CD2H_ASFB7
ID CD2H_ASFB7 Reviewed; 402 AA.
AC Q89501;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
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:0000303|PubMed:30185597};
DE Flags: Precursor;
GN OrderedLocusNames=Ba71V-058; ORFNames=EP402R;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP FUNCTION.
RX PubMed=8102411; DOI=10.1128/jvi.67.9.5312-5320.1993;
RA Rodriguez J.M., Yanez R.J., Almazan F., Vinuela E., Rodriguez J.F.;
RT "African swine fever virus encodes a CD2 homolog responsible for the
RT adhesion of erythrocytes to infected cells.";
RL J. Virol. 67:5312-5320(1993).
RN [3]
RP FUNCTION.
RX PubMed=8615037; DOI=10.1006/viro.1996.0193;
RA Ruiz-Gonzalvo F., Rodriguez F., Escribano J.M.;
RT "Functional and immunological properties of the baculovirus-expressed
RT hemagglutinin of African swine fever virus.";
RL Virology 218:285-289(1996).
RN [4]
RP FUNCTION.
RC STRAIN=Isolate NH/P68;
RX PubMed=19729182; DOI=10.1016/j.virol.2009.07.040;
RA Rowlands R.J., Duarte M.M., Boinas F., Hutchings G., Dixon L.K.;
RT "The CD2v protein enhances African swine fever virus replication in the
RT tick vector, Ornithodoros erraticus.";
RL Virology 393:319-328(2009).
RN [5]
RP INTERACTION WITH THE HOST AP-1 COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=Ba71V, and Isolate NH/P68;
RX PubMed=25915900; DOI=10.1371/journal.pone.0123714;
RA Perez-Nunez D., Garcia-Urdiales E., Martinez-Bonet M., Nogal M.L.,
RA Barroso S., Revilla Y., Madrid R.;
RT "CD2v interacts with adaptor protein AP-1 during African swine fever
RT infection.";
RL PLoS ONE 10:E0123714-E0123714(2015).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=28814514; DOI=10.1128/jvi.01058-17;
RA Monteagudo P.L., Lacasta A., Lopez E., Bosch L., Collado J.,
RA Pina-Pedrero S., Correa-Fiz F., Accensi F., Navas M.J., Vidal E.,
RA Bustos M.J., Rodriguez J.M., Gallei A., Nikolin V., Salas M.L.,
RA Rodriguez F.;
RT "BA71DeltaCD2: a New Recombinant Live Attenuated African Swine Fever Virus
RT with Cross-Protective Capabilities.";
RL J. Virol. 91:0-0(2017).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [8]
RP INDUCTION, AND ALTERNATIVE INITIATION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=34006158; DOI=10.1080/10717544.2021.1909178;
RA Yang S., Zhang X., Cao Y., Li S., Shao J., Sun S., Guo H., Yin S.;
RT "Identification of a new cell-penetrating peptide derived from the african
RT swine fever virus CD2v protein.";
RL Drug Deliv. 28:957-962(2021).
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 (PubMed:8102411,
CC PubMed:8615037). Increases virus replication in the tick vector at the
CC step of virus uptake or replication in the tick gut (PubMed:19729182).
CC May play a role in the host Golgi reorganization to yield viral
CC factories (PubMed:25915900). May play a role in host cell penetration
CC (PubMed:34006158). {ECO:0000250|UniProtKB:P0C9V9,
CC ECO:0000269|PubMed:19729182, ECO:0000269|PubMed:25915900,
CC ECO:0000269|PubMed:34006158, ECO:0000269|PubMed:8102411,
CC ECO:0000269|PubMed:8615037}.
CC -!- SUBUNIT: Both glycosylated and nonglycosylated forms interact (via C-
CC terminus) with the host AP-1 complex. {ECO:0000269|PubMed:25915900}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000269|PubMed:30185597};
CC Single-pass type I membrane protein {ECO:0000305}. Virion membrane
CC {ECO:0000305|PubMed:30185597}. Host Golgi apparatus
CC {ECO:0000269|PubMed:30185597}. Note=Localizes mainly around the
CC perinuclear cytoplasmic viral factories which are probably derived from
CC the host Golgi membrane (PubMed:25915900). Both proteolytic fragments
CC localize to membrane compartements (By similarity). A minor fraction
CC localizes on the host plasma membrane and on the outer viral envelope
CC of budding particles (Probable). {ECO:0000250|UniProtKB:P0C9V9,
CC ECO:0000269|PubMed:25915900, ECO:0000305|PubMed:30185597}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q89501-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q89501-2; Sequence=VSP_061340;
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- DOMAIN: The C-terminus contains repetitive amino-acids that may
CC function as a cell-penetrating peptide. {ECO:0000269|PubMed:34006158}.
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 -!- DISRUPTION PHENOTYPE: Highly attenuates the virulence in vivo.
CC {ECO:0000269|PubMed:28814514}.
CC -!- SIMILARITY: Belongs to the asfivirus CD2 homolog protein family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65288.1; -; Genomic_DNA.
DR PIR; A40678; A40678.
DR RefSeq; NP_042752.1; NC_001659.2.
DR SMR; Q89501; -.
DR DNASU; 1488823; -.
DR GeneID; 22220440; -.
DR KEGG; vg:22220440; -.
DR Proteomes; UP000000624; 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:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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 Alternative initiation; Disulfide bond; Glycoprotein; Host cell membrane;
KW Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus; Late protein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..402
FT /note="CD2 homolog"
FT /id="PRO_0000379092"
FT TOPO_DOM 17..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 302..307
FT /note="1"
FT REPEAT 308..313
FT /note="2"
FT REPEAT 314..319
FT /note="3"
FT REPEAT 320..325
FT /note="4"
FT REPEAT 326..331
FT /note="5"
FT REPEAT 332..337
FT /note="6"
FT REPEAT 338..343
FT /note="7"
FT REPEAT 344..349
FT /note="8"
FT REPEAT 350..355
FT /note="9"
FT REPEAT 356..361
FT /note="10"
FT REPEAT 362..367
FT /note="11"
FT REGION 238..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..367
FT /note="11 X 6 AA tandem repeats of K-P-C-[PRS]-[P]-[PS]"
FT REGION 319..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
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 81
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
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 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 126..191
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT DISULFID 133..174
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:32075923"
FT /id="VSP_061340"
SQ SEQUENCE 402 AA; 45325 MW; B8C18BE6C5C6BE04 CRC64;
MIIIVIFLMC LKIVLNNIII WSTLNQTVFL NNIFTINDTY GGLFWNTYYD NNRSNFTYCG
IAGNYCSCCG HNISLYNTTN NCSLIIFPNN TEIFNRTYEL VYLDKKINYT VKLLKSVDSP
TITYNCTNSL ITCKNNNGTN VNIYLIINNT IVNDTNGDIL NYYWNGNNNF TATCMINNTI
SSLNETENIN CTNPILKYQN YLSTLFYIII FIVSGLIIGI FISIISVLSI RRKRKKHVEE
IESPPPSESN EEDISHDDTT SIHEPSPREP LLPKPYSRYQ YNTPIYYMRP STQPLNPFPL
PKPCPPPKPC PPPKPCPPPK PCPPPKPCSP PKPCRPPKPC PPPKPCPPPK PCPPPKPCPP
SKPCPSPESY SPPKPLPSIP LLPNIPPLST QNISLIHVDR II
