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Protein

Killer cell lectin-like receptor 3

Gene

Klra3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor on natural killer (NK) cells for class I MHC.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Killer cell lectin-like receptor 3
Alternative name(s):
5E6
Lymphocyte antigen 49c
Short name:
Ly-49c
Nk2.1
T-cell surface glycoprotein Ly-49C
Gene namesi
Name:Klra3
Synonyms:Ly-49c, Ly49C
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:101905. Klra3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 48CytoplasmicSequence analysisAdd BLAST48
Transmembranei49 – 69Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini70 – 266ExtracellularSequence analysisAdd BLAST197

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121R → G: Increases stability and improves binding to MHC I class ligand; when associated with G-175; G-197 and K-227. 1 Publication1
Mutagenesisi160N → D: Greatly reduces MHC class I peptide tetramer binding; when associated with L-162. 1 Publication1
Mutagenesisi161K → R: No effect on MHC class I peptide tetramer binding. 1 Publication1
Mutagenesisi162T → K: Greatly reduces MHC class I peptide tetramer binding; when associated with D-160. 1 Publication1
Mutagenesisi169A → Q: No effect on MHC class I peptide tetramer binding; when associated with T-170. 1 Publication1
Mutagenesisi170N → T: No effect on MHC class I peptide tetramer binding; when associated with Q-169. 1 Publication1
Mutagenesisi173H → S: No effect on MHC class I peptide tetramer binding; when associated with S-174. 1 Publication1
Mutagenesisi174Y → S: No effect on MHC class I binding; when associated with S-173. 1 Publication1
Mutagenesisi175S → G: Increases stability. Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-197 and K-227. 1 Publication1
Mutagenesisi195I → P: Greatly reduces MHC class I peptide tetramer binding; when associated with S-196. 1 Publication1
Mutagenesisi196P → S: Greatly reduces MHC class I peptide tetramer binding; when associated with P-195. 1 Publication1
Mutagenesisi197E → G: Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-175 and K-227. 1 Publication1
Mutagenesisi225K → N: Greatly reduces MHC class I peptide tetramer binding; when associated with T-226. 1 Publication1
Mutagenesisi226I → T: Greatly reduces MHC class I peptide tetramer binding; when associated with N-225. 1 Publication1
Mutagenesisi227R → K: Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-175 and G-197. 1 Publication1
Mutagenesisi234R → G: No effect on MHC class I peptide tetramer binding. 1 Publication1
Mutagenesisi248D → N: No effect on MHC class I peptide tetramer binding; when associated with D-250. 1 Publication1
Mutagenesisi250N → D: No effect on MHC class I peptide tetramer binding; when associated with N-248. 1 Publication1
Mutagenesisi251I → Q: No effect on MHC class I peptide tetramer binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000466811 – 266Killer cell lectin-like receptor 3Add BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
Glycosylationi87N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi149 ↔ 154
Glycosylationi160N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi167 ↔ 255
Disulfide bondi171 ↔ 257
Disulfide bondi236 ↔ 249

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ64329.
PaxDbiQ64329.
PRIDEiQ64329.

Expressioni

Gene expression databases

BgeeiENSMUSG00000067591.
GenevisibleiQ64329. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085333.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi145 – 151Combined sources7
Beta strandi153 – 162Combined sources10
Helixi164 – 173Combined sources10
Helixi184 – 193Combined sources10
Beta strandi199 – 206Combined sources8
Turni207 – 210Combined sources4
Beta strandi211 – 214Combined sources4
Helixi223 – 227Combined sources5
Beta strandi233 – 239Combined sources7
Beta strandi244 – 247Combined sources4
Beta strandi253 – 260Combined sources8
Beta strandi262 – 264Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P1ZX-ray3.26D143-262[»]
1P4LX-ray2.90D142-263[»]
3C8JX-ray2.60A/B/C/D67-266[»]
3C8KX-ray2.90D142-266[»]
5J6GX-ray3.30G/H136-266[»]
ProteinModelPortaliQ64329.
SMRiQ64329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64329.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 258C-type lectinPROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 151Involved in dimerization5
Regioni160 – 162Implicated in MHC class I binding3
Regioni195 – 196Implicated in MHC class I binding2
Regioni207 – 208Implicated in MHC class I binding2
Regioni224 – 233Implicated in MHC class I binding10
Regioni240 – 245Implicated in MHC class I binding6

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00390000008117.
HOGENOMiHOG000113237.
HOVERGENiHBG053176.
InParanoidiQ64329.
OMAiHEKHEPA.
OrthoDBiEOG091G0TU6.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR013600. Ly49_N.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
PF08391. Ly49. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPEVTYST VRLHKSSGLQ KLVRHEETQG PREVGNRKCS APWQLIVKAL
60 70 80 90 100
GILCFLLLVT VAVLAVKIFQ YNQHKQEINE TLNHHHNCSN MQRAFNLKEE
110 120 130 140 150
MLTNKSIDCR PSNETLEYIK REQDRWDSKT KTVLDSSRDT GRGVKYWFCY
160 170 180 190 200
STKCYYFIMN KTTWSGCKAN CQHYSVPILK IEDEDELKFL QRHVIPENYW
210 220 230 240 250
IGLSYDKKKK EWAWIDNGPS KLDMKIRKMN FKSRGCVFLS KARIEDIDCN
260
IPYYCICGKK LDKFPD
Length:266
Mass (Da):31,311
Last modified:October 31, 2012 - v2
Checksum:iBF9B10D9B6EFD628
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4P → L in AAH99880 (PubMed:15489334).Curated1
Sequence conflicti4P → L in AAH99879 (PubMed:15489334).Curated1
Sequence conflicti4P → L in AAH99878 (PubMed:15489334).Curated1
Sequence conflicti4P → L in AAH99867 (PubMed:15489334).Curated1
Sequence conflicti162T → M in BAE35215 (PubMed:16141072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2S → N in strain: C57BL/6 and C57BL/6 X BALB/c. 1
Natural varianti22L → Q in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB. 1
Natural varianti34V → A in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti41 – 42AP → VS in strain: C57BL/6 X BALB/c, NZB and C57BL/6. 2
Natural varianti60T → I in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti65 – 66AV → TI in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 2
Natural varianti72N → S in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti85H → Y in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti93 – 94RA → SD in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB. 2
Natural varianti115T → L in strain: C57BL/6, C57BL/6 X BALB/c and NZB; requires 2 nucleotide substitutions. 1
Natural varianti117E → D in strain: C57BL/6 and C57BL/6 X BALB/c. 1
Natural varianti127D → N in strain: C57BL/6 and C57BL/6 X BALB/c. 1
Natural varianti129K → E in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti131K → N in strain: NZB. 1
Natural varianti133V → I in strain: NZB. 1
Natural varianti146Y → H in strain: C57BL/6 and C57BL/6 X BALB/c. 1
Natural varianti151S → G in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti174Y → F in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB. 1
Natural varianti179L → V in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti189F → S in strain: NZB. 1
Natural varianti198N → S in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti219P → Q in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti226I → T in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti232K → T in strain: NZB. 1
Natural varianti247I → T in strain: C57BL/6, C57BL/6 X BALB/c and NZB. 1
Natural varianti251I → T in strain: NZB. 1
Natural varianti260K → R in strain: NZB. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10305 mRNA. Translation: AAA19053.1.
U09739 mRNA. Translation: AAA86873.1.
U49865 mRNA. Translation: AAA92951.1.
U49866 mRNA. Translation: AAA92952.1.
U49867 mRNA. Translation: AAA92953.1.
U49868 mRNA. Translation: AAA92954.1.
U56404 mRNA. Translation: AAB19100.1.
U56405 mRNA. Translation: AAB19101.1.
AK159595 mRNA. Translation: BAE35215.1.
AC087336 Genomic DNA. No translation available.
BC099867 mRNA. Translation: AAH99867.1.
BC099878 mRNA. Translation: AAH99878.1.
BC099879 mRNA. Translation: AAH99879.1.
BC099880 mRNA. Translation: AAH99880.1.
BC101952 mRNA. Translation: AAI01953.1.
BC103543 mRNA. Translation: AAI03544.1.
BC103544 mRNA. Translation: AAI03545.1.
BC103545 mRNA. Translation: AAI03546.1.
BC132524 mRNA. Translation: AAI32525.1.
BC132526 mRNA. Translation: AAI32527.1.
BC145192 mRNA. Translation: AAI45193.1.
BC145193 mRNA. Translation: AAI45194.1.
CCDSiCCDS20601.1.
PIRiI49059.
I49363.
RefSeqiNP_001276533.1. NM_001289604.1.
NP_001276534.1. NM_001289605.1.
NP_034778.2. NM_010648.3.
NP_034781.2. NM_010651.3.
XP_011239535.1. XM_011241233.1.
XP_011239537.1. XM_011241235.1.
UniGeneiMm.425338.
Mm.439698.
Mm.457996.

Genome annotation databases

EnsembliENSMUST00000088017; ENSMUSP00000085333; ENSMUSG00000067591.
ENSMUST00000111998; ENSMUSP00000107629; ENSMUSG00000067591.
GeneIDi16634.
16640.
KEGGimmu:16634.
mmu:16640.
UCSCiuc009eik.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10305 mRNA. Translation: AAA19053.1.
U09739 mRNA. Translation: AAA86873.1.
U49865 mRNA. Translation: AAA92951.1.
U49866 mRNA. Translation: AAA92952.1.
U49867 mRNA. Translation: AAA92953.1.
U49868 mRNA. Translation: AAA92954.1.
U56404 mRNA. Translation: AAB19100.1.
U56405 mRNA. Translation: AAB19101.1.
AK159595 mRNA. Translation: BAE35215.1.
AC087336 Genomic DNA. No translation available.
BC099867 mRNA. Translation: AAH99867.1.
BC099878 mRNA. Translation: AAH99878.1.
BC099879 mRNA. Translation: AAH99879.1.
BC099880 mRNA. Translation: AAH99880.1.
BC101952 mRNA. Translation: AAI01953.1.
BC103543 mRNA. Translation: AAI03544.1.
BC103544 mRNA. Translation: AAI03545.1.
BC103545 mRNA. Translation: AAI03546.1.
BC132524 mRNA. Translation: AAI32525.1.
BC132526 mRNA. Translation: AAI32527.1.
BC145192 mRNA. Translation: AAI45193.1.
BC145193 mRNA. Translation: AAI45194.1.
CCDSiCCDS20601.1.
PIRiI49059.
I49363.
RefSeqiNP_001276533.1. NM_001289604.1.
NP_001276534.1. NM_001289605.1.
NP_034778.2. NM_010648.3.
NP_034781.2. NM_010651.3.
XP_011239535.1. XM_011241233.1.
XP_011239537.1. XM_011241235.1.
UniGeneiMm.425338.
Mm.439698.
Mm.457996.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P1ZX-ray3.26D143-262[»]
1P4LX-ray2.90D142-263[»]
3C8JX-ray2.60A/B/C/D67-266[»]
3C8KX-ray2.90D142-266[»]
5J6GX-ray3.30G/H136-266[»]
ProteinModelPortaliQ64329.
SMRiQ64329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085333.

Proteomic databases

EPDiQ64329.
PaxDbiQ64329.
PRIDEiQ64329.

Protocols and materials databases

DNASUi16640.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088017; ENSMUSP00000085333; ENSMUSG00000067591.
ENSMUST00000111998; ENSMUSP00000107629; ENSMUSG00000067591.
GeneIDi16634.
16640.
KEGGimmu:16634.
mmu:16640.
UCSCiuc009eik.2. mouse.

Organism-specific databases

CTDi16634.
16640.
MGIiMGI:101905. Klra3.

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00390000008117.
HOGENOMiHOG000113237.
HOVERGENiHBG053176.
InParanoidiQ64329.
OMAiHEKHEPA.
OrthoDBiEOG091G0TU6.
TreeFamiTF336674.

Miscellaneous databases

EvolutionaryTraceiQ64329.
PROiQ64329.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000067591.
GenevisibleiQ64329. MM.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR013600. Ly49_N.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
PF08391. Ly49. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKLRA3_MOUSE
AccessioniPrimary (citable) accession number: Q64329
Secondary accession number(s): Q3TWQ1
, Q3ZB40, Q499I4, Q61154, Q61198, Q64257
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 31, 2012
Last modified: November 30, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.