SERC1_PONAB
ID SERC1_PONAB Reviewed; 453 AA.
AC Q5R419; Q5R4G3; Q5RCN8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=SERINC1; Synonyms=TDE2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enhances the incorporation of serine into phosphatidylserine
CC and sphingolipids. {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- SUBUNIT: Interacts with SPTLC1. {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7TNK0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; CR858232; CAH90469.1; -; mRNA.
DR EMBL; CR859032; CAH91227.1; -; mRNA.
DR EMBL; CR861286; CAH93353.1; -; mRNA.
DR EMBL; CR861441; CAH93497.1; -; mRNA.
DR RefSeq; NP_001125724.1; NM_001132252.1.
DR AlphaFoldDB; Q5R419; -.
DR SMR; Q5R419; -.
DR STRING; 9601.ENSPPYP00000019007; -.
DR Ensembl; ENSPPYT00000046612; ENSPPYP00000039127; ENSPPYG00000016977.
DR GeneID; 100172649; -.
DR KEGG; pon:100172649; -.
DR CTD; 57515; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR InParanoid; Q5R419; -.
DR OrthoDB; 1276632at2759; -.
DR Proteomes; UP000001595; Chromosome 6.
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:0006658; P:phosphatidylserine metabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR InterPro; IPR029557; Serinc1/3.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF15; PTHR10383:SF15; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Lipoprotein;
KW Membrane; Myristate; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT CHAIN 2..453
FT /note="Serine incorporator 1"
FT /id="PRO_0000289995"
FT TOPO_DOM 2..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..309
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..426
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT CONFLICT 36
FT /note="T -> A (in Ref. 1; CAH93353)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="E -> K (in Ref. 1; CAH90469/CAH93353)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="I -> T (in Ref. 1; CAH90469)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="H -> R (in Ref. 1; CAH90469)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="W -> R (in Ref. 1; CAH90469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50509 MW; 89946E927801ECDF 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 VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
