NR3L1_HUMAN
ID NR3L1_HUMAN Reviewed; 454 AA.
AC Q68D85; Q7Z3M6;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
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; Synonyms=B7H6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH NCR3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19528259; DOI=10.1084/jem.20090681;
RA Brandt C.S., Baratin M., Yi E.C., Kennedy J., Gao Z., Fox B., Haldeman B.,
RA Ostrander C.D., Kaifu T., Chabannon C., Moretta A., West R., Xu W.,
RA Vivier E., Levin S.D.;
RT "The B7 family member B7-H6 is a tumor cell ligand for the activating
RT natural killer cell receptor NKp30 in humans.";
RL J. Exp. Med. 206:1495-1503(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-262 ALONE AND IN COMPLEX WITH
RP NCR3, GLYCOSYLATION AT ASN-43; ASN-57; ASN-208 AND ASN-242, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=21422170; DOI=10.1084/jem.20102548;
RA Li Y., Wang Q., Mariuzza R.A.;
RT "Structure of the human activating natural cytotoxicity receptor NKp30
RT bound to its tumor cell ligand B7-H6.";
RL J. Exp. Med. 208:703-714(2011).
CC -!- FUNCTION: Triggers NCR3-dependent natural killer cell activation.
CC {ECO:0000269|PubMed:19528259}.
CC -!- SUBUNIT: Monomer. Interacts specifically with NCR3, but not with other
CC natural killer cell-activating receptors, including NCR1, NCR2 and
CC KLRK1. {ECO:0000269|PubMed:19528259, ECO:0000269|PubMed:21422170}.
CC -!- INTERACTION:
CC Q68D85; P29400-2: COL4A5; NbExp=3; IntAct=EBI-14061804, EBI-12211159;
CC Q68D85; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-14061804, EBI-711490;
CC Q68D85; O14931: NCR3; NbExp=16; IntAct=EBI-14061804, EBI-14989262;
CC Q68D85; Q8N912: NRAC; NbExp=3; IntAct=EBI-14061804, EBI-12051377;
CC Q68D85; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-14061804, EBI-11721828;
CC Q68D85; Q9UNK0: STX8; NbExp=3; IntAct=EBI-14061804, EBI-727240;
CC Q68D85; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-14061804, EBI-2339195;
CC Q68D85; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-14061804, EBI-347385;
CC Q68D85; P30536: TSPO; NbExp=3; IntAct=EBI-14061804, EBI-6623146;
CC Q68D85; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-14061804, EBI-10243654;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19528259};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19528259}.
CC -!- TISSUE SPECIFICITY: Not detected in any normal tissue tested. Expressed
CC at the surface of several tumor cell lines including T and B-lymphomas,
CC myeloid leukemias, melanomas, carcinomas and large T SV40 antigen-
CC transformed cells (at protein level). {ECO:0000269|PubMed:19528259}.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97811.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX537685; CAD97811.1; ALT_INIT; mRNA.
DR EMBL; CR749521; CAH18335.1; -; mRNA.
DR EMBL; AC124798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136800; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC136797; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS55748.1; -.
DR RefSeq; NP_001189368.1; NM_001202439.2.
DR PDB; 3PV6; X-ray; 2.30 A; A=25-262.
DR PDB; 3PV7; X-ray; 2.00 A; A=25-262.
DR PDB; 4ZSO; X-ray; 2.50 A; E/F=25-262.
DR PDB; 6YJP; X-ray; 3.10 A; C/D/E=24-244.
DR PDBsum; 3PV6; -.
DR PDBsum; 3PV7; -.
DR PDBsum; 4ZSO; -.
DR PDBsum; 6YJP; -.
DR AlphaFoldDB; Q68D85; -.
DR SMR; Q68D85; -.
DR BioGRID; 131895; 64.
DR DIP; DIP-59940N; -.
DR IntAct; Q68D85; 39.
DR STRING; 9606.ENSP00000341637; -.
DR GlyConnect; 642; 2 N-Linked glycans (2 sites).
DR GlyGen; Q68D85; 7 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q68D85; -.
DR PhosphoSitePlus; Q68D85; -.
DR BioMuta; NCR3LG1; -.
DR DMDM; 74708829; -.
DR EPD; Q68D85; -.
DR jPOST; Q68D85; -.
DR MassIVE; Q68D85; -.
DR MaxQB; Q68D85; -.
DR PaxDb; Q68D85; -.
DR PeptideAtlas; Q68D85; -.
DR PRIDE; Q68D85; -.
DR ProteomicsDB; 66058; -.
DR ABCD; Q68D85; 1 sequenced antibody.
DR Antibodypedia; 6152; 388 antibodies from 21 providers.
DR DNASU; 374383; -.
DR Ensembl; ENST00000338965.9; ENSP00000341637.4; ENSG00000188211.9.
DR Ensembl; ENST00000530403.1; ENSP00000434394.1; ENSG00000188211.9.
DR GeneID; 374383; -.
DR KEGG; hsa:374383; -.
DR MANE-Select; ENST00000338965.9; ENSP00000341637.4; NM_001202439.3; NP_001189368.1.
DR UCSC; uc001mmz.5; human.
DR CTD; 374383; -.
DR DisGeNET; 374383; -.
DR GeneCards; NCR3LG1; -.
DR HGNC; HGNC:42400; NCR3LG1.
DR HPA; ENSG00000188211; Tissue enhanced (parathyroid).
DR MIM; 613714; gene.
DR neXtProt; NX_Q68D85; -.
DR OpenTargets; ENSG00000188211; -.
DR VEuPathDB; HostDB:ENSG00000188211; -.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00940000163348; -.
DR HOGENOM; CLU_602620_0_0_1; -.
DR InParanoid; Q68D85; -.
DR OMA; GKYMCES; -.
DR OrthoDB; 1030784at2759; -.
DR PhylomeDB; Q68D85; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; Q68D85; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q68D85; -.
DR BioGRID-ORCS; 374383; 17 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; Q68D85; -.
DR GenomeRNAi; 374383; -.
DR Pharos; Q68D85; Tbio.
DR PRO; PR:Q68D85; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q68D85; protein.
DR Bgee; ENSG00000188211; Expressed in cerebellar vermis and 100 other tissues.
DR Genevisible; Q68D85; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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; IPR010999; Retrovr_matrix.
DR Pfam; PF07654; C1-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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..454
FT /note="Natural cytotoxicity triggering receptor 3 ligand 1"
FT /id="PRO_0000390564"
FT TOPO_DOM 25..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..244
FT /note="Ig-like C1-type"
FT REGION 59..62
FT /note="Interaction with NCR3"
FT /evidence="ECO:0000269|PubMed:19528259"
FT REGION 127..130
FT /note="Interaction with NCR3"
FT /evidence="ECO:0000269|PubMed:19528259"
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 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21422170"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21422170"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21422170"
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:0000269|PubMed:21422170"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21422170"
FT DISULFID 163..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21422170"
FT CONFLICT 37
FT /note="I -> V (in Ref. 1; CAD97811)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> N (in Ref. 1; CAD97811)"
FT /evidence="ECO:0000305"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3PV7"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3PV6"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3PV6"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3PV7"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3PV7"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3PV7"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 129..141
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6YJP"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:3PV7"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4ZSO"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:3PV7"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3PV7"
SQ SEQUENCE 454 AA; 50827 MW; 433CE0B0EE0A4470 CRC64;
MTWRAAASTC AALLILLWAL TTEGDLKVEM MAGGTQITPL NDNVTIFCNI FYSQPLNITS
MGITWFWKSL TFDKEVKVFE FFGDHQEAFR PGAIVSPWRL KSGDASLRLP GIQLEEAGEY
RCEVVVTPLK AQGTVQLEVV ASPASRLLLD QVGMKENEDK YMCESSGFYP EAINITWEKQ
TQKFPHPIEI SEDVITGPTI KNMDGTFNVT SCLKLNSSQE DPGTVYQCVV RHASLHTPLR
SNFTLTAARH SLSETEKTDN FSIHWWPISF IGVGLVLLIV LIPWKKICNK SSSAYTPLKC
ILKHWNSFDT QTLKKEHLIF FCTRAWPSYQ LQDGEAWPPE GSVNINTIQQ LDVFCRQEGK
WSEVPYVQAF FALRDNPDLC QCCRIDPALL TVTSGKSIDD NSTKSEKQTP REHSDAVPDA
PILPVSPIWE PPPATTSTTP VLSSQPPTLL LPLQ
