYEELS LGTGVCRVFN RLVEVAYAAK
     LEQGNSTREG DSNLDFLFLM LHTFSNIRLH AFKFQLQLIV FSNHRLLQLG DLQN
//
DBGET integrated database retrieval system