SERC5_DANRE
ID SERC5_DANRE Reviewed; 460 AA.
AC Q803X0; B2GT27; G1K2T1; Q6IQA9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine incorporator 5;
GN Name=serinc5; ORFNames=zgc:55396 {ECO:0000303|Ref.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q63175, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71500.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL935198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU984575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044159; AAH44159.1; -; mRNA.
DR EMBL; BC071500; AAH71500.1; ALT_SEQ; mRNA.
DR EMBL; BC165736; AAI65736.1; -; mRNA.
DR RefSeq; NP_998679.1; NM_213514.1.
DR AlphaFoldDB; Q803X0; -.
DR SMR; Q803X0; -.
DR STRING; 7955.ENSDARP00000087966; -.
DR PaxDb; Q803X0; -.
DR PRIDE; Q803X0; -.
DR Ensembl; ENSDART00000097194; ENSDARP00000087966; ENSDARG00000008153.
DR GeneID; 406835; -.
DR KEGG; dre:406835; -.
DR CTD; 256987; -.
DR ZFIN; ZDB-GENE-040426-2918; serinc5.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_2_1; -.
DR InParanoid; Q803X0; -.
DR OMA; ASCWVCV; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q803X0; -.
DR TreeFam; TF312881; -.
DR Reactome; R-DRE-977347; Serine biosynthesis.
DR PRO; PR:Q803X0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000008153; Expressed in tail bud paraxial mesoderm and 44 other tissues.
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; 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; IEA:InterPro.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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..460
FT /note="Serine incorporator 5"
FT /id="PRO_0000330634"
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..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 188
FT /note="A -> V (in Ref. 2; AAH71500)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> V (in Ref. 2; AAH71500)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="I -> T (in Ref. 2; AAH71500)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51983 MW; EF2F22629EEC0C1C CRC64;
MCTPCCVSQL ACCCGSAACS LCCGCCPKIK QSTSTRFMYA LFFMLVTVTC VIMMSPTVEM
AMREHIPFYS QMCQQLNAGE NCSTLVGYSA VYKVCFGMAC FFFFFAVFTI RVQNSTGCRA
AVHNGFWFFK FVALLACCAG GFFLPNQDQF LEVWRYVGAA GGFLFIIIQL MLLVQFAHRW
NQNWSSGATY NKLWYAALAL VTLVLFSVAV GGMVFMFMYY THPEACFLNK IFLGVNGGLC
FIVSLLAISP CIQTFQPTSG LLQPAVITLY VMYLTFSALA SKPIEMVEDE IKGNITVCVF
PFKSGLKSDT NIVTGVGTAI LFCCILYSCL ISTTKRSSAA LQVYRNDMPE NERARCCFCW
VDDTEDYDDE KTSGGQNVKY DERDGTVYSY CFFHFVFFLG SLYVMMTVTN WFHYDNAKIE
RLLEGSWSVF WIKMASSWVC LFFYMWTLVV PMLFPQRFQA
