ID A0A2K5CDL5_AOTNA Unreviewed; 453 AA.
AC A0A2K5CDL5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Serine incorporator 1 {ECO:0000256|ARBA:ARBA00040945};
DE AltName: Full=Tumor differentially expressed protein 2 {ECO:0000256|ARBA:ARBA00041691};
GN Name=SERINC1 {ECO:0000313|Ensembl:ENSANAP00000006694.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000006694.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000006694.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Enhances the incorporation of serine into phosphatidylserine
CC and sphingolipids. {ECO:0000256|ARBA:ARBA00037552}.
CC -!- SUBUNIT: Interacts with SPTLC1. {ECO:0000256|ARBA:ARBA00011492}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TDE1 family.
CC {ECO:0000256|ARBA:ARBA00006665}.
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DR RefSeq; XP_012305482.1; XM_012450059.1.
DR AlphaFoldDB; A0A2K5CDL5; -.
DR STRING; 37293.ENSANAP00000006694; -.
DR Ensembl; ENSANAT00000024464.1; ENSANAP00000006694.1; ENSANAG00000021397.1.
DR GeneID; 105715660; -.
DR CTD; 57515; -.
DR GeneTree; ENSGT01030000234623; -.
DR OMA; DKHCNPL; -.
DR OrthoDB; 53161at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; SERINE INCORPORATOR; 1.
DR PANTHER; PTHR10383:SF15; SERINE INCORPORATOR 1; 1.
DR Pfam; PF03348; Serinc; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 453 AA; 50523 MW; 6552142EA801F464 CRC64;
MGSVLGLCSM ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF AAAIAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIVLFFVYY THPASCSENK AFISVNMLLC
IGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGYNTT
STVPKEGQSV QWWHAQGIIG LILFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGGAR
SDGSLEDGDD VHRAIDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
//
