CD2H_ASFWA
ID CD2H_ASFWA Reviewed; 381 AA.
AC P0C9V6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=War-068;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
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:P0C9V9, 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 membrane {ECO:0000250|UniProtKB:P0C9V9};
CC Single-pass type I membrane protein {ECO:0000305}. 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 compartements (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 -!- DOMAIN: The C-terminus contains repetitive amino-acids that may
CC function as a cell-penetrating peptide. {ECO:0000250|UniProtKB:Q89501}.
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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9V6; -.
DR Proteomes; UP000000858; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell 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 Golgi apparatus; Host membrane;
KW Late protein; Membrane; Receptor; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Virion.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..381
FT /note="CD2 homolog"
FT /id="PRO_0000373359"
FT TOPO_DOM 17..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 305..310
FT /note="1"
FT REPEAT 311..316
FT /note="2"
FT REPEAT 317..322
FT /note="3"
FT REPEAT 323..328
FT /note="4"
FT REPEAT 329..334
FT /note="5"
FT REPEAT 335..340
FT /note="6"
FT REPEAT 341..346
FT /note="7"
FT REGION 243..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..334
FT /note="7 X 6 AA tandem repeats of K-[LP]-C-[PRS]-[PS]-[PS]"
FT REGION 341..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
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 189
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 122..190
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT DISULFID 129..173
FT /evidence="ECO:0000250|UniProtKB:P06729"
SQ SEQUENCE 381 AA; 43624 MW; 7C932795A07DE7A2 CRC64;
MIIKLIFLIC FKIVLSINYW VRYNDTVTLN SNINSETEGI FWNFYNNTFN TIATCGKKNN
VCECSNYDKS LYNITNNCSL TIFPNNTKIF NTTYQLVYSR NRINYTINLL LPVTSPIITY
NCTQSLITCE KTNGTNIHLF LNLNDTINEY TNKSFLNYYW NSSELNNIFL ATCIINNTLN
SANTTKVINC TNPLLKSYQN YFLENIHTLF YMIIFIVSGI TISIFISIIT FLSLRKRKKH
VEEIESPPPE SNEEEQCQHD DTTSIHEPSP REPLLPKPYS RYQYNTPIYY MRPSTQPLNP
FPLPKPCPPP KPCPPPKPCP PPKPCPPPKP CPPPKPCPPP KPCPPPESYS PPKPLPSIPL
LPNIPPLSTQ NISLIHVDRI I
