ID   BT2A2_PONAB             Reviewed;         528 AA.
AC   Q5R7W8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-MAY-2023, entry version 84.
DE   RecName: Full=Butyrophilin subfamily 2 member A2;
DE   Flags: Precursor;
GN   Name=BTN2A2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated
CC       by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000305}.
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DR   EMBL; CR859991; CAH92142.1; -; mRNA.
DR   RefSeq; NP_001126252.1; NM_001132780.1.
DR   AlphaFoldDB; Q5R7W8; -.
DR   SMR; Q5R7W8; -.
DR   STRING; 9601.ENSPPYP00000018261; -.
DR   GlyCosmos; Q5R7W8; 3 sites, No reported glycans.
DR   GeneID; 100173224; -.
DR   KEGG; pon:100173224; -.
DR   CTD; 11120; -.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   InParanoid; Q5R7W8; -.
DR   OrthoDB; 2943983at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR   CDD; cd05713; IgV_MOG_like; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR24100; BUTYROPHILIN; 1.
DR   PANTHER; PTHR24100:SF79; BUTYROPHILIN SUBFAMILY 2 MEMBER A1; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..528
FT                   /note="Butyrophilin subfamily 2 member A2"
FT                   /id="PRO_0000367055"
FT   TOPO_DOM        30..249
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..528
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..142
FT                   /note="Ig-like V-type"
FT   DOMAIN          150..232
FT                   /note="Ig-like C2-type"
FT   DOMAIN          311..507
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   COILED          270..320
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   528 AA;  60060 MW;  818C23F038FE4E66 CRC64;
     MESAAALHFS RPASLLLLLL LSLCALVSAQ VTVVGPTDPI LGMVGENTTL RCHLSPEKNA
     EDMEVRWFRS QFSPAVFVYK GGRERTEEQM EEYRGRTTFV SKDISRGSVA LVIHNITAQE
     NGTYRCYFQE GRSYDEAILH LIVAGLGSKP LIEMRGHEDG GIRLECISRG WYPKPLTVWR
     DPYGGVVPAL KEVSMPDADS LFMVTTAVII RDKSVRNMFC SINNTLLSQK KESVIFIPES
     FMPSVSPCAV ALPIVVVILM ILFAVCMYWI NKLQKEKKIL SGEKEFERET REIAVKELEK
     ERVQKEEELQ VKEKLQEELR WRRTFLHAVD VVLDPDTAHP DLFLSEDRRS VRRRPFRHLG
     ESMPDNPERF NSQPCVLGRE SFASGKHYWE VEVENVIEWT VGVCRDSVER KGEVLLIPQN
     GFWTLEMHKS QYRAVSSPDR IIPLKESLCR VGVFLDYEAG DVSFYNMRDR SHIYTCPRSA
     FSVPVRPFFR LGCEDSPIFI CPALTGANGV TVPEEGLTLH RVGTHQSL
//