ID   BTNL2_RAT               Reviewed;         454 AA.
AC   Q6MG97;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Butyrophilin-like protein 2;
GN   Name=Btnl2;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
CC   -!- FUNCTION: Negative regulator of T-cell proliferation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000305}.
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DR   EMBL; BX883043; CAE83949.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6MG97; -.
DR   SMR; Q6MG97; -.
DR   STRING; 10116.ENSRNOP00000057110; -.
DR   GlyGen; Q6MG97; 3 sites.
DR   PaxDb; Q6MG97; -.
DR   PRIDE; Q6MG97; -.
DR   UCSC; RGD:620731; rat.
DR   RGD; 620731; Btnl2.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   InParanoid; Q6MG97; -.
DR   PhylomeDB; Q6MG97; -.
DR   TreeFam; TF331083; -.
DR   Reactome; R-RNO-8851680; Butyrophilin (BTN) family interactions.
DR   PRO; PR:Q6MG97; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR013162; CD80_C2-set.
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; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00406; IGv; 2.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..454
FT                   /note="Butyrophilin-like protein 2"
FT                   /id="PRO_0000014539"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..454
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..140
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          148..234
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          236..355
FT                   /note="Ig-like V-type 3"
FT   DOMAIN          365..452
FT                   /note="Ig-like V-type 4"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        164..218
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        267..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        381..435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   454 AA;  50767 MW;  D56CC3FE0BDA706D CRC64;
     MVDFPGYSLS GVAASFLFVL LTMKHPDDFR VVGPALPILA NVGEDALLTC RLLPKRTTAR
     MEVRWYRSDP DTPVMLYRDG AEVPGLAMEG YRGRVEWMED STEEGSVALK IRQVQPGDDG
     QYWCRIQEGD YWREASVLLQ VAALGSSPNI HVEGPGEEGV QLVCTSRGWF PEPEVYWEGI
     RGEKLMSLSE NHVYGEDGLF SVEDTLVVRN DSVETISCFI YNRGLREPQE ATIALPEKLQ
     TELASSRVIG PSQAIPVRVG ETIELTCQLS PQTDAQSLEV RWLRARYYPV VHVYTNGAHE
     AGEQMAEYRG RTSLVTDAIH EGKLTLQIHN ARTSDEGQYR CLFGKDGVYQ EARVDVQVMA
     VGSTPQITRE VLKDGGTQLR CTSDGWFPRP HVQWRDRDGR TLPSFSEAFR QGSQELFQVE
     TLLLVTNGSM VNVTCSISLP LGEEKTARFP LSGW