SERC1_RAT
ID SERC1_RAT Reviewed; 453 AA.
AC Q7TNK0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Tumor differentially expressed protein 1-like;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=Serinc1; Synonyms=Tde1l, Tde2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SPTLC1, SUBCELLULAR
RP LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=16120614; DOI=10.1074/jbc.m505712200;
RA Inuzuka M., Hayakawa M., Ingi T.;
RT "Serinc, an activity-regulated protein family, incorporates serine into
RT membrane lipid synthesis.";
RL J. Biol. Chem. 280:35776-35783(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Zhou G., Li W., Yu L., Wang J., Zhao S.;
RT "Rattus norvegicus tumor differentially expressed 1, like (Tde1l).";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Enhances the incorporation of serine into phosphatidylserine
CC and sphingolipids. {ECO:0000269|PubMed:16120614}.
CC -!- SUBUNIT: Interacts with SPTLC1. {ECO:0000269|PubMed:16120614}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16120614}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16120614}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus and
CC cerebellar granule cell layer. {ECO:0000269|PubMed:16120614}.
CC -!- INDUCTION: Up-regulated by kainate treatment in neuronal cell layers of
CC the hippocampus. {ECO:0000269|PubMed:16120614}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; AY339894; AAQ17069.1; -; mRNA.
DR EMBL; DQ103708; AAZ80295.1; -; mRNA.
DR EMBL; BC088852; AAH88852.1; -; mRNA.
DR RefSeq; NP_891996.1; NM_182951.1.
DR AlphaFoldDB; Q7TNK0; -.
DR SMR; Q7TNK0; -.
DR STRING; 10116.ENSRNOP00000001066; -.
DR iPTMnet; Q7TNK0; -.
DR PhosphoSitePlus; Q7TNK0; -.
DR jPOST; Q7TNK0; -.
DR PaxDb; Q7TNK0; -.
DR Ensembl; ENSRNOT00000001066; ENSRNOP00000001066; ENSRNOG00000029360.
DR GeneID; 294421; -.
DR KEGG; rno:294421; -.
DR UCSC; RGD:727843; rat.
DR CTD; 57515; -.
DR RGD; 727843; Serinc1.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01050000244881; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; Q7TNK0; -.
DR OMA; MEPDDKQ; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q7TNK0; -.
DR TreeFam; TF312881; -.
DR Reactome; R-RNO-977347; Serine biosynthesis.
DR PRO; PR:Q7TNK0; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000029360; Expressed in frontal cortex and 18 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0044091; P:membrane biogenesis; IDA:BHF-UCL.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:HGNC-UCL.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1904219; P:positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IDA:BHF-UCL.
DR GO; GO:1904222; P:positive regulation of serine C-palmitoyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:HGNC-UCL.
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 1: Evidence at protein 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_0000315995"
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:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
SQ SEQUENCE 453 AA; 50553 MW; 1DB300318421A4C1 CRC64;
MGSVLGLCSV ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF ATAVAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIILFFVYY THPASCSENK AFISVNMLLC
IGASVMSILP KIQESQPRSG LLQSSVITIY TMYLTWSAMT NEPETNCNPS LLSIIGFNTT
RPVPKDGQSV QWWHPQGIIG LVLFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGNGR
SDGSLDDGEG VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
