SERINC5
entrez
256987
canonical
uniprot
Q86VE9
canonical
ensembl
ENSG00000164300
resolver
ensp
ENSP00000426134
resolver
ensp
ENSP00000426237
resolver
ensp
ENSP00000673538
resolver
genesymbol
SERINC5
resolver
genesymbol_syn
C5orf12
resolver
hgnc
HGNC:18825
resolver
uniprot
B4DMH7
resolver
uniprot
Q495A4
resolver
uniprot
Q495A6
resolver
uniprot_entry
SERC5_HUMAN
resolver
uniprot_sec
B4DMH7
resolver
uniprot_sec
Q495A4
resolver
uniprot_sec
Q495A6
resolver
amino_acid_sequence
MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAHKMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRAHIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKWNKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLCLLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVPDFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFSPGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFHLLP
uniprot
proteins
function
FUNCTION: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm (PubMed:26416733, PubMed:26416734). Non-ATP-dependent, non-specific lipid transporter for phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine. Functions as a scramblase that flips lipids in both directions across the membrane. Phospholipid scrambling results in HIV-1 surface exposure of phosphatidylserine and loss of membrane asymmetry, which leads to changes in HIV-1 Env conformation and loss of infectivity (PubMed:37474505). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:Q63175, ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734, ECO:0000269|PubMed:37474505}.
uniprot
proteins
mass_dalton
47009
uniprot
proteins
mutagenesis
MUTAGEN 328; /note="S->I: No effect on scrambalase activity. Impaired antiviral activity."; /evidence="ECO:0000269|PubMed:37474505"; MUTAGEN 397; /note="F->L: No effect on scrambalase activity. Impaired antiviral activity."; /evidence="ECO:0000269|PubMed:37474505
uniprot
proteins
protein_family
TDE1 family
uniprot
proteins
pubmed
12688535
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
26416733
uniprot
proteins
pubmed
26416734
uniprot
proteins
pubmed
37474505
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26416733, ECO:0000269|PubMed:26416734}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (PubMed:26416733, PubMed:26416734). Localizes to the cell membrane, where it is efficiently incorporated into budding virions and impairs subsequent virion entry into target cells (PubMed:26416733, PubMed:26416734). {ECO:0000269|PubMed:26416734, ECO:0000305|PubMed:26416733}.
uniprot
proteins
transmembrane_region
TRANSMEM 37..57; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 90..110; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 125..145; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 157..177; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 199..219; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 231..251; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 259..279; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 312..332; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 386..406; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins