SERIC_MONBE
ID SERIC_MONBE Reviewed; 483 AA.
AC A9UY97;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Probable serine incorporator;
GN Name=serinc; ORFNames=18904;
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154;
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- FUNCTION: Enhances the incorporation of serine into phosphatidylserine
CC and sphingolipids. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; CH991549; EDQ89821.1; -; Genomic_DNA.
DR RefSeq; XP_001745243.1; XM_001745191.1.
DR AlphaFoldDB; A9UY97; -.
DR SMR; A9UY97; -.
DR STRING; 81824.XP_001745243.1; -.
DR EnsemblProtists; EDQ89821; EDQ89821; MONBRDRAFT_18904.
DR GeneID; 5890460; -.
DR KEGG; mbr:MONBRDRAFT_18904; -.
DR eggNOG; KOG2592; Eukaryota.
DR InParanoid; A9UY97; -.
DR OMA; MEPDDKQ; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005016; TDE1/TMS.
DR InterPro; IPR029559; Tms1-like.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF9; PTHR10383:SF9; 1.
DR Pfam; PF03348; Serinc; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..483
FT /note="Probable serine incorporator"
FT /id="PRO_0000342156"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 483 AA; 52665 MW; 51196206B5806C33 CRC64;
MGLVASCFGG LAAYAAESVA CCCGSAACSL CCRSCPSCTN STSTRITYAI LFFLSSIAAW
IMLDKDVSKG LMKVCCYHST LFRLVLFTQP AIKTTTNVVP WGELGVMRIM FSVCLFHLFL
SLCTIGVSSS KDPRSSLHNG MWFIKLILLV GAMVGSFFIS NSFFIGASWS WIGLVGAVLF
MIVQFILLVD FAYSWNDSWV GKLEEGSKCA GFGSYRLISA TVMLMAFVIT LTVLMFHFYT
NGDCKLSNFF IGFNLALALL VTLTSMLPSV REALPSSGIL QSSVVAAYAT YLVWSAVSGV
PSTCHPLIAV APLFLSSRGF LPPLPYVALK PAECGGDAGT NTAAIVIGAL LTFISVAYSS
IRTSSKSQLG KLGLQQGSNE NIYLMDDKAA DFDEDDEDRR LQRVVDNEQD AVRYSWSFFH
LTFAVAALYL MMVLTEWDSS DADVRIGKGW ASVWVQVVSS WVIFLLYGWT MMAPVCLPDR
DFS