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Q7TSA3 (BTLA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
B- and T-lymphocyte attenuator
Alternative name(s):
B- and T-lymphocyte-associated protein
CD_antigen=CD272
Gene names
Name:Btla
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.

Subunit structure

Interacts with tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. Interacts with TNFRSF14/HVEM. Ref.1 Ref.3 Ref.4 Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expressed in splenic T- and B-cells as well as lymph node tissues but very weakly in somatic tissues. Also expressed in macrophages, NK cells and dendritic cells. A polymorphic tissue distribution between several strains is seen. Ref.1 Ref.5

Post-translational modification

Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11. Ref.4

N-glycosylated. Ref.1

Disruption phenotype

Mice exhibit no developmental defects in T- or B-cells in thymus or bone marrow, but increased antibody responses and sensitivity to antigen-induced 'experimental autoimmune encephalomyelitis'. T-cells lacking Btla show increased proliferation with a heightened response to anti-CD3 and a slightly greater response to stimulation with anti-IgM. Ref.1

Sequence similarities

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7TSA3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7TSA3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     37-142: Missing.
Isoform 3 (identifier: Q7TSA3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     156-157: TV → I

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 306277B- and T-lymphocyte attenuator
PRO_0000014524

Regions

Topological domain30 – 183154Extracellular Potential
Transmembrane184 – 20421Helical; Potential
Topological domain205 – 306102Cytoplasmic Potential
Domain37 – 139103Ig-like V-type

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 69 Ref.6
Disulfide bond64 ↔ 124 Ref.6
Disulfide bond78 ↔ 85 Ref.6

Natural variations

Alternative sequence37 – 142106Missing in isoform 2.
VSP_014836
Alternative sequence156 – 1572TV → I in isoform 3.
VSP_014837
Natural variant411P → E in strain: 129/SvEv; requires 2 nucleotide substitutions. Ref.1
Natural variant45 – 473TIT → NIK in strain: 129/SvEv.
Natural variant521Q → H in strain: 129/SvEv. Ref.1
Natural variant551R → W in strain: 129/SvEv. Ref.1
Natural variant631Q → E in strain: 129/SvEv. Ref.1
Natural variant851C → W in strain: 129/SvEv. Ref.1
Natural variant911S → G in strain: 129/SvEv. Ref.1
Natural variant1021Q → R in strain: 129/SvEv. Ref.1
Natural variant1431R → T in strain: C57BL/6J. Ref.2

Experimental info

Mutagenesis441L → H: Loss of interaction with TNFRSF14. Ref.6
Mutagenesis481R → D: Loss of interaction with TNFRSF14. Ref.6
Mutagenesis651P → A: Loss of interaction with TNFRSF14. Ref.6
Mutagenesis1361H → D: Loss of interaction with TNFRSF14. Ref.6
Mutagenesis2451Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-274 and/or F-299. Ref.1 Ref.3
Mutagenesis2741Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-299. Ref.1 Ref.3
Mutagenesis2991Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-245 and/or F-274. Ref.1 Ref.3

Secondary structure

......................... 306
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: A5B4584BAC882B93

FASTA30634,337
        10         20         30         40         50         60 
MKTVPAMLGT PRLFREFFIL HLGLWSILCE KATKRNDEEC PVQLTITRNS KQSARTGELF 

        70         80         90        100        110        120 
KIQCPVKYCV HRPNVTWCKH NGTICVPLEV SPQLYTSWEE NQSVPVFVLH FKPIHLSDNG 

       130        140        150        160        170        180 
SYSCSTNFNS QVINSHSVTI HVRERTQNSS EHPLITVSDI PDATNASGPS TMEERPGRTW 

       190        200        210        220        230        240 
LLYTLLPLGA LLLLLACVCL LCFLKRIQGK EKKPSDLAGR DTNLVDIPAS SRTNHQALPS 

       250        260        270        280        290        300 
GTGIYDNDPW SSMQDESELT ISLQSERNNQ GIVYASLNHC VIGRNPRQEN NMQEAPTEYA 


SICVRS 

« Hide

Isoform 2 [UniParc].

Checksum: 94A167B779171DF0
Show »

FASTA20022,326
Isoform 3 [UniParc].

Checksum: 14C51F126F2F519A
Show »

FASTA30534,250

References

« Hide 'large scale' references
[1]"BTLA is a lymphocyte inhibitory receptor with similarities to CTLA-4 and PD-1."
Watanabe N., Gavrieli M., Sedy J.R., Yang J., Fallarino F., Loftin S.K., Hurchla M.A., Zimmerman N., Sim J., Zang X., Murphy T.L., Russell J.H., Allison J.P., Murphy K.M.
Nat. Immunol. 4:670-679(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF TYR-245; TYR-274 AND TYR-299, GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH PTPN6 AND PTPN11, DISRUPTION PHENOTYPE, VARIANTS GLU-41; 45-ASN--LYS-47; HIS-52; TRP-55; GLU-63; TRP-85; GLY-91 AND ARG-102.
Strain: 129/SvEv.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT THR-143.
Strain: C57BL/6J.
Tissue: Thymus.
[3]"Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2."
Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., Murphy K.M.
Biochem. Biophys. Res. Commun. 312:1236-1243(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-245; TYR-274 AND TYR-299, INTERACTION WITH PTPN6 AND PTPN11.
[4]"B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator."
Sedy J.R., Gavrieli M., Potter K.G., Hurchla M.A., Lindsley R.C., Hildner K., Scheu S., Pfeffer K., Ware C.F., Murphy T.L., Murphy K.M.
Nat. Immunol. 6:90-98(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNFRSF14, PHOSPHORYLATION.
[5]"B and T lymphocyte attenuator exhibits structural and expression polymorphisms and is highly induced in anergic CD4+ T cells."
Hurchla M.A., Sedy J.R., Gavrieli M., Drake C.G., Murphy T.L., Murphy K.M.
J. Immunol. 174:3377-3385(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, POLYMORPHISM.
[6]"Structural determinants of herpesvirus entry mediator recognition by murine B and T lymphocyte attenuator."
Nelson C.A., Fremont M.D., Sedy J.R., Norris P.S., Ware C.F., Murphy K.M., Fremont D.H.
J. Immunol. 180:940-947(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-150, MUTAGENESIS OF LEU-44; ARG-48; PRO-65 AND HIS-136, INTERACTION WITH TNFRSF14/HVEM, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY293285 mRNA. Translation: AAP44002.1.
AK041334 mRNA. Translation: BAC30910.1.
CCDSCCDS28195.1. [Q7TSA3-1]
CCDS28196.1. [Q7TSA3-3]
RefSeqNP_001032808.2. NM_001037719.2.
NP_808252.1. NM_177584.3.
UniGeneMm.38199.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XAUX-ray1.80A30-150[»]
ProteinModelPortalQ7TSA3.
SMRQ7TSA3. Positions 40-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid228954. 1 interaction.
STRING10090.ENSMUSP00000067877.

PTM databases

PhosphoSiteQ7TSA3.

Proteomic databases

PRIDEQ7TSA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102802; ENSMUSP00000099866; ENSMUSG00000052013.
GeneID208154.
KEGGmmu:208154.
UCSCuc007zik.1. mouse. [Q7TSA3-3]

Organism-specific databases

CTD151888.
MGIMGI:2658978. Btla.

Phylogenomic databases

eggNOGNOG42530.
GeneTreeENSGT00390000017390.
HOGENOMHOG000168895.
HOVERGENHBG080937.
InParanoidQ7TSA3.
KOK06707.
OrthoDBEOG7F513T.
PhylomeDBQ7TSA3.
TreeFamTF337694.

Gene expression databases

ArrayExpressQ7TSA3.
BgeeQ7TSA3.
CleanExMM_BTLA.
GenevestigatorQ7TSA3.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7TSA3.
NextBio372176.
PROQ7TSA3.
SOURCESearch...

Entry information

Entry nameBTLA_MOUSE
AccessionPrimary (citable) accession number: Q7TSA3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot