SERC3_PONAB
ID SERC3_PONAB Reviewed; 473 AA.
AC Q5R533;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Serine incorporator 3;
GN Name=SERINC3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861044; CAH93133.1; -; mRNA.
DR RefSeq; NP_001128733.1; NM_001135261.1.
DR AlphaFoldDB; Q5R533; -.
DR SMR; Q5R533; -.
DR STRING; 9601.ENSPPYP00000012323; -.
DR Ensembl; ENSPPYT00000012805; ENSPPYP00000012323; ENSPPYG00000011035.
DR GeneID; 100173651; -.
DR KEGG; pon:100173651; -.
DR CTD; 10955; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; Q5R533; -.
DR OMA; GNPRVWY; -.
DR OrthoDB; 1276632at2759; -.
DR TreeFam; TF312881; -.
DR Proteomes; UP000001595; Chromosome 20.
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: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..473
FT /note="Serine incorporator 3"
FT /id="PRO_0000342159"
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..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..473
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"
SQ SEQUENCE 473 AA; 52550 MW; 66919A8FCAC3333F CRC64;
MGAVLGVFSL ASWVPCLCSG ASCLLCSCCP NSKNSTVTRL IYAFILLLST VVSYIMQRKE
METYLKKIPG FCEGGFKIHE ADINADKDCD VLVGYKAVYR ISFAMAIFFF VFSLLMFKVK
TSKDPRAAVH NGFWFFKIAA LIGIMVGSFY IPGGYFSSVW FVVGMIGAAL FILIQLVLLV
DFAHSWNESW VNRMEEGNPR LWYAALLSFT SAFYILSIIC VGLLYTYYTK PDGCTENKFF
ISINLILCVV ASIISIHPKI QEHQPRSGLL QSSVITLYTM YLTWSAMSNE PDRSCNPNLM
SFITRITAPT LAPGNSTAVV PTPTPPSKSG SLLDSDNFIG LFVFVLCLLY SSIRTSTNSQ
VDKLTLSGSD SVILGDTTTS GASDEEDGQP RRAVDNEKEG VQYSYSLFHL MLCLASLYIM
MTLTSWYSPD AKFQSMTSKW PAVWVKISSS WVCLLLYVWT LVAPLVLTSR DFS
