CD2H_ASFM2
ID CD2H_ASFM2 Reviewed; 375 AA.
AC P0C9V9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=Mal-066;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
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.
RN [2]
RP FUNCTION.
RX PubMed=9525608; DOI=10.1128/jvi.72.4.2881-2889.1998;
RA Borca M.V., Carrillo C., Zsak L., Laegreid W.W., Kutish G.F., Neilan J.G.,
RA Burrage T.G., Rock D.L.;
RT "Deletion of a CD2-like gene, 8-DR, from African swine fever virus affects
RT viral infection in domestic swine.";
RL J. Virol. 72:2881-2889(1998).
RN [3]
RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=21248037; DOI=10.1128/jvi.01994-10;
RA Goatley L.C., Dixon L.K.;
RT "Processing and localization of the african swine fever virus CD2v
RT transmembrane protein.";
RL J. Virol. 85:3294-3305(2011).
CC -!- FUNCTION: May play an immunosuppressive role by inhibiting lymphocyte
CC proliferation and subsequently facilitating viral replication and
CC generalization of infection (PubMed:9525608). 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, ECO:0000269|PubMed:9525608}.
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:0000269|PubMed:21248037};
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 (PubMed:21248037). 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:Q89501,
CC ECO:0000269|PubMed:21248037}.
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 (PubMed:21248037). A full-length 89-kDa glycosylated form also
CC exists (PubMed:21248037). {ECO:0000269|PubMed:21248037}.
CC -!- SIMILARITY: Belongs to the asfivirus CD2 homolog protein family.
CC {ECO:0000305}.
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DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000000860; 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 1: Evidence at protein level;
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..375
FT /note="CD2 homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000373362"
FT TOPO_DOM 17..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..375
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 REGION 242..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..334
FT /note="5 X 6 AA tandem repeats of K-[LP]-C-[PRS]-[PS]-[PS]"
FT REGION 323..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..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 80
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
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 134
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
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 DISULFID 123..190
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT DISULFID 130..173
FT /evidence="ECO:0000250|UniProtKB:P06729"
SQ SEQUENCE 375 AA; 42396 MW; 56C12288C9DF76E6 CRC64;
MIIILIFLII PNIVLSIDYW VSFNKTIILD SNITNDNNDI NGVSWNFLNN SLNTLATCGK
AGNFCECSNY STSLYNIAHN CSLTIFPHND VFGTPYQVVW NQIINYTIKL LTPVTPPNIT
YNCTNFLITC KKNNGTNTII YFNINDTNVK YTNESILEYN WNNSNFNNFT ATCIINNTIN
SSNDTQTIDC INTLLSSYLD FFQVASYMFY MIIFIATGII ASIFISIITF LSLRKRKKHV
EEIESPSPSE SNEEEQCQHD DTTSIHEPSP REPLLPKPYS RYQYNTPIYY MRPLTQPLNP
SPLPKLCPPP KPCPPPKPCP PPKPCPPPKP CPSSESCSPP ESYSLPKPLP NIPLLPNIPP
LSTQNISLIH VDRII
