ID R0FS57_9BRAS Unreviewed; 305 AA.
AC R0FS57;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
GN ORFNames=CARUB_v10018990mg {ECO:0000313|EMBL:EOA25642.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA25642.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000256|ARBA:ARBA00005441}.
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DR EMBL; KB870809; EOA25642.1; -; Genomic_DNA.
DR RefSeq; XP_006292744.1; XM_006292682.1.
DR AlphaFoldDB; R0FS57; -.
DR STRING; 81985.R0FS57; -.
DR GeneID; 17885896; -.
DR KEGG; crb:17885896; -.
DR eggNOG; KOG3058; Eukaryota.
DR OrthoDB; 67418at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF62; PHOSPHATIDYLINOSITOL:CERAMIDE INOSITOLPHOSPHOTRANSFERASE 1; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..240
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
FT REGION 269..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 34899 MW; BB459658E9982F9A CRC64;
MNLYIRREAS KLWKRLCSEI TTEIGLLAEN WKYLLAGLLC QYIHGLAARG VHYIHRPGPT
LQDSGFFVLP ELGQDKGYIS ETVFTCVFVS FFLWTFHPFI VKSKKIYTVL IWCRVLAFLV
ACQFLRIITF YSTQLPGPNY HCREGSELAR LPRPHSVLEV LLLNFPRGVI YGCGDLIFSS
HMIFTLVFVR TYQRYGSKRF IKLLGWVIAI LQSLLIIASR KHYTVDVVVA WYTVNLVVFF
LESKLPELPD RTMVLLPVIT KDRTKEENHK LLNGNGVDPA DWRPRAQANG KDSNGGHTDN
TTNGA
//
