BTLA_RAT
ID BTLA_RAT Reviewed; 308 AA.
AC Q6PNM1; Q569B2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=B- and T-lymphocyte attenuator {ECO:0000250|UniProtKB:Q7TSA3, ECO:0000250|UniProtKB:Q7Z6A9};
DE AltName: Full=B- and T-lymphocyte-associated protein;
DE AltName: CD_antigen=CD272;
DE Flags: Precursor;
GN Name=Btla {ECO:0000250|UniProtKB:Q7TSA3, ECO:0000250|UniProtKB:Q7Z6A9};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Lewis;
RA Oaks M.K., Hallett K.M., Oaks T.M.;
RT "Nucleotide sequence of the rat BTLA receptor.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Inhibitory receptor on lymphocytes that negatively regulates
CC antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2. May
CC interact in cis (on the same cell) or in trans (on other cells) with
CC TNFRSF14. In cis interactions, appears to play an immune regulatory
CC role inhibiting in trans interactions in naive T cells to maintain a
CC resting state. In trans interactions, can predominate during adaptive
CC immune response to provide survival signals to effector T cells.
CC {ECO:0000250|UniProtKB:Q7TSA3, ECO:0000250|UniProtKB:Q7Z6A9}.
CC -!- SUBUNIT: Interacts with tyrosine phosphatases PTPN6/SHP-1 and
CC PTPN11/SHP-2. Interacts with TNFRSF14/HVEM (via cysteine-rich domain
CC 1). {ECO:0000250|UniProtKB:Q7TSA3, ECO:0000250|UniProtKB:Q7Z6A9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TSA3,
CC ECO:0000250|UniProtKB:Q7Z6A9}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PNM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PNM1-2; Sequence=VSP_014838;
CC -!- PTM: Phosphorylated on Tyr residues by TNFRSF14 and by antigen
CC receptors cross-linking, both inducing association with PTPN6 and
CC PTPN11. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AY590499; AAT00435.1; -; mRNA.
DR EMBL; BC092588; AAH92588.1; -; mRNA.
DR RefSeq; NP_998795.1; NM_213630.1. [Q6PNM1-1]
DR AlphaFoldDB; Q6PNM1; -.
DR SMR; Q6PNM1; -.
DR STRING; 10116.ENSRNOP00000050172; -.
DR GlyGen; Q6PNM1; 5 sites.
DR PaxDb; Q6PNM1; -.
DR GeneID; 407756; -.
DR KEGG; rno:407756; -.
DR UCSC; RGD:1303280; rat. [Q6PNM1-1]
DR CTD; 151888; -.
DR RGD; 1303280; Btla.
DR eggNOG; ENOG502SGTG; Eukaryota.
DR InParanoid; Q6PNM1; -.
DR OrthoDB; 1342267at2759; -.
DR PhylomeDB; Q6PNM1; -.
DR Reactome; R-RNO-388841; Costimulation by the CD28 family.
DR PRO; PR:Q6PNM1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0046642; P:negative regulation of alpha-beta T cell proliferation; ISO:RGD.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039257; BTLA.
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 PANTHER; PTHR37996; PTHR37996; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..308
FT /note="B- and T-lymphocyte attenuator"
FT /id="PRO_0000014525"
FT TOPO_DOM 30..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..134
FT /note="Ig-like V-type"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 64..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 78..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 156..167
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014838"
FT CONFLICT 4
FT /note="V -> L (in Ref. 2; AAH92588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34476 MW; C99E6EB8BE199467 CRC64;
MKTVPAMLVT PRSFREFFIL LLGLWSILCK EPTKRIGEEC RVQLKIKRNS SRSAWTGELF
KIECPVTYCV HRPNVTWCKH NGTRCVPLEV GPQLHTSWVE NDQASAFVLY FEPIHLSDDG
VYTCSANLNS EVINSHSVVI HVTERTQNCS EHPLITASDI PDATNASRPS TMEERPGRTW
LLYALLPLGT SLLLLACVCL LCFLRRIQGK EKKPSDLAGR ERETNLVDIP VSSRTNSQIL
TSETGIYDND PWSSRLGESE STISSQLEGN KQGIVYASLN HCVIGRTPRQ ASKIQEAPTE
YASICVRS
