SERC1_MOUSE
ID SERC1_MOUSE Reviewed; 453 AA.
AC Q9QZI8; Q3UZ93;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Axotomy-induced glyco/Golgi protein 2;
DE AltName: Full=Membrane protein TMS-2;
DE AltName: Full=Tumor differentially expressed protein 1-like;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=Serinc1; Synonyms=Aigp2, Tde1l, Tde2, Tms2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10637174; DOI=10.1242/jeb.203.3.447;
RA Grossman T.R., Luque J.M., Nelson N.;
RT "Identification of a ubiquitous family of membrane proteins and their
RT expression in mouse brain.";
RL J. Exp. Biol. 203:447-457(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li H., Aoki S., Hara Y., Wada K.;
RT "An axotomy activated gene, mouse AIGP1: genomic organization,
RT transcriptional regulation and genetic mapping on chromosome 2.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Hippocampus, Kidney, Pituitary, Sympathetic ganglion,
RC and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Highly expressed in the neuronal populations such
CC as Purkinje cells in the cerebellum, brainstem and spinal motor
CC neurons, locus coeruleus and raphe nuclei.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF181685; AAD54421.1; -; mRNA.
DR EMBL; AB078030; BAC05512.1; -; Genomic_DNA.
DR EMBL; AK002847; BAB22403.1; -; mRNA.
DR EMBL; AK005203; BAB23881.1; -; mRNA.
DR EMBL; AK088340; BAC40293.1; -; mRNA.
DR EMBL; AK133668; BAE21775.1; -; mRNA.
DR EMBL; AK133975; BAE21964.1; -; mRNA.
DR EMBL; AK135359; BAE22504.1; -; mRNA.
DR EMBL; AK141574; BAE24743.1; -; mRNA.
DR EMBL; AK148745; BAE28654.1; -; mRNA.
DR EMBL; AK159280; BAE34958.1; -; mRNA.
DR EMBL; AK159436; BAE35082.1; -; mRNA.
DR EMBL; BC017148; AAH17148.1; -; mRNA.
DR CCDS; CCDS23853.1; -.
DR RefSeq; NP_062734.1; NM_019760.3.
DR AlphaFoldDB; Q9QZI8; -.
DR SMR; Q9QZI8; -.
DR BioGRID; 207983; 1.
DR STRING; 10090.ENSMUSP00000020027; -.
DR iPTMnet; Q9QZI8; -.
DR PhosphoSitePlus; Q9QZI8; -.
DR SwissPalm; Q9QZI8; -.
DR EPD; Q9QZI8; -.
DR jPOST; Q9QZI8; -.
DR MaxQB; Q9QZI8; -.
DR PaxDb; Q9QZI8; -.
DR PRIDE; Q9QZI8; -.
DR ProteomicsDB; 261320; -.
DR Antibodypedia; 46589; 185 antibodies from 25 providers.
DR DNASU; 56442; -.
DR Ensembl; ENSMUST00000020027; ENSMUSP00000020027; ENSMUSG00000019877.
DR GeneID; 56442; -.
DR KEGG; mmu:56442; -.
DR UCSC; uc007fcm.3; mouse.
DR CTD; 57515; -.
DR MGI; MGI:1926228; Serinc1.
DR VEuPathDB; HostDB:ENSMUSG00000019877; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; Q9QZI8; -.
DR OMA; MEPDDKQ; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q9QZI8; -.
DR TreeFam; TF312881; -.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR BioGRID-ORCS; 56442; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Serinc1; mouse.
DR PRO; PR:Q9QZI8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QZI8; protein.
DR Bgee; ENSMUSG00000019877; Expressed in cerebellum lobe and 265 other tissues.
DR ExpressionAtlas; Q9QZI8; baseline and differential.
DR Genevisible; Q9QZI8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS: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:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0044091; P:membrane biogenesis; ISS:BHF-UCL.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS: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; ISS:HGNC.
DR GO; GO:1904222; P:positive regulation of serine C-palmitoyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS: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_0000218967"
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:19144319"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
SQ SEQUENCE 453 AA; 50509 MW; 0FE8718FA3EA62B7 CRC64;
MGSVLGLCSV ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF ATAVAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAVVLFFVYY THPASCAENK AFISVNMLLC
IGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGFNTT
RPIPKDGQSV QWWHPQGIIG LVLFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGNGR
SDGSLDDGDG IHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGLVLYVWT LVAPLVLTNR DFD
