CD86_RABIT
ID CD86_RABIT Reviewed; 330 AA.
AC P42071;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=T-lymphocyte activation antigen CD86;
DE AltName: Full=Activation B7-2 antigen;
DE AltName: CD_antigen=CD86;
DE Flags: Precursor;
GN Name=CD86;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B/J X Chbb:HM;
RX PubMed=7642234; DOI=10.1007/bf00191228;
RA Isono T., Seto A.;
RT "Cloning and sequencing of the rabbit gene encoding T-cell costimulatory
RT molecules.";
RL Immunogenetics 42:217-220(1995).
CC -!- FUNCTION: Receptor involved in the costimulatory signal essential for
CC T-lymphocyte proliferation and interleukin-2 production, by binding
CC CD28 or CTLA-4. May play a critical role in the early events of T-cell
CC activation and costimulation of naive T-cells, such as deciding between
CC immunity and anergy that is made by T-cells within 24 hours after
CC activation. Also involved in the regulation of B cells function, plays
CC a role in regulating the level of IgG(1) produced. Upon CD40
CC engagement, activates NF-kappa-B signaling pathway via phospholipase C
CC and protein kinase C activation (By similarity).
CC {ECO:0000250|UniProtKB:P42082}.
CC -!- SUBUNIT: Homodimer. Interacts with MARCH8 (By similarity). Interacts
CC (via cytoplasmic domain) with PHB1 and PHB2; the interactions increases
CC after priming with CD40 (By similarity). {ECO:0000250|UniProtKB:P42081,
CC ECO:0000250|UniProtKB:P42082}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Polyubiquitinated; which is promoted by MARCH8 and results in
CC endocytosis and lysosomal degradation. {ECO:0000250}.
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DR EMBL; D49842; BAA08642.1; -; mRNA.
DR PIR; I46691; I46691.
DR RefSeq; NP_001075677.1; NM_001082208.1.
DR AlphaFoldDB; P42071; -.
DR SMR; P42071; -.
DR STRING; 9986.ENSOCUP00000009930; -.
DR GeneID; 100008999; -.
DR KEGG; ocu:100008999; -.
DR CTD; 942; -.
DR eggNOG; ENOG502S1FF; Eukaryota.
DR InParanoid; P42071; -.
DR OrthoDB; 1051626at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR CDD; cd16087; IgV_CD86; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR037677; CD86_IgV.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..330
FT /note="T-lymphocyte activation antigen CD86"
FT /id="PRO_0000014552"
FT TOPO_DOM 23..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..127
FT /note="Ig-like V-type"
FT DOMAIN 150..225
FT /note="Ig-like C2-type"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 330 AA; 37143 MW; 935CDD65C57E3EE1 CRC64;
MDAGCTMGLS VTVFVMALLL SGAASLRIQA YFNKTADLPC QFTNSQSRSL SELVVFWQDQ
ERLVLYELFL GREKPDNVDP KYIGRTSFDQ ESWNLQLHNV QIKDKGVYQC FVHHRGAKGL
VPIYQMNSEL SVLANFTQPE ITLISNITRN SAINLTCSSV QGYPEPKKMF FVLKTENATT
EYDGVIEKSQ DNVTGLYNIS ISGSITFSDD IRNATIYCVL QTESTETYSQ HFPIVPADPV
PVEKPRLWIA AVALTLIVVC GIVLFLTLWK RKKEQQPGVC ECETIKMDKA ENEHVEERVK
IHEPEKIPAK AAKCEHRLKT PSSDKSAAHF
