CD2H_ASFK5
ID CD2H_ASFK5 Reviewed; 392 AA.
AC P0C9V7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=CD2 homolog;
DE Short=CD2H;
DE AltName: Full=5HL;
DE AltName: Full=CD2v;
DE AltName: Full=T-lymphocyte CD2 receptor-like protein;
DE AltName: Full=pEP402R {ECO:0000250|UniProtKB:Q89501};
DE Flags: Precursor;
GN OrderedLocusNames=Ken-070;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play an immunosuppressive role by inhibiting lymphocyte
CC proliferation and subsequently facilitating viral replication and
CC generalization of infection (By similarity). Responsible for viral
CC hemadsorption, which may help viral spread (By similarity). Increases
CC virus replication in the tick vector at the step of virus uptake or
CC replication in the tick gut (By similarity). May play a role in the
CC host Golgi reorganization to yield viral factories (By similarity). May
CC play a role in host cell penetration (By similarity).
CC {ECO:0000250|UniProtKB:Q89501}.
CC -!- SUBUNIT: Both glycosylated and nonglycosylated forms interact (via C-
CC terminus) with the host AP-1 complex. {ECO:0000250|UniProtKB:Q89501}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane
CC {ECO:0000250|UniProtKB:Q89501}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q89501}. Virion membrane
CC {ECO:0000250|UniProtKB:Q89501}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:Q89501}. Note=Localizes around the cytoplasmic
CC viral factories which are probably derived from the host Golgi membrane
CC (By similarity). Both proteolytic fragments localize to membrane
CC compartments (By similarity). A minor fraction localizes on the host
CC plasma membrane and on the outer viral envelope of budding particles
CC (By similarity). {ECO:0000250|UniProtKB:P0C9V9,
CC ECO:0000250|UniProtKB:Q89501}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- PTM: Cleaved into two fragments of 63 kDa and 26 kDa containing
CC respectively the glycosylated N-terminus and the nonglycosylated C-
CC terminus (By similarity). A full-length 89-kDa glycosylated form also
CC exists (By similarity). {ECO:0000250|UniProtKB:P0C9V9}.
CC -!- SIMILARITY: Belongs to the asfivirus CD2 homolog protein family.
CC {ECO:0000305}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9V7; -.
DR Proteomes; UP000000861; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host Golgi apparatus;
KW Host membrane; Late protein; Membrane; Receptor; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Virion.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..392
FT /note="CD2 homolog"
FT /id="PRO_0000373360"
FT TOPO_DOM 17..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 319..324
FT /note="1"
FT REPEAT 325..330
FT /note="2"
FT REPEAT 331..336
FT /note="3"
FT REPEAT 337..342
FT /note="4"
FT REPEAT 343..348
FT /note="5"
FT REGION 258..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="5 X 6 AA tandem repeats of K-P-C-[PRS]-[P]-[PS]"
FT REGION 328..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 137..205
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT DISULFID 144..188
FT /evidence="ECO:0000250|UniProtKB:P06729"
SQ SEQUENCE 392 AA; 44586 MW; A0695B4E4E67BA72 CRC64;
MIIKLIFLIC FKIVLSIDNK TKFNETLILD NIDYWVKFND TITLDSNITS EIEAVSWNFY
NNTFNLLAIC GKASNFCSCS NYSTSFFNIT NNCSLTIFLI DETLFNTTYQ IVYSTNIINY
KINLLIPVTP PIISYNCANC SINCKKSNGT NTNIFLSIND TIVTYTNESI LNYDYNCSIL
NNNFTVTCII NNTISTSNTT EFINCTNILL SSYLDFFQVT SYIFYMIIFI VTGITVSILI
SIITFLFIRK RKHVEEIESP PPESNEEEQQ CHHDTTSIHE PSPREPLLPK PYSRYQYNTP
IYYMRPSTQQ LFKSYSLPKP CPPPKPCPPP KPCPPPKPCP PSKPCPPPEP YSPPKPCPPP
KPYPSLPSIP LPPDIPPLST QNISLIHVDR II
