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Protein

C-type lectin domain family 4 member K

Gene

CD207

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

Functioni

Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.4 Publications

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • mannose binding Source: ProtInc

GO - Biological processi

Keywordsi

LigandLectin

Enzyme and pathway databases

ReactomeiR-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)

Protein family/group databases

UniLectiniQ9UJ71

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 4 member K
Alternative name(s):
Langerin
CD_antigen: CD207
Gene namesi
Name:CD207
Synonyms:CLEC4K
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000116031.8
HGNCiHGNC:17935 CD207
MIMi604862 gene
neXtProtiNX_Q9UJ71

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 43CytoplasmicSequence analysisAdd BLAST43
Transmembranei44 – 64Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini65 – 328ExtracellularSequence analysisAdd BLAST264

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Birbeck granule deficiency (BIRGD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by the absence of Birbeck granules in epidermal Langerhans cells. Despite the lack of Birbeck granules, Langerhans cells are present in normal numbers and have normal morphologic characteristics and antigen-presenting capacity.
See also OMIM:613393
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063828264W → R in BIRGD; abolishes mannose-binding ability. 2 PublicationsCorresponds to variant dbSNP:rs200837270EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi285E → A: Loss of binding to 6'-sulfo-LacNAc and invertase. 1 Publication1
Mutagenesisi287N → A: Loss of binding to 6'-sulfo-LacNAc and invertase. 1 Publication1
Mutagenesisi299K → A: Loss of binding to 6'-sulfo-LacNAc. 1 Publication1
Mutagenesisi313K → A: Loss of binding to 6'-sulfo-LacNAc and 6-sulfo-GlcNAc. 1 Publication1

Organism-specific databases

DisGeNETi50489
MalaCardsiCD207
MIMi613393 phenotype
OpenTargetsiENSG00000116031
PharmGKBiPA134986203

Chemistry databases

ChEMBLiCHEMBL2176853

Polymorphism and mutation databases

BioMutaiCD207
DMDMi229784129

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002236931 – 328C-type lectin domain family 4 member KAdd BLAST328

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi87N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi180N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi223 ↔ 319PROSITE-ProRule annotation1 Publication
Disulfide bondi295 ↔ 311PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9UJ71
PeptideAtlasiQ9UJ71
PRIDEiQ9UJ71
ProteomicsDBi84594

PTM databases

iPTMnetiQ9UJ71
PhosphoSitePlusiQ9UJ71

Expressioni

Tissue specificityi

Exclusively expressed by Langerhans cells. Expressed in astrocytoma and malignant ependymoma, but not in normal brain tissues.2 Publications

Gene expression databases

BgeeiENSG00000116031
CleanExiHS_CD207
GenevisibleiQ9UJ71 HS

Organism-specific databases

HPAiCAB002222
HPA011216

Interactioni

Subunit structurei

Homotrimer.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi119076, 7 interactors
IntActiQ9UJ71, 7 interactors
STRINGi9606.ENSP00000386378

Chemistry databases

BindingDBiQ9UJ71

Structurei

Secondary structure

1328
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi160 – 195Combined sources36
Turni196 – 198Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi205 – 209Combined sources5
Helixi216 – 225Combined sources10
Helixi236 – 246Combined sources11
Beta strandi251 – 258Combined sources8
Turni259 – 262Combined sources4
Beta strandi263 – 266Combined sources4
Helixi274 – 277Combined sources4
Helixi278 – 280Combined sources3
Helixi289 – 291Combined sources3
Beta strandi295 – 298Combined sources4
Beta strandi300 – 304Combined sources5
Beta strandi306 – 309Combined sources4
Beta strandi315 – 322Combined sources8

3D structure databases

ProteinModelPortaliQ9UJ71
SMRiQ9UJ71
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJ71

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini202 – 320C-type lectinPROSITE-ProRule annotationAdd BLAST119

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili145 – 190Sequence analysisAdd BLAST46

Domaini

The C-type lectin domain mediates dual recognition of both sulfated and mannosylated glycans.1 Publication

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297 Eukaryota
ENOG410XPJ1 LUCA
GeneTreeiENSGT00760000118924
HOGENOMiHOG000064516
HOVERGENiHBG073250
InParanoidiQ9UJ71
KOiK06561
OMAiEVPDAHF
OrthoDBiEOG091G0GQS
PhylomeDBiQ9UJ71
TreeFamiTF333341

Family and domain databases

CDDicd03590 CLECT_DC-SIGN_like, 1 hit
Gene3Di3.10.100.10, 1 hit
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR033989 CD209-like_CTLD
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF00059 Lectin_C, 1 hit
SMARTiView protein in SMART
SM00034 CLECT, 1 hit
SUPFAMiSSF56436 SSF56436, 1 hit
PROSITEiView protein in PROSITE
PS00615 C_TYPE_LECTIN_1, 1 hit
PS50041 C_TYPE_LECTIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9UJ71-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVEKEAPDA HFTVDKQNIS LWPREPPPKS GPSLVPGKTP TVRAALICLT
60 70 80 90 100
LVLVASVLLQ AVLYPRFMGT ISDVKTNVQL LKGRVDNIST LDSEIKKNSD
110 120 130 140 150
GMEAAGVQIQ MVNESLGYVR SQFLKLKTSV EKANAQIQIL TRSWEEVSTL
160 170 180 190 200
NAQIPELKSD LEKASALNTK IRALQGSLEN MSKLLKRQND ILQVVSQGWK
210 220 230 240 250
YFKGNFYYFS LIPKTWYSAE QFCVSRNSHL TSVTSESEQE FLYKTAGGLI
260 270 280 290 300
YWIGLTKAGM EGDWSWVDDT PFNKVQSVRF WIPGEPNNAG NNEHCGNIKA
310 320
PSLQAWNDAP CDKTFLFICK RPYVPSEP
Length:328
Mass (Da):36,725
Last modified:March 24, 2009 - v2
Checksum:i83DF432682BF4B62
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05478155A → V. Corresponds to variant dbSNP:rs10489990Ensembl.1
Natural variantiVAR_056151136Q → E. Corresponds to variant dbSNP:rs17718987Ensembl.1
Natural variantiVAR_054782213P → S. Corresponds to variant dbSNP:rs17006436Ensembl.1
Natural variantiVAR_063828264W → R in BIRGD; abolishes mannose-binding ability. 2 PublicationsCorresponds to variant dbSNP:rs200837270EnsemblClinVar.1
Natural variantiVAR_054783278V → A No effect on mannose-binding ability. 2 PublicationsCorresponds to variant dbSNP:rs741326Ensembl.1
Natural variantiVAR_054784288N → D Significant reduction in mannose-binding ability. 1 PublicationCorresponds to variant dbSNP:rs13383830Ensembl.1
Natural variantiVAR_059448300A → P Significant reduction in mannose-binding ability; significant decrease in thermal stability; increased sensitivity of sugar binding to pH change. 1 PublicationCorresponds to variant dbSNP:rs2080391Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ242859 mRNA Translation: CAB62403.1
AC007395 Genomic DNA No translation available.
BC022278 mRNA Translation: AAH22278.1
CCDSiCCDS74520.1
RefSeqiNP_056532.4, NM_015717.4
XP_011531176.1, XM_011532874.1
UniGeneiHs.199731

Genome annotation databases

EnsembliENST00000410009; ENSP00000386378; ENSG00000116031
GeneIDi50489
KEGGihsa:50489
UCSCiuc002shg.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCLC4K_HUMAN
AccessioniPrimary (citable) accession number: Q9UJ71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 24, 2009
Last modified: July 18, 2018
This is version 148 of the entry and version 2 of the sequence. See 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 2
    Human chromosome 2: 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

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