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Protein

Killer cell immunoglobulin-like receptor 2DL2

Gene

KIR2DL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Names & Taxonomyi

Protein namesi
Recommended name:
Killer cell immunoglobulin-like receptor 2DL2
Alternative name(s):
CD158 antigen-like family member B1
MHC class I NK cell receptor
Natural killer-associated transcript 6
Short name:
NKAT-6
p58 natural killer cell receptor clone CL-43
Short name:
p58 NK receptor CL-43
CD_antigen: CD158b1
Gene namesi
Name:KIR2DL2
Synonyms:CD158B1, NKAT6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6330. KIR2DL2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 245224ExtracellularSequence analysisAdd
BLAST
Transmembranei246 – 26419HelicalSequence analysisAdd
BLAST
Topological domaini265 – 34884CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30115.

Polymorphism and mutation databases

DMDMi1171725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 348327Killer cell immunoglobulin-like receptor 2DL2PRO_0000015079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 100Combined sources2 Publications
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi149 ↔ 198Combined sources2 Publications
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP43627.

PTM databases

iPTMnetiP43627.
PhosphoSiteiP43627.

Expressioni

Gene expression databases

CleanExiHS_KIR2DL2.

Interactioni

Protein-protein interaction databases

BioGridi110004. 3 interactions.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi37 – 404Combined sources
Beta strandi45 – 539Combined sources
Beta strandi56 – 616Combined sources
Beta strandi64 – 663Combined sources
Beta strandi69 – 724Combined sources
Beta strandi77 – 8711Combined sources
Turni92 – 943Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1896Combined sources
Beta strandi194 – 2018Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi216 – 2194Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFXX-ray3.00D/E22-221[»]
2DL2X-ray3.00A26-221[»]
2DLIX-ray2.90A25-221[»]
ProteinModelPortaliP43627.
SMRiP43627. Positions 26-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43627.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10766Ig-like C2-type 1Add
BLAST
Domaini142 – 20564Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG074353.
InParanoidiP43627.
KOiK07981.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLMVVSMAC VGFFLLQGAW PHEGVHRKPS LLAHPGRLVK SEETVILQCW
60 70 80 90 100
SDVRFEHFLL HREGKFKDTL HLIGEHHDGV SKANFSIGPM MQDLAGTYRC
110 120 130 140 150
YGSVTHSPYQ LSAPSDPLDI VITGLYEKPS LSAQPGPTVL AGESVTLSCS
160 170 180 190 200
SRSSYDMYHL SREGEAHECR FSAGPKVNGT FQADFPLGPA THGGTYRCFG
210 220 230 240 250
SFRDSPYEWS NSSDPLLVSV IGNPSNSWPS PTEPSSKTGN PRHLHILIGT
260 270 280 290 300
SVVIILFILL FFLLHRWCSN KKNAAVMDQE SAGNRTANSE DSDEQDPQEV
310 320 330 340
TYTQLNHCVF TQRKITRPSQ RPKTPPTDII VYAELPNAES RSKVVSCP
Length:348
Mass (Da):38,472
Last modified:November 1, 1995 - v1
Checksum:i5B54C548F5CF3FBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2902SE → RQ in AAB36597 (PubMed:8662091).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91A → V.
Corresponds to variant rs3810343 [ dbSNP | Ensembl ].
VAR_059417
Natural varianti37 – 371R → P.
Corresponds to variant rs613240 [ dbSNP | Ensembl ].
VAR_021929
Natural varianti66 – 661F → Y.
Corresponds to variant rs673568 [ dbSNP | Ensembl ].
VAR_059418

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24075 mRNA. Translation: AAC50334.1.
L76669 mRNA. Translation: AAB36597.1.
EU791544 Genomic DNA. Translation: ACI49715.1.
RefSeqiNP_055034.2. NM_014219.2.
UniGeneiHs.743949.

Genome annotation databases

EnsembliENST00000611724; ENSP00000482519; ENSG00000275546.
ENST00000613410; ENSP00000483373; ENSG00000276731.
ENST00000616831; ENSP00000482201; ENSG00000278731.
ENST00000618388; ENSP00000480161; ENSG00000275914.
ENST00000618796; ENSP00000481907; ENSG00000275407.
ENST00000619621; ENSP00000483052; ENSG00000276011.
GeneIDi3803.
KEGGihsa:3803.
UCSCiuc032lsh.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24075 mRNA. Translation: AAC50334.1.
L76669 mRNA. Translation: AAB36597.1.
EU791544 Genomic DNA. Translation: ACI49715.1.
RefSeqiNP_055034.2. NM_014219.2.
UniGeneiHs.743949.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFXX-ray3.00D/E22-221[»]
2DL2X-ray3.00A26-221[»]
2DLIX-ray2.90A25-221[»]
ProteinModelPortaliP43627.
SMRiP43627. Positions 26-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110004. 3 interactions.

PTM databases

iPTMnetiP43627.
PhosphoSiteiP43627.

Polymorphism and mutation databases

DMDMi1171725.

Proteomic databases

PRIDEiP43627.

Protocols and materials databases

DNASUi3803.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000611724; ENSP00000482519; ENSG00000275546.
ENST00000613410; ENSP00000483373; ENSG00000276731.
ENST00000616831; ENSP00000482201; ENSG00000278731.
ENST00000618388; ENSP00000480161; ENSG00000275914.
ENST00000618796; ENSP00000481907; ENSG00000275407.
ENST00000619621; ENSP00000483052; ENSG00000276011.
GeneIDi3803.
KEGGihsa:3803.
UCSCiuc032lsh.2. human.

Organism-specific databases

CTDi3803.
GeneCardsiKIR2DL2.
HGNCiHGNC:6330. KIR2DL2.
MIMi604937. gene.
neXtProtiNX_P43627.
PharmGKBiPA30115.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG074353.
InParanoidiP43627.
KOiK07981.

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

EvolutionaryTraceiP43627.
GenomeRNAii3803.
PROiP43627.
SOURCEiSearch...

Gene expression databases

CleanExiHS_KIR2DL2.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related molecules with diversity in both the extra- and intracellular domains."
    Wagtmann N., Biassoni R., Cantoni C., Verdiani S., Malnati M.S., Vitale M., Bottino C., Moretta L., Moretta A., Long E.O.
    Immunity 2:439-449(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Natural killer cell.
  2. "Alternatively spliced forms of human killer inhibitory receptors."
    Doehring C., Samaridis J., Colonna M.
    Immunogenetics 44:227-230(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Highly homologous KIR genes require additional strategies to obtain complete coding sequences of KIR2DL2/3 alleles from genomic DNA."
    Hou L., Hurley C.K., Steiner N.K., Belle I.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2."
    Snyder G.A., Brooks A.G., Sun P.D.
    Proc. Natl. Acad. Sci. U.S.A. 96:3864-3869(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 25-221, FUNCTION, DISULFIDE BONDS.
  5. "Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand."
    Boyington J.C., Motyka S.A., Schuck P., Brooks A.G., Sun P.D.
    Nature 405:537-543(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-221 IN COMPLEX WITH HLA-CW3, DISULFIDE BONDS.

Entry informationi

Entry nameiKI2L2_HUMAN
AccessioniPrimary (citable) accession number: P43627
Secondary accession number(s): C6EVR8, Q14951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.