SERC3_BOVIN
ID SERC3_BOVIN Reviewed; 472 AA.
AC A4FUZ5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Serine incorporator 3;
GN Name=SERINC3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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. {ECO:0000250|UniProtKB:Q13530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VE9};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9QZI9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9QZI9}. Note=Localizes to the cell membrane,
CC where it is efficiently incorporated into budding gammaretrovirus
CC virions and impairs subsequent virion penetration of susceptible target
CC cells (By similarity). {ECO:0000250|UniProtKB:Q86VE9}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9QZI9}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; BC123501; AAI23502.1; -; mRNA.
DR RefSeq; NP_001076881.1; NM_001083412.1.
DR AlphaFoldDB; A4FUZ5; -.
DR SMR; A4FUZ5; -.
DR STRING; 9913.ENSBTAP00000002833; -.
DR PaxDb; A4FUZ5; -.
DR PRIDE; A4FUZ5; -.
DR Ensembl; ENSBTAT00000002833; ENSBTAP00000002833; ENSBTAG00000002187.
DR GeneID; 511861; -.
DR KEGG; bta:511861; -.
DR CTD; 10955; -.
DR VEuPathDB; HostDB:ENSBTAG00000002187; -.
DR VGNC; VGNC:34462; SERINC3.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; A4FUZ5; -.
DR OMA; GNPRVWY; -.
DR OrthoDB; 1276632at2759; -.
DR TreeFam; TF312881; -.
DR Reactome; R-BTA-977347; Serine biosynthesis.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000002187; Expressed in spermatocyte and 105 other tissues.
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; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
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 2: Evidence at transcript 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_0000342158"
FT TOPO_DOM 1..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..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 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRX5"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 52418 MW; C32AF14F63A6EEA1 CRC64;
MGAVLGVFSL ASWVPCLCGG ASCLLCSCCP NSKNSTLTRL IYAFILFLGT IVCCIMFHEG
METQLKKIPG FCDEGLSTRI TDIMDKECDV LVRYKAVYRI SFALAVFFFA FSLLMLNVKT
SKDPRAAIHN GFWFFKIAAI VGVMVGSFYI PGGHFNTAWF VIGMVGAAFF ILIQLVLLVD
FAHSWNESWV NRMEEGNPKC WYAALLSVTS LFYILSIIFA GLLYTYYTKP DGCTENKFFI
SFNLILCVVI SVLSIHPKIQ EHQPRSGLLQ SSLITLYTMY LTWSAMSNEP DRSCNPGLLS
IITHMTSSTL APANTTAPAP TPAVPLQSGP SLNKENFIGL LVFVLSLSYS SIRNSSNSQV
SKLTLSGSDS VILRDTAANG ASDEEDGRPR RAVDNEREGV QYNYSMFHLM LCSASLYIMM
TLTNWYSPDA NFQSMTSKWP AVWVKISSSW VCLLLYVWTL VAPLVLTNRD FS
