ID   NR3L1_PONAB             Reviewed;         454 AA.
AC   Q5RFR2;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Natural cytotoxicity triggering receptor 3 ligand 1;
DE   AltName: Full=B7 homolog 6;
DE            Short=B7-H6;
DE   Flags: Precursor;
GN   Name=NCR3LG1;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Triggers NCR3-dependent natural killer cell activation.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts specifically with NCR3.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal part is similar to retroviral Gag protein. This
CC       putative protein seems to be the result of a fusion between an Ig-like
CC       domain-containing protein and a ERV.
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DR   EMBL; CR857090; CAH89395.1; -; mRNA.
DR   RefSeq; NP_001124587.1; NM_001131115.1.
DR   AlphaFoldDB; Q5RFR2; -.
DR   SMR; Q5RFR2; -.
DR   STRING; 9601.ENSPPYP00000003966; -.
DR   GeneID; 100171423; -.
DR   KEGG; pon:100171423; -.
DR   CTD; 374383; -.
DR   eggNOG; KOG3866; Eukaryota.
DR   InParanoid; Q5RFR2; -.
DR   OrthoDB; 1030784at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.150.180; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..454
FT                   /note="Natural cytotoxicity triggering receptor 3 ligand 1"
FT                   /id="PRO_0000390565"
FT   TOPO_DOM        24..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..454
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..138
FT                   /note="Ig-like V-type"
FT   DOMAIN          143..246
FT                   /note="Ig-like C1-type"
FT   REGION          59..62
FT                   /note="Interaction with NCR3"
FT                   /evidence="ECO:0000250"
FT   REGION          127..130
FT                   /note="Interaction with NCR3"
FT                   /evidence="ECO:0000250"
FT   REGION          291..429
FT                   /note="Retroviral-Gag-like"
FT   REGION          395..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..414
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        163..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   454 AA;  50851 MW;  67557F59DC7C07BB CRC64;
     MAWRAAASTC AALLILRWAL TTAGDLKVEM MAGGTQITPL NDNVTIFCNV FYSQPLNITS
     MGITWFRKSL TFDKEVKVFE FFGDHQEAFR PGAIVSPWRL KSGDASLQLP GIQLEEAGEY
     RCEVVVTPLK AQGTVQLRVV ASPASRLFLD QVGVKENEGK YMCESSGFYP EAINIIWKKQ
     TLKFPHPIEI SEDVITGPTI KNMDGTFNVT SCLKLNSSQE DPGTVYQCVV WHESLHTPLR
     NNFTLTAARH SLSETEKTDI FSIHWWPISF IGVGLVLLIV LIPWKKMCNK SSSAYTPLKC
     IMKHWNSFDT QTLKKEHLVF FCTWAWPSYQ LQDGEAWPPE GSVNINTIQQ LDVFCRQEGK
     WSEVPYVQAF FALRDNPDLC QCCRIDPALL TVTSGKSIDD NSPKSEKQTP REHSDAVPDA
     PILPVSPIWE SPPATTSITP VLPSQPPTLL LPLQ