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Protein

C-type lectin domain family 4 member A

Gene

Clec4a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in regulating immune reactivity. May play a role in modulating dendritic cells (DC) differentiation and/or maturation (By similarity). May be involved in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation.By similarity1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity, Innate immunity

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 4 member A
Alternative name(s):
C-type lectin superfamily member 6
Dendritic cell immunoreceptor
Gene namesi
Name:Clec4a
Synonyms:Clec4a2, Clecsf6, Dcir
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1349412. Clec4a2.

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 – 238169ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71Y → F: Loss of inhibition of B-cell calcium mobilization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238C-type lectin domain family 4 member APRO_0000046613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi107 ↔ 118PROSITE-ProRule annotation
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence analysis
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi137 ↔ 231PROSITE-ProRule annotation
Disulfide bondi205 ↔ 223PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9QZ15.
PRIDEiQ9QZ15.

PTM databases

iPTMnetiQ9QZ15.
PhosphoSiteiQ9QZ15.

Expressioni

Tissue specificityi

Expressed in splenic antigen-presenting cells including B-cells, monocytes/macrophages, and dendritic cells (at protein level). Expressed in spleen and lymph node and slightly increased with dendritic cell maturation.1 Publication

Gene expression databases

BgeeiQ9QZ15.
CleanExiMM_CLEC4A2.
ExpressionAtlasiQ9QZ15. baseline and differential.
GenevisibleiQ9QZ15. MM.

Interactioni

Subunit structurei

May interact with PTPN6 via its ITIM site.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9QZ15.
SMRiQ9QZ15. Positions 69-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 233108C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 106ITIM motif

Domaini

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000118924.
HOGENOMiHOG000059556.
HOVERGENiHBG050992.
InParanoidiQ9QZ15.
KOiK10057.
PhylomeDBiQ9QZ15.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QZ15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEITYAEV KFKNESNSLH TYSESPAAPR EKPIRDLRKP GSPSLLLTSL
60 70 80 90 100
MLLLLLLAIT FLVAFIIYFQ KYSQLLEEKK AAKNIMHNEL NCTKSVSPME
110 120 130 140 150
DKVWSCCPKD WRLFGSHCYL VPTVSSSASW NKSEENCSRM GAHLVVIQSQ
160 170 180 190 200
EEQDFITGIL DTHAAYFIGL WDTGHRQWQW VDQTPYEESI TFWHNGEPSS
210 220 230
GNEKCATIIY RWKTGWGWND ISCSLKQKSV CQMKKINL
Length:238
Mass (Da):27,323
Last modified:May 1, 2000 - v1
Checksum:i2DB8AE0E11B18A56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133533 mRNA. Translation: CAB57870.1.
AF387099 mRNA. Translation: AAM22402.1.
AK049002 mRNA. Translation: BAC33509.1.
BC075729 mRNA. Translation: AAH75729.1.
BC096565 mRNA. Translation: AAH96565.1.
CCDSiCCDS20510.1.
RefSeqiNP_001163803.1. NM_001170332.1.
NP_001163804.1. NM_001170333.1.
NP_036129.1. NM_011999.4.
UniGeneiMm.47384.

Genome annotation databases

EnsembliENSMUST00000041779; ENSMUSP00000045781; ENSMUSG00000030148.
ENSMUST00000161365; ENSMUSP00000124615; ENSMUSG00000030148.
GeneIDi26888.
KEGGimmu:26888.
UCSCiuc009dqa.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

DCIR1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133533 mRNA. Translation: CAB57870.1.
AF387099 mRNA. Translation: AAM22402.1.
AK049002 mRNA. Translation: BAC33509.1.
BC075729 mRNA. Translation: AAH75729.1.
BC096565 mRNA. Translation: AAH96565.1.
CCDSiCCDS20510.1.
RefSeqiNP_001163803.1. NM_001170332.1.
NP_001163804.1. NM_001170333.1.
NP_036129.1. NM_011999.4.
UniGeneiMm.47384.

3D structure databases

ProteinModelPortaliQ9QZ15.
SMRiQ9QZ15. Positions 69-235.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9QZ15.
PhosphoSiteiQ9QZ15.

Proteomic databases

MaxQBiQ9QZ15.
PRIDEiQ9QZ15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041779; ENSMUSP00000045781; ENSMUSG00000030148.
ENSMUST00000161365; ENSMUSP00000124615; ENSMUSG00000030148.
GeneIDi26888.
KEGGimmu:26888.
UCSCiuc009dqa.1. mouse.

Organism-specific databases

CTDi26888.
MGIiMGI:1349412. Clec4a2.

Phylogenomic databases

GeneTreeiENSGT00760000118924.
HOGENOMiHOG000059556.
HOVERGENiHBG050992.
InParanoidiQ9QZ15.
KOiK10057.
PhylomeDBiQ9QZ15.

Miscellaneous databases

PROiQ9QZ15.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZ15.
CleanExiMM_CLEC4A2.
ExpressionAtlasiQ9QZ15. baseline and differential.
GenevisibleiQ9QZ15. MM.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif."
    Bates E.E.M., Fournier N., Garcia E., Valladeau J., Durand I., Pin J.-J., Zurawski S.M., Patel S., Abrams J.S., Lebecque S., Garrone P., Saeland S.
    J. Immunol. 163:1973-1983(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymph node.
  2. "DCIR acts as an inhibitory receptor depending on its immunoreceptor tyrosine-based inhibitory motif."
    Kanazawa N., Okazaki T., Nishimura H., Tashiro K., Inaba K., Miyachi Y.
    J. Invest. Dermatol. 118:261-266(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-7.
    Strain: BALB/cJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Jaw, Limb and Mammary gland.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLC4A_MOUSE
AccessioniPrimary (citable) accession number: Q9QZ15
Secondary accession number(s): Q4VA33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.