BTNL2_MOUSE
ID BTNL2_MOUSE Reviewed; 454 AA.
AC O70355; A6X8K1; Q3UW94;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Butyrophilin-like protein 2;
GN Name=Btnl2; Synonyms=Gm315, Ng9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RA Rowen L., Qin S., Loretz C., Mix L., Lasky S., Madan A., Hood L.;
RT "Sequence of the mouse major histocompatibility class II region.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16751379; DOI=10.4049/jimmunol.176.12.7354;
RA Nguyen T., Liu X.K., Zhang Y., Dong C.;
RT "BTNL2, a butyrophilin-like molecule that functions to inhibit T cell
RT activation.";
RL J. Immunol. 176:7354-7360(2006).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17237401; DOI=10.4049/jimmunol.178.3.1523;
RA Arnett H.A., Escobar S.S., Gonzalez-Suarez E., Budelsky A.L., Steffen L.A.,
RA Boiani N., Zhang M., Siu G., Brewer A.W., Viney J.L.;
RT "BTNL2, a butyrophilin/B7-like molecule, is a negative costimulatory
RT molecule modulated in intestinal inflammation.";
RL J. Immunol. 178:1523-1533(2007).
CC -!- FUNCTION: Negative regulator of T-cell proliferation.
CC {ECO:0000269|PubMed:16751379, ECO:0000269|PubMed:17237401}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O70355-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70355-2; Sequence=VSP_022147;
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine and at reduced levels
CC in lung and stomach. Also expressed in thymus, spleen, lymph nodes, T-
CC cells, B-cells, and macrophages. {ECO:0000269|PubMed:16751379,
CC ECO:0000269|PubMed:17237401}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; AK136521; BAE23022.1; -; mRNA.
DR EMBL; AF050157; AAC05288.1; ALT_TERM; Genomic_DNA.
DR EMBL; CR974457; CAO77746.1; -; Genomic_DNA.
DR CCDS; CCDS37585.1; -. [O70355-2]
DR RefSeq; NP_524574.1; NM_079835.2. [O70355-2]
DR PDB; 6L7Z; NMR; -; A=28-143.
DR PDBsum; 6L7Z; -.
DR AlphaFoldDB; O70355; -.
DR SMR; O70355; -.
DR STRING; 10090.ENSMUSP00000025198; -.
DR GlyGen; O70355; 4 sites.
DR PhosphoSitePlus; O70355; -.
DR MaxQB; O70355; -.
DR PaxDb; O70355; -.
DR PRIDE; O70355; -.
DR ProteomicsDB; 265389; -. [O70355-1]
DR ProteomicsDB; 265390; -. [O70355-2]
DR Antibodypedia; 50239; 133 antibodies from 19 providers.
DR Ensembl; ENSMUST00000025198; ENSMUSP00000025198; ENSMUSG00000024340. [O70355-2]
DR GeneID; 547431; -.
DR KEGG; mmu:547431; -.
DR UCSC; uc008ccl.1; mouse. [O70355-2]
DR CTD; 56244; -.
DR MGI; MGI:1859549; Btnl2.
DR VEuPathDB; HostDB:ENSMUSG00000024340; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000162484; -.
DR HOGENOM; CLU_032563_1_0_1; -.
DR InParanoid; O70355; -.
DR OMA; SESRMIY; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; O70355; -.
DR TreeFam; TF331083; -.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR BioGRID-ORCS; 547431; 1 hit in 72 CRISPR screens.
DR PRO; PR:O70355; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O70355; protein.
DR Bgee; ENSMUSG00000024340; Expressed in small intestine Peyer's patch and 24 other tissues.
DR ExpressionAtlas; O70355; baseline and differential.
DR Genevisible; O70355; MM.
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; IDA:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Butyrophilin-like protein 2"
FT /id="PRO_0000014538"
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 244..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 296
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"
FT VAR_SEQ 453..454
FT /note="GW -> DSKIALLWMTLPVVVLPLAMAIDLIKVKRWRRTNEQTHSSNQENNK
FT NDENHRRRLPSDERLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022147"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6L7Z"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:6L7Z"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:6L7Z"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:6L7Z"
SQ SEQUENCE 454 AA; 50894 MW; CE09E537F72CF123 CRC64;
MVDCPRYSLS GVAASFLFVL LTIKHPDDFR VVGPNLPILA KVGEDALLTC QLLPKRTTAH
MEVRWYRSDP DMPVIMYRDG AEVTGLPMEG YGGRAEWMED STEEGSVALK IRQVQPSDDG
QYWCRFQEGD YWRETSVLLQ VAALGSSPNI HVEGLGEGEV QLVCTSRGWF PEPEVHWEGI
WGEKLMSFSE NHVPGEDGLF YVEDTLMVRN DSVETISCFI YSHGLRETQE ATIALSERLQ
TELASVSVIG HSQPSPVQVG ENIELTCHLS PQTDAQNLEV RWLRSRYYPA VHVYANGTHV
AGEQMVEYKG RTSLVTDAIH EGKLTLQIHN ARTSDEGQYR CLFGKDGVYQ EARVDVQVMA
VGSTPRITRE VLKDGGMQLR CTSDGWFPRP HVQWRDRDGK TMPSFSEAFQ QGSQELFQVE
TLLLVTNGSM VNVTCSISLP LGQEKTARFP LSGW
