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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848CytoplasmicSequence analysisAdd
BLAST
Transmembranei49 – 6921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini70 – 266197ExtracellularSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211R → G: Increases stability and improves binding to MHC I class ligand; when associated with G-175; G-197 and K-227. 1 Publication
Mutagenesisi160 – 1601N → D: Greatly reduces MHC class I peptide tetramer binding; when associated with L-162. 1 Publication
Mutagenesisi161 – 1611K → R: No effect on MHC class I peptide tetramer binding. 1 Publication
Mutagenesisi162 – 1621T → K: Greatly reduces MHC class I peptide tetramer binding; when associated with D-160. 1 Publication
Mutagenesisi169 – 1691A → Q: No effect on MHC class I peptide tetramer binding; when associated with T-170. 1 Publication
Mutagenesisi170 – 1701N → T: No effect on MHC class I peptide tetramer binding; when associated with Q-169. 1 Publication
Mutagenesisi173 – 1731H → S: No effect on MHC class I peptide tetramer binding; when associated with S-174. 1 Publication
Mutagenesisi174 – 1741Y → S: No effect on MHC class I binding; when associated with S-173. 1 Publication
Mutagenesisi175 – 1751S → G: Increases stability. Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-197 and K-227. 1 Publication
Mutagenesisi195 – 1951I → P: Greatly reduces MHC class I peptide tetramer binding; when associated with S-196. 1 Publication
Mutagenesisi196 – 1961P → S: Greatly reduces MHC class I peptide tetramer binding; when associated with P-195. 1 Publication
Mutagenesisi197 – 1971E → G: Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-175 and K-227. 1 Publication
Mutagenesisi225 – 2251K → N: Greatly reduces MHC class I peptide tetramer binding; when associated with T-226. 1 Publication
Mutagenesisi226 – 2261I → T: Greatly reduces MHC class I peptide tetramer binding; when associated with N-225. 1 Publication
Mutagenesisi227 – 2271R → K: Increases stability and improves binding to MHC I class ligand; when associated with G-121; G-175 and G-197. 1 Publication
Mutagenesisi234 – 2341R → G: No effect on MHC class I peptide tetramer binding. 1 Publication
Mutagenesisi248 – 2481D → N: No effect on MHC class I peptide tetramer binding; when associated with D-250. 1 Publication
Mutagenesisi250 – 2501N → D: No effect on MHC class I peptide tetramer binding; when associated with N-248. 1 Publication
Mutagenesisi251 – 2511I → Q: No effect on MHC class I peptide tetramer binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Killer cell lectin-like receptor 3PRO_0000046681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi149 ↔ 154
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence analysis
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

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi145 – 1517Combined sources
Beta strandi153 – 16210Combined sources
Helixi164 – 17310Combined sources
Helixi184 – 19310Combined sources
Beta strandi199 – 2068Combined sources
Turni207 – 2104Combined sources
Beta strandi211 – 2144Combined sources
Helixi223 – 2275Combined sources
Beta strandi233 – 2397Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi253 – 2608Combined sources
Beta strandi262 – 2643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1ZX-ray3.26D143-262[»]
1P4LX-ray2.90D142-263[»]
3C8JX-ray2.60A/B/C/D67-266[»]
3C8KX-ray2.90D142-266[»]
ProteinModelPortaliQ64329.
SMRiQ64329. Positions 107-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64329.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini150 – 258109C-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 1515Involved in dimerization
Regioni160 – 1623Implicated in MHC class I binding
Regioni195 – 1962Implicated in MHC class I binding
Regioni207 – 2082Implicated in MHC class I binding
Regioni224 – 23310Implicated in MHC class I binding
Regioni240 – 2456Implicated in MHC class I binding

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.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41P → L in AAH99880 (PubMed:15489334).Curated
Sequence conflicti4 – 41P → L in AAH99879 (PubMed:15489334).Curated
Sequence conflicti4 – 41P → L in AAH99878 (PubMed:15489334).Curated
Sequence conflicti4 – 41P → L in AAH99867 (PubMed:15489334).Curated
Sequence conflicti162 – 1621T → M in BAE35215 (PubMed:16141072).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → N in strain: C57BL/6 and C57BL/6 X BALB/c.
Natural varianti22 – 221L → Q in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB.
Natural varianti34 – 341V → A in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti41 – 422AP → VS in strain: C57BL/6 X BALB/c, NZB and C57BL/6.
Natural varianti60 – 601T → I in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti65 – 662AV → TI in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti72 – 721N → S in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti85 – 851H → Y in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti93 – 942RA → SD in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB.
Natural varianti115 – 1151T → L in strain: C57BL/6, C57BL/6 X BALB/c and NZB; requires 2 nucleotide substitutions.
Natural varianti117 – 1171E → D in strain: C57BL/6 and C57BL/6 X BALB/c.
Natural varianti127 – 1271D → N in strain: C57BL/6 and C57BL/6 X BALB/c.
Natural varianti129 – 1291K → E in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti131 – 1311K → N in strain: NZB.
Natural varianti133 – 1331V → I in strain: NZB.
Natural varianti146 – 1461Y → H in strain: C57BL/6 and C57BL/6 X BALB/c.
Natural varianti151 – 1511S → G in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti174 – 1741Y → F in strain: A/Sn, BALB/c, C57BL/6, C57BL/6 X BALB/c, C57BL/6 X CBA, CB-17/SCID and NZB.
Natural varianti179 – 1791L → V in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti189 – 1891F → S in strain: NZB.
Natural varianti198 – 1981N → S in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti219 – 2191P → Q in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti226 – 2261I → T in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti232 – 2321K → T in strain: NZB.
Natural varianti247 – 2471I → T in strain: C57BL/6, C57BL/6 X BALB/c and NZB.
Natural varianti251 – 2511I → T in strain: NZB.
Natural varianti260 – 2601K → R in strain: NZB.

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_011239536.1. XM_011241234.1.
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_011239536.1. XM_011241234.1.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1ZX-ray3.26D143-262[»]
1P4LX-ray2.90D142-263[»]
3C8JX-ray2.60A/B/C/D67-266[»]
3C8KX-ray2.90D142-266[»]
ProteinModelPortaliQ64329.
SMRiQ64329. Positions 107-265.
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.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_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: September 7, 2016
This is version 140 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.