Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C-type lectin domain family 4 member E

Gene

CLEC4E

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

Functioni

C-type lectin that functions as cell-surface receptor for a wide variety of ligands such as damaged cells, fungi and mycobacteria. Plays a role in the recognition of pathogenic fungi, such as Candida albicans. The detection of mycobacteria is via trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid. Specifically recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia. Recognizes also SAP130, a nuclear protein, that is released by dead or dying cells. Transduces signals through an ITAM-containing adapter protein, Fc receptor gamma chain /FCER1G. Induces secretion of inflammatory cytokines through a pathway that depends on SYK, CARD9 and NF-kappa-B.1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: ProtInc
  • receptor activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-HSA-5621480. Dectin-2 family.

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 4 member E
Alternative name(s):
C-type lectin superfamily member 9
Macrophage-inducible C-type lectin
Gene namesi
Name:CLEC4E
Synonyms:CLECSF9, MINCLE
ORF Names:UNQ218/PRO244
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:14555. CLEC4E.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini41 – 219179ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26586.

Polymorphism and mutation databases

BioMutaiCLEC4E.
DMDMi59797976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219C-type lectin domain family 4 member EPRO_0000046619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi80 ↔ 91PROSITE-ProRule annotation
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi108 ↔ 205PROSITE-ProRule annotation
Disulfide bondi179 ↔ 197PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9ULY5.
PaxDbiQ9ULY5.
PRIDEiQ9ULY5.

PTM databases

PhosphoSiteiQ9ULY5.

Expressioni

Gene expression databases

BgeeiQ9ULY5.
CleanExiHS_CLEC4E.
ExpressionAtlasiQ9ULY5. baseline and differential.
GenevisibleiQ9ULY5. HS.

Organism-specific databases

HPAiHPA004935.

Interactioni

Subunit structurei

Monomer. Homodimer.1 Publication

Protein-protein interaction databases

BioGridi117639. 3 interactions.
STRINGi9606.ENSP00000299663.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi85 – 873Combined sources
Beta strandi90 – 945Combined sources
Helixi101 – 11010Combined sources
Helixi121 – 13010Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi174 – 1829Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi201 – 2088Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WH2X-ray1.30A74-219[»]
3WH3X-ray1.32A74-219[»]
ProteinModelPortaliQ9ULY5.
SMRiQ9ULY5. Positions 78-209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 206120C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IS3J. Eukaryota.
ENOG410YTFW. LUCA.
GeneTreeiENSGT00760000118924.
HOGENOMiHOG000059556.
HOVERGENiHBG050992.
InParanoidiQ9ULY5.
KOiK10059.
OMAiVKNCCPL.
OrthoDBiEOG70ZZPH.
PhylomeDBiQ9ULY5.
TreeFamiTF333341.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 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.

Q9ULY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSSKSSETQ CTERGCFSSQ MFLWTVAGIP ILFLSACFIT RCVVTFRIFQ
60 70 80 90 100
TCDEKKFQLP ENFTELSCYN YGSGSVKNCC PLNWEYFQSS CYFFSTDTIS
110 120 130 140 150
WALSLKNCSA MGAHLVVINS QEEQEFLSYK KPKMREFFIG LSDQVVEGQW
160 170 180 190 200
QWVDGTPLTK SLSFWDVGEP NNIATLEDCA TMRDSSNPRQ NWNDVTCFLN
210
YFRICEMVGI NPLNKGKSL
Length:219
Mass (Da):25,073
Last modified:May 1, 2000 - v1
Checksum:iC5D48DD7427D7FC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024718 mRNA. Translation: BAA83755.1.
AY358499 mRNA. Translation: AAQ88863.1.
AK312671 mRNA. Translation: BAG35553.1.
AC092746 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88618.1.
BC000715 mRNA. Translation: AAH00715.1.
CCDSiCCDS8594.1.
RefSeqiNP_055173.1. NM_014358.3.
UniGeneiHs.236516.

Genome annotation databases

EnsembliENST00000299663; ENSP00000299663; ENSG00000166523.
GeneIDi26253.
KEGGihsa:26253.
UCSCiuc001quo.2. human.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Mincle

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024718 mRNA. Translation: BAA83755.1.
AY358499 mRNA. Translation: AAQ88863.1.
AK312671 mRNA. Translation: BAG35553.1.
AC092746 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88618.1.
BC000715 mRNA. Translation: AAH00715.1.
CCDSiCCDS8594.1.
RefSeqiNP_055173.1. NM_014358.3.
UniGeneiHs.236516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WH2X-ray1.30A74-219[»]
3WH3X-ray1.32A74-219[»]
ProteinModelPortaliQ9ULY5.
SMRiQ9ULY5. Positions 78-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117639. 3 interactions.
STRINGi9606.ENSP00000299663.

PTM databases

PhosphoSiteiQ9ULY5.

Polymorphism and mutation databases

BioMutaiCLEC4E.
DMDMi59797976.

Proteomic databases

EPDiQ9ULY5.
PaxDbiQ9ULY5.
PRIDEiQ9ULY5.

Protocols and materials databases

DNASUi26253.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299663; ENSP00000299663; ENSG00000166523.
GeneIDi26253.
KEGGihsa:26253.
UCSCiuc001quo.2. human.

Organism-specific databases

CTDi26253.
GeneCardsiCLEC4E.
HGNCiHGNC:14555. CLEC4E.
HPAiHPA004935.
MIMi609962. gene.
neXtProtiNX_Q9ULY5.
PharmGKBiPA26586.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IS3J. Eukaryota.
ENOG410YTFW. LUCA.
GeneTreeiENSGT00760000118924.
HOGENOMiHOG000059556.
HOVERGENiHBG050992.
InParanoidiQ9ULY5.
KOiK10059.
OMAiVKNCCPL.
OrthoDBiEOG70ZZPH.
PhylomeDBiQ9ULY5.
TreeFamiTF333341.

Enzyme and pathway databases

ReactomeiR-HSA-5621480. Dectin-2 family.

Miscellaneous databases

GenomeRNAii26253.
NextBioi48470.
PROiQ9ULY5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULY5.
CleanExiHS_CLEC4E.
ExpressionAtlasiQ9ULY5. baseline and differential.
GenevisibleiQ9ULY5. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel LPS-inducible C-type lectin is a transcriptional target of NF-IL6 in macrophages."
    Matsumoto M., Shimada T., Kaisho T., Sanjo H., Tanaka T., Copeland N.G., Gilbert D.J., Jenkins N.A., Akira S.
    J. Immunol. 163:5039-5048(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocytic leukemia.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Kidney.
  7. "Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans."
    Bugarcic A., Hitchens K., Beckhouse A.G., Wells C.A., Ashman R.B., Blanchard H.
    Glycobiology 18:679-685(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS RECEPTOR FOR CANDIDA ALBICANS, SUBUNIT.
  8. "Mincle is an ITAM-coupled activating receptor that senses damaged cells."
    Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., Saito T.
    Nat. Immunol. 9:1179-1188(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCER1G.

Entry informationi

Entry nameiCLC4E_HUMAN
AccessioniPrimary (citable) accession number: Q9ULY5
Secondary accession number(s): B2R6Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 119 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 chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.