ID   BT3A3_PONAB             Reviewed;         585 AA.
AC   Q5R996;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Butyrophilin subfamily 3 member A3;
DE   Flags: Precursor;
GN   Name=BTN3A3;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000305}.
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DR   EMBL; CR859495; CAH91664.1; -; mRNA.
DR   RefSeq; NP_001125975.1; NM_001132503.1.
DR   AlphaFoldDB; Q5R996; -.
DR   SMR; Q5R996; -.
DR   STRING; 9601.ENSPPYP00000018260; -.
DR   GeneID; 100172913; -.
DR   KEGG; pon:100172913; -.
DR   CTD; 10384; -.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   InParanoid; Q5R996; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   CDD; cd15820; SPRY_PRY_BTN3; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; -; 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   InterPro; IPR037954; SPRY_PRY_BTN3.
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; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..585
FT                   /note="Butyrophilin subfamily 3 member A3"
FT                   /id="PRO_0000014535"
FT   TOPO_DOM        30..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..585
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..139
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          145..236
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          322..518
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          560..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        166..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   585 AA;  64839 MW;  9D1046FEE617D361 CRC64;
     MKMASSLACL LLNFHVSVFL VQLLTPCSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA
     ETMELRWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD
     SGKYLCYFQD GDFYEKALVE LKVAALGSDL HVEVKGYENG GIHLECRSTG WYPQPQIKWS
     DAKGENIPAV EAPVVADGVG LYAVAASVIM RGGSGGGVSC IIRNSLLGLE KTASISIADP
     FFTSAQPWIA ALAGTLPISL LLLAGASYFL WRQQKEKIAL SRETEREREL KEMGYAATKQ
     EISLREKLQD ELKWRKIRYM ARGEKSLAYH EWKMALFKPA DVILDPDTAN AILLVSEDQR
     SVQRAEEPRD LPDNPERFEW RYCVLGCENF TSGRHYWEVE VGDRKEWHIG VCSKNVERKK
     GWVKMTPENG YWTMGPTDGN KYRALTEPRT NLKLPEPPRK VGIFLDYETG EISFYNAMDG
     SHIYTFPHTS FSEPVYPVFR ILTLEPTALT ICPTPKEVDR SPNPDLVLDH SLETPVTPAL
     ANESGEPQAE VTSLLLPANA GAEGVSPSTT TSQNHKPQAC TEALY