SERC3_MOUSE
ID SERC3_MOUSE Reviewed; 472 AA.
AC Q9QZI9; Q3U7C6; Q62310; Q8BSP9; Q8CFD3; Q91VN9;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine incorporator 3;
DE AltName: Full=Axotomy-induced glyco/Golgi protein 1 {ECO:0000303|PubMed:12486168};
DE Short=AIGP-1 {ECO:0000303|PubMed:12486168};
DE AltName: Full=Axotomy-induced glycoprotein 1 {ECO:0000303|PubMed:12486168};
DE AltName: Full=Membrane protein TMS-1;
DE AltName: Full=Tumor differentially expressed protein 1;
GN Name=Serinc3;
GN Synonyms=Aigp1 {ECO:0000303|PubMed:12486168}, Diff33, Tde1, Tms1;
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], AND TISSUE SPECIFICITY.
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 [MRNA], GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Hypoglossal nucleus;
RX PubMed=12486168; DOI=10.1523/jneurosci.22-24-10751.2002;
RA Aoki S., Su Q., Li H., Nishikawa K., Ayukawa K., Hara Y., Namikawa K.,
RA Kiryu-Seo S., Kiyama H., Wada K.;
RT "Identification of an axotomy-induced glycosylated protein, AIGP1, possibly
RT involved in cell death triggered by endoplasmic reticulum-Golgi stress.";
RL J. Neurosci. 22:10751-10760(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Cerebellum, Forelimb, and Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-472.
RC TISSUE=Testis;
RX PubMed=7894057; DOI=10.3109/10425179409039702;
RA Lebel M., Mes-Masson A.-M.;
RT "Sequence analysis of a novel cDNA which is overexpressed in testicular
RT tumors from polyomavirus large T-antigen transgenic mice.";
RL DNA Seq. 5:31-39(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Pancreas, Spleen, 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: Restriction factor required to restrict infectivity of
CC gammaretroviruses: acts by inhibiting early step of viral infection and
CC impairing the ability of the viral particle to translocate its content
CC to the cytoplasm. {ECO:0000250|UniProtKB:Q13530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12486168};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12486168}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:12486168}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:12486168}. Note=Localizes to the cell
CC membrane, where it is efficiently incorporated into budding
CC gammaretrovirus virions and impairs subsequent virion penetration of
CC susceptible target cells (By similarity).
CC {ECO:0000250|UniProtKB:Q86VE9}.
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. Highly expressed also in
CC thymus, kidney liver and testis. {ECO:0000269|PubMed:10637174}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12486168}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF181684; AAD54420.1; -; mRNA.
DR EMBL; AB029499; BAC44828.1; -; mRNA.
DR EMBL; AB078029; BAC05511.1; -; Genomic_DNA.
DR EMBL; AK031101; BAC27253.1; -; mRNA.
DR EMBL; AK150106; BAE29313.1; -; mRNA.
DR EMBL; AK152720; BAE31443.1; -; mRNA.
DR EMBL; AK155921; BAE33504.1; -; mRNA.
DR EMBL; AK159347; BAE35009.1; -; mRNA.
DR EMBL; AK159819; BAE35399.1; -; mRNA.
DR EMBL; AK160005; BAE35553.1; -; mRNA.
DR EMBL; AK160055; BAE35593.1; -; mRNA.
DR EMBL; AK161981; BAE36664.1; -; mRNA.
DR EMBL; AK164807; BAE37929.1; -; mRNA.
DR EMBL; AK166924; BAE39119.1; -; mRNA.
DR EMBL; AK170350; BAE41738.1; -; mRNA.
DR EMBL; BC011295; AAH11295.1; -; mRNA.
DR EMBL; BC022901; AAH22901.1; -; mRNA.
DR EMBL; BC029026; AAH29026.1; -; mRNA.
DR EMBL; L29441; AAA74236.1; ALT_INIT; mRNA.
DR CCDS; CCDS17013.1; -.
DR PIR; I53063; I53063.
DR RefSeq; NP_036162.3; NM_012032.4.
DR AlphaFoldDB; Q9QZI9; -.
DR SMR; Q9QZI9; -.
DR STRING; 10090.ENSMUSP00000017851; -.
DR GlyGen; Q9QZI9; 1 site.
DR iPTMnet; Q9QZI9; -.
DR PhosphoSitePlus; Q9QZI9; -.
DR SwissPalm; Q9QZI9; -.
DR EPD; Q9QZI9; -.
DR jPOST; Q9QZI9; -.
DR MaxQB; Q9QZI9; -.
DR PaxDb; Q9QZI9; -.
DR PRIDE; Q9QZI9; -.
DR ProteomicsDB; 256966; -.
DR Antibodypedia; 43693; 191 antibodies from 27 providers.
DR DNASU; 26943; -.
DR Ensembl; ENSMUST00000017851; ENSMUSP00000017851; ENSMUSG00000017707.
DR GeneID; 26943; -.
DR KEGG; mmu:26943; -.
DR UCSC; uc008ntg.2; mouse.
DR CTD; 10955; -.
DR MGI; MGI:1349457; Serinc3.
DR VEuPathDB; HostDB:ENSMUSG00000017707; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; Q9QZI9; -.
DR OMA; GNPRVWY; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q9QZI9; -.
DR TreeFam; TF312881; -.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR BioGRID-ORCS; 26943; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Serinc3; mouse.
DR PRO; PR:Q9QZI9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QZI9; protein.
DR Bgee; ENSMUSG00000017707; Expressed in lobe of prostate and 272 other tissues.
DR Genevisible; Q9QZI9; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0009597; P:detection of virus; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IEA:InterPro.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:MGI.
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:SF51; PTHR10383:SF51; 1.
DR Pfam; PF03348; Serinc; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Cell membrane; Glycoprotein; Golgi apparatus; Immunity;
KW Innate immunity; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..472
FT /note="Serine incorporator 3"
FT /id="PRO_0000218971"
FT TOPO_DOM 1..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 6
FT /note="G -> A (in Ref. 1; AAD54420)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> I (in Ref. 4; BAC27253)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> F (in Ref. 5; AAH11295/AAH22901/AAH29026)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="A -> R (in Ref. 1 and 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="S -> N (in Ref. 5; AAH11295/AAH22901/AAH29026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52623 MW; F0EE1DA4BECE8CF0 CRC64;
MGAVLGVFSL ASWVPCLCSG ASCLLCSCCP ISKNSTVTRL IYAFILFLGT IVSCIMMTEG
IQTQLKKIPG FCEGGFQIKM VDTKAEKDCD VLVGFKAVYR INFAVAIFFF AFFLLMLKVK
TSKDPRAAVH NGFWFFKIAA IIGIMIGSFY IPGGSFTEVW FVAGMLGASF FIIIQLVLLV
DMAHSWNELW VNRMEEGNPR LWYAALLSFT SLFYILSIVF AALLYVFYTK PDDCTENKVF
ISLNLIFCVA VSIVSILPKV QEHQPRSGLL QSSIITLYTL YLTWSAMTNE PERSCNPSLM
SIITHLTSPT VSPANSTTLA PAYAPPSQSG HFMNLDDIWG LIIFVFCLIY SSFRTSSNSQ
VNKLTLSGSD SVILGDTTNG ANDEEDGQPR RAVDNEKEGV QYSYSFFHLM LCCASLYIMM
TITSWYSPDA KFQKVSSKWL AVWFKMGSSW LCLLLYLWTL VAPLVLTGRD FS
