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   27-MAR-2024, entry version 166.
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
RC   ganglion, 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}.
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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; 10090-ENSMUSP00000020027; -.
DR   ProteomicsDB; 261320; -.
DR   Pumba; Q9QZI8; -.
DR   Antibodypedia; 46589; 219 antibodies from 25 providers.
DR   DNASU; 56442; -.
DR   Ensembl; ENSMUST00000020027.11; ENSMUSP00000020027.5; ENSMUSG00000019877.11.
DR   GeneID; 56442; -.
DR   KEGG; mmu:56442; -.
DR   UCSC; uc007fcm.3; mouse.
DR   AGR; MGI:1926228; -.
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; DKHCNPL; -.
DR   OrthoDB; 53161at2759; -.
DR   PhylomeDB; Q9QZI8; -.
DR   TreeFam; TF312881; -.
DR   Reactome; R-MMU-977347; Serine biosynthesis.
DR   BioGRID-ORCS; 56442; 3 hits in 82 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 268 other cell types or tissues.
DR   ExpressionAtlas; Q9QZI8; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC-UCL.
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; IPR005016; TDE1/TMS.
DR   PANTHER; PTHR10383; SERINE INCORPORATOR; 1.
DR   PANTHER; PTHR10383:SF15; SERINE INCORPORATOR 1; 1.
DR   Pfam; PF03348; Serinc; 1.
DR   Genevisible; Q9QZI8; MM.
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
//