CD2H_ASFP4
ID CD2H_ASFP4 Reviewed; 404 AA.
AC P0C9V8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
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 Short=CD2-like protein;
DE AltName: Full=pEP402R {ECO:0000250|UniProtKB:Q89501};
DE Flags: Precursor;
GN OrderedLocusNames=Pret-070;
OS African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561443;
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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9V8; -.
DR Proteomes; UP000000859; 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..404
FT /note="CD2 homolog"
FT /id="PRO_0000373361"
FT TOPO_DOM 17..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 322..327
FT /note="1"
FT REPEAT 328..333
FT /note="2"
FT REPEAT 334..339
FT /note="3"
FT REPEAT 340..345
FT /note="4"
FT REPEAT 346..351
FT /note="5"
FT REPEAT 352..357
FT /note="6"
FT REPEAT 358..363
FT /note="7"
FT REGION 260..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..363
FT /note="7 X 6 AA tandem repeats of [KN]-P-C-P-P-P"
FT REGION 357..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Pro 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 87
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 96
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 140..207
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT DISULFID 147..190
FT /evidence="ECO:0000250|UniProtKB:P06729"
SQ SEQUENCE 404 AA; 45995 MW; A5D90FB27B68CD8D CRC64;
MFITLIFLSY INIVLSNNYW ARLNETITLN SNITNDTNNE LGIFWNSYNN TYYNNTFNNI
AICGKKGIFC ECNINYNTSI SNTSISNTSI YNVTNNCSLT IFLYDDNIFK TYQLVYQNYK
INYTINLLLP VTSPNITYNC TNSLITCEKN DGTNTNMFLS INNITINHTN QDILTYYWNN
SEFNNFTATC MINNTLNSAN TTKVINCTNP LLNSYQNYFL ENIHTLFYII IFIVSGLIAS
IFISIITFLS LRKRKKHVEE IESPPPESNE EEQCQHDDTT SIHEPSPREP LLPKPYSRYQ
YNTPIYYMRP STQPLNPFPL PNPCPPPKPC PPPKPCPPPK PCPPPKPCPP PKPCPPPKPC
PPPKPCSSPE SYSPPKPLPS IPLLPNIPPL STQNISLIHV DRII
