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Protein

C-type lectin domain family 4 member K

Gene

CD207

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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).

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

HGNCiHGNC:17935. CD207.

Subcellular locationi

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

GO - Cellular componenti

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:rs200837270Ensembl.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

EPDiQ9UJ71.
PaxDbiQ9UJ71.
PeptideAtlasiQ9UJ71.
PRIDEiQ9UJ71.

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. 5 interactors.
MINTiMINT-6631688.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C22X-ray1.50A/B/C/D188-328[»]
3KQGX-ray2.30A/B/C/D/E/F147-328[»]
3P5DX-ray1.80A/B/C/D193-328[»]
3P5EX-ray1.70A/B/C/D193-328[»]
3P5FX-ray1.75A/B/C/D193-328[»]
3P5GX-ray1.60A/B/C/D193-328[»]
3P5HX-ray1.61A/B/C/D193-328[»]
3P5IX-ray1.80A/B/C/D193-328[»]
3P7FX-ray2.50A/B/C/D193-328[»]
3P7GX-ray1.60A/B/C/D193-328[»]
3P7HX-ray2.30A/B/C/D193-328[»]
4AK8X-ray1.40A/B/C/D188-328[»]
4N32X-ray1.75A/B/C/D193-328[»]
4N33X-ray1.85A/B/C/D193-328[»]
4N34X-ray1.75A/B/C/D193-328[»]
4N35X-ray1.85A/B/C/D193-328[»]
4N36X-ray1.85A/B/C/D193-328[»]
4N37X-ray2.00A/B/C/D193-328[»]
4N38X-ray2.00A/B/C/D193-328[»]
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.
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:rs200837270Ensembl.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: August 30, 2017
This is version 140 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