SERC5_MOUSE
ID SERC5_MOUSE Reviewed; 461 AA.
AC Q8BHJ6; Q80ZH8; Q8CHM0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine incorporator 5;
DE AltName: Full=Axotomy-induced glycoprotein 3 {ECO:0000303|PubMed:12486168};
DE Short=AIGP-3 {ECO:0000303|PubMed:12486168};
GN Name=Serinc5; Synonyms=Aigp3 {ECO:0000303|PubMed:12486168};
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].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Ovary, Spleen, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, and Olfactory epithelium;
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).
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 (By similarity). Enhances the incorporation of serine
CC into phosphatidylserine and sphingolipids. May play a role in providing
CC serine molecules for the formation of myelin glycosphingolipids in
CC oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175,
CC ECO:0000250|UniProtKB:Q86VE9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VE9};
CC Multi-pass membrane protein {ECO:0000255}. 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. {ECO:0000250|UniProtKB:Q86VE9}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; AB029501; BAC44829.1; -; mRNA.
DR EMBL; AK037699; BAC29851.1; -; mRNA.
DR EMBL; AK054475; BAC35794.1; -; mRNA.
DR EMBL; AK136799; BAE23132.1; -; mRNA.
DR EMBL; AK165334; BAE38139.1; -; mRNA.
DR EMBL; BC049189; AAH49189.2; -; mRNA.
DR EMBL; BC062131; AAH62131.1; -; mRNA.
DR CCDS; CCDS36744.1; -.
DR RefSeq; NP_766176.1; NM_172588.2.
DR AlphaFoldDB; Q8BHJ6; -.
DR SMR; Q8BHJ6; -.
DR STRING; 10090.ENSMUSP00000047547; -.
DR GlyGen; Q8BHJ6; 2 sites.
DR iPTMnet; Q8BHJ6; -.
DR PhosphoSitePlus; Q8BHJ6; -.
DR SwissPalm; Q8BHJ6; -.
DR EPD; Q8BHJ6; -.
DR PaxDb; Q8BHJ6; -.
DR PeptideAtlas; Q8BHJ6; -.
DR PRIDE; Q8BHJ6; -.
DR ProteomicsDB; 261321; -.
DR Antibodypedia; 49006; 22 antibodies from 8 providers.
DR DNASU; 218442; -.
DR Ensembl; ENSMUST00000049488; ENSMUSP00000047547; ENSMUSG00000021703.
DR GeneID; 218442; -.
DR KEGG; mmu:218442; -.
DR UCSC; uc007rkt.1; mouse.
DR CTD; 256987; -.
DR MGI; MGI:2444223; Serinc5.
DR VEuPathDB; HostDB:ENSMUSG00000021703; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_2_1; -.
DR InParanoid; Q8BHJ6; -.
DR OMA; ASCWVCV; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q8BHJ6; -.
DR TreeFam; TF312881; -.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR BioGRID-ORCS; 218442; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Serinc5; mouse.
DR PRO; PR:Q8BHJ6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BHJ6; protein.
DR Bgee; ENSMUSG00000021703; Expressed in humerus cartilage element and 242 other tissues.
DR Genevisible; Q8BHJ6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0042552; P:myelination; IDA:MGI.
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; IEA:InterPro.
DR InterPro; IPR029555; Serinc5.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF16; PTHR10383:SF16; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cell membrane; Glycoprotein; Immunity; Innate immunity;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..461
FT /note="Serine incorporator 5"
FT /id="PRO_0000330632"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 68
FT /note="F -> S (in Ref. 1; BAC44829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51831 MW; 13698C24FFEFEBD9 CRC64;
MSARCCAGQL ACCCGSAGCS LCCGCCPKFR QSRTTRFMYL FYFILVIALC CVMMTPSVMK
QVKDHIPFFE EFCKKTQAGG DACENLVGYS AVYRVCFGMA CFFALFCLLT LKVNNSKSCR
AYIHNGFWFF KLLLLGAMCS GAFFIPDQET FLKVWRYVGA GGSFLFICIQ LLLIVQFAHK
WNKNWTAGTV RNKLWYASLS LVTLIMYSVA VGGLALMAVF YTQWDDCMDN KILLGVHGGL
CVLISLVAIS PCVQNRQPHS GLLQSGLISC YVTYLTFSAL TSKPEKKVLD EHGKNVTICA
PDFGQDLHRD ENMVTWLGTL LLIVCISYSC LTSTTRSSSD ALQSRYGAPE LEVARCCFCF
GPDGEDTEEQ QNVKKGPRVI YDEKKGTVYS YSYFHFVFFL ASLYVMMTLT SWFHYENATI
KTFFSGWSVF WVKMASCWMC VLLYLQTLVA PLCCPSRQFS V
