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Q9H2X3

- CLC4M_HUMAN

UniProt

Q9H2X3 - CLC4M_HUMAN

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Protein
C-type lectin domain family 4 member M
Gene
CLEC4M, CD209L, CD209L1, CD299
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi359 – 3591Calcium
Metal bindingi361 – 3611Calcium
Metal bindingi363 – 3631Calcium; via carbonyl oxygen
Metal bindingi366 – 3661Calcium
Metal bindingi377 – 3771Calcium
Metal bindingi378 – 3781Calcium

GO - Molecular functioni

  1. ICAM-3 receptor activity Source: UniProtKB
  2. carbohydrate binding Source: UniProtKB
  3. mannose binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. peptide antigen binding Source: UniProtKB
  6. receptor activity Source: UniProtKB
  7. virion binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation Source: UniProtKB
  2. cell-cell recognition Source: UniProtKB
  3. endocytosis Source: UniProtKB-KW
  4. innate immune response Source: UniProtKB-KW
  5. intracellular signal transduction Source: UniProtKB
  6. intracellular transport of virus Source: UniProtKB
  7. leukocyte cell-cell adhesion Source: UniProtKB
  8. modulation by virus of host morphology or physiology Source: UniProtKB
  9. peptide antigen transport Source: UniProtKB
  10. regulation of blood coagulation Source: UniProt
  11. regulation of gene expression Source: UniProt
  12. viral genome replication Source: UniProtKB
  13. virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Endocytosis, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 4 member M
Alternative name(s):
CD209 antigen-like protein 1
DC-SIGN-related protein
Short name:
DC-SIGNR
Dendritic cell-specific ICAM-3-grabbing non-integrin 2
Short name:
DC-SIGN2
Liver/lymph node-specific ICAM-3-grabbing non-integrin
Short name:
L-SIGN
CD_antigen: CD299
Gene namesi
Name:CLEC4M
Synonyms:CD209L, CD209L1, CD299
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:13523. CLEC4M.

Subcellular locationi

Isoform 5 : Secreted Reviewed prediction
Isoform 6 : Secreted Reviewed prediction
Isoform 7 : Secreted Reviewed prediction
Isoform 10 : Secreted Reviewed prediction

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949Cytoplasmic Inferred
Add
BLAST
Transmembranei50 – 7021Helical; Signal-anchor for type II membrane protein; Inferred
Add
BLAST
Topological domaini71 – 399329Extracellular Inferred
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular region Source: UniProtKB-SubCell
  3. integral component of plasma membrane Source: ProtInc
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26200.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399C-type lectin domain family 4 member M
PRO_0000046626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi92 – 921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi265 ↔ 3952 Publications
Disulfide bondi268 ↔ 2792 Publications
Disulfide bondi296 ↔ 3892 Publications
Glycosylationi361 – 3611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi368 ↔ 3812 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9H2X3.
PRIDEiQ9H2X3.

PTM databases

PhosphoSiteiQ9H2X3.

Expressioni

Tissue specificityi

Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells.3 Publications

Gene expression databases

ArrayExpressiQ9H2X3.
BgeeiQ9H2X3.
GenevestigatoriQ9H2X3.

Organism-specific databases

HPAiCAB033689.
CAB033691.
HPA042661.

Interactioni

Subunit structurei

Homotetramer. Binds to many viral surface glycoproteins such as HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus S protein.6 Publications

Protein-protein interaction databases

BioGridi115615. 5 interactions.
IntActiQ9H2X3. 2 interactions.
MINTiMINT-1489134.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi220 – 23213
Helixi262 – 2643
Beta strandi273 – 2753
Beta strandi278 – 2825
Helixi289 – 29810
Helixi309 – 32214
Beta strandi326 – 3316
Beta strandi333 – 3353
Helixi349 – 3546
Beta strandi362 – 3654
Beta strandi368 – 3725
Beta strandi375 – 3795
Beta strandi385 – 3928

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9JX-ray1.90A/B262-399[»]
1SL6X-ray2.25A/B/C/D/E/F216-399[»]
1XARX-ray2.25A/B216-399[»]
1XPHX-ray1.41A250-399[»]
1Z0Ymodel-A/B/C/D85-399[»]
3JQHX-ray2.20A101-264[»]
ProteinModelPortaliQ9H2X3.
SMRiQ9H2X3. Positions 71-398.

Miscellaneous databases

EvolutionaryTraceiQ9H2X3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati108 – 130231
Add
BLAST
Repeati131 – 153232
Add
BLAST
Repeati154 – 176233
Add
BLAST
Repeati177 – 199234
Add
BLAST
Repeati200 – 222235
Add
BLAST
Repeati223 – 245236
Add
BLAST
Repeati246 – 268237
Add
BLAST
Domaini274 – 390117C-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 2691627 X approximate tandem repeats
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 152Endocytosis signal By similarity

Domaini

The tandem repeat domain, also called neck domain, mediates oligomerization.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG314197.
HOVERGENiHBG050992.
InParanoidiQ9H2X3.
KOiK06563.
OMAiDNYWICK.
OrthoDBiEOG7DFXC9.
PhylomeDBiQ9H2X3.
TreeFamiTF333341.

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]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist. Several splicing events may occur independently in a modular way. Deletion of the transmembrane domain encoding exon through alternative splicing produces soluble isoforms.

Isoform 1 (identifier: Q9H2X3-1) [UniParc]FASTAAdd to Basket

Also known as: mDC-SIGN2 type I

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA    50
LVLQLLSFML LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV 100
GELSEKSKLQ EIYQELTQLK AAVGELPEKS KLQEIYQELT RLKAAVGELP 150
EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE IYQELTRLKA AVGELPEKSK 200
LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE LPDQSKQQQI 250
YQELTDLKTA FERLCRHCPK DWTFFQGNCY FMSNSQRNWH DSVTACQEVR 300
AQLVVIKTAE EQNFLQLQTS RSNRFSWMGL SDLNQEGTWQ WVDGSPLSPS 350
FQRYWNSGEP NNSGNEDCAE FSGSGWNDNR CDVDNYWICK KPAACFRDE 399
Length:399
Mass (Da):45,350
Last modified:March 1, 2001 - v1
Checksum:i0FADC99F72AEA593
GO
Isoform 2 (identifier: Q9H2X3-2) [UniParc]FASTAAdd to Basket

Also known as: mDC-SIGN2 type III, mDC-SIGN2 type IV

The sequence of this isoform differs from the canonical sequence as follows:
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Show »
Length:272
Mass (Da):30,481
Checksum:iB26BE2F2DE541F5E
GO
Isoform 3 (identifier: Q9H2X3-3) [UniParc]FASTAAdd to Basket

Also known as: mDC-SIGN2 type V

The sequence of this isoform differs from the canonical sequence as follows:
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Show »
Length:324
Mass (Da):36,769
Checksum:iB22BD6E0C926649A
GO
Isoform 4 (identifier: Q9H2X3-4) [UniParc]FASTAAdd to Basket

Also known as: mDC-SIGN2 type VI

The sequence of this isoform differs from the canonical sequence as follows:
     170-238: Missing.
     239-261: Missing.
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Show »
Length:232
Mass (Da):26,283
Checksum:iB50EB1500097CB70
GO
Isoform 5 (identifier: Q9H2X3-5) [UniParc]FASTAAdd to Basket

Also known as: sDC-SIGN2 type I

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     177-199: Missing.
     239-261: Missing.

Show »
Length:332
Mass (Da):37,954
Checksum:iC6FDEF92C1B073C6
GO
Isoform 6 (identifier: Q9H2X3-6) [UniParc]FASTAAdd to Basket

Also known as: sDC-SIGN2 type II

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Show »
Length:251
Mass (Da):28,373
Checksum:i86F69F6CD6055D6E
GO
Isoform 7 (identifier: Q9H2X3-7) [UniParc]FASTAAdd to Basket

Also known as: sDC-SIGN2 type III

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     147-261: Missing.

Show »
Length:263
Mass (Da):30,131
Checksum:i2BB0AAF2C506495E
GO
Isoform 8 (identifier: Q9H2X3-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-199: Missing.

Note: Non-canonical intron-exon splice junction.

Show »
Length:376
Mass (Da):42,724
Checksum:i36CB19991F23BE90
GO
Isoform 9 (identifier: Q9H2X3-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-43: Missing.
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Show »
Length:296
Mass (Da):33,528
Checksum:i70228F848F2DE64F
GO
Isoform 10 (identifier: Q9H2X3-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-43: Missing.
     44-71: Missing.
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Show »
Length:216
Mass (Da):24,408
Checksum:i45F01AD20E279619
GO

Sequence cautioni

The sequence AAR04559.1 differs from that shown. Reason: Aberrant splicing.

Polymorphismi

The number of repeats in the tandem repeat domain is shown to vary between 3 and 9 per allele thus contributing to a further variability in addition to alternative splicing. The shown 7 repeat-containing form has been shown to be the most frequent one (53.9%) in a study with 350 Caucasian individuals.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641R → Q.1 Publication
Corresponds to variant rs11465376 [ dbSNP | Ensembl ].
VAR_050107
Natural varianti205 – 2051Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].
VAR_050108
Natural varianti251 – 2511Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].
VAR_050109
Natural varianti291 – 2911D → N.1 Publication
Corresponds to variant rs2277998 [ dbSNP | Ensembl ].
VAR_021957

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 4328Missing in isoform 9 and isoform 10.
VSP_010056Add
BLAST
Alternative sequencei44 – 7128Missing in isoform 10.
VSP_010057Add
BLAST
Alternative sequencei44 – 7128GCLGH…AILVQ → VPFLLGP in isoform 5, isoform 6 and isoform 7.
VSP_010058Add
BLAST
Alternative sequencei147 – 261115Missing in isoform 7.
VSP_010059Add
BLAST
Alternative sequencei170 – 23869Missing in isoform 4.
VSP_010060Add
BLAST
Alternative sequencei177 – 19923Missing in isoform 5 and isoform 8.
VSP_010061Add
BLAST
Alternative sequencei239 – 26123Missing in isoform 4 and isoform 5.
VSP_010062Add
BLAST
Alternative sequencei262 – 27211ERLCRHCPKDW → GEFLHIKGPWA in isoform 2, isoform 6 and isoform 10.
VSP_010063Add
BLAST
Alternative sequencei273 – 399127Missing in isoform 2, isoform 6 and isoform 10.
VSP_010064Add
BLAST
Alternative sequencei313 – 32412NFLQL…SRSNR → LPAVLEQWRTQQ in isoform 3, isoform 4 and isoform 9.
VSP_010065Add
BLAST
Alternative sequencei325 – 39975Missing in isoform 3, isoform 4 and isoform 9.
VSP_010066Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991A → T in BAB14667. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015629 mRNA. Translation: BAA76496.1.
AF245219 mRNA. Translation: AAG13848.2.
AF209481, AF209480 Genomic DNA. Translation: AAG13815.2.
AY042234 mRNA. Translation: AAK91859.1.
AY042235 mRNA. Translation: AAK91860.1.
AY042236 mRNA. Translation: AAK91861.1.
AY042237 mRNA. Translation: AAK91862.1.
AY042238 mRNA. Translation: AAK91863.1.
AY042239 mRNA. Translation: AAK91864.1.
AY042240 mRNA. Translation: AAK91865.1.
AF290887 mRNA. Translation: AAK20998.1.
AY343913 mRNA. Translation: AAR04559.1. Sequence problems.
AK023750 mRNA. Translation: BAB14667.1.
AK292278 mRNA. Translation: BAF84967.1.
AC008812 Genomic DNA. No translation available.
BC038851 mRNA. Translation: AAH38851.1.
CCDSiCCDS12187.1. [Q9H2X3-1]
CCDS59346.1. [Q9H2X3-4]
CCDS59347.1. [Q9H2X3-7]
CCDS59348.1. [Q9H2X3-9]
RefSeqiNP_001138377.1. NM_001144905.1.
NP_001138378.1. NM_001144906.1. [Q9H2X3-7]
NP_001138379.1. NM_001144907.1. [Q9H2X3-5]
NP_001138380.1. NM_001144908.1. [Q9H2X3-4]
NP_001138381.1. NM_001144909.1.
NP_001138382.1. NM_001144910.1. [Q9H2X3-8]
NP_001138383.1. NM_001144911.1. [Q9H2X3-9]
NP_055072.3. NM_014257.4. [Q9H2X3-1]
XP_006722678.1. XM_006722615.1. [Q9H2X3-3]
UniGeneiHs.421437.

Genome annotation databases

EnsembliENST00000327325; ENSP00000316228; ENSG00000104938. [Q9H2X3-1]
ENST00000357361; ENSP00000349924; ENSG00000104938. [Q9H2X3-3]
ENST00000359059; ENSP00000351954; ENSG00000104938. [Q9H2X3-5]
ENST00000595496; ENSP00000470132; ENSG00000104938. [Q9H2X3-7]
ENST00000596363; ENSP00000471125; ENSG00000104938. [Q9H2X3-9]
ENST00000597522; ENSP00000471132; ENSG00000104938. [Q9H2X3-4]
GeneIDi10332.
KEGGihsa:10332.
UCSCiuc002mhy.2. human. [Q9H2X3-10]
uc002mhz.3. human. [Q9H2X3-4]
uc002mia.3. human. [Q9H2X3-7]
uc002mic.3. human. [Q9H2X3-9]
uc002mih.3. human. [Q9H2X3-8]
uc010xjw.2. human. [Q9H2X3-5]

Polymorphism databases

DMDMi46395990.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

DC-SIGNR

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015629 mRNA. Translation: BAA76496.1 .
AF245219 mRNA. Translation: AAG13848.2 .
AF209481 , AF209480 Genomic DNA. Translation: AAG13815.2 .
AY042234 mRNA. Translation: AAK91859.1 .
AY042235 mRNA. Translation: AAK91860.1 .
AY042236 mRNA. Translation: AAK91861.1 .
AY042237 mRNA. Translation: AAK91862.1 .
AY042238 mRNA. Translation: AAK91863.1 .
AY042239 mRNA. Translation: AAK91864.1 .
AY042240 mRNA. Translation: AAK91865.1 .
AF290887 mRNA. Translation: AAK20998.1 .
AY343913 mRNA. Translation: AAR04559.1 . Sequence problems.
AK023750 mRNA. Translation: BAB14667.1 .
AK292278 mRNA. Translation: BAF84967.1 .
AC008812 Genomic DNA. No translation available.
BC038851 mRNA. Translation: AAH38851.1 .
CCDSi CCDS12187.1. [Q9H2X3-1 ]
CCDS59346.1. [Q9H2X3-4 ]
CCDS59347.1. [Q9H2X3-7 ]
CCDS59348.1. [Q9H2X3-9 ]
RefSeqi NP_001138377.1. NM_001144905.1.
NP_001138378.1. NM_001144906.1. [Q9H2X3-7 ]
NP_001138379.1. NM_001144907.1. [Q9H2X3-5 ]
NP_001138380.1. NM_001144908.1. [Q9H2X3-4 ]
NP_001138381.1. NM_001144909.1.
NP_001138382.1. NM_001144910.1. [Q9H2X3-8 ]
NP_001138383.1. NM_001144911.1. [Q9H2X3-9 ]
NP_055072.3. NM_014257.4. [Q9H2X3-1 ]
XP_006722678.1. XM_006722615.1. [Q9H2X3-3 ]
UniGenei Hs.421437.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K9J X-ray 1.90 A/B 262-399 [» ]
1SL6 X-ray 2.25 A/B/C/D/E/F 216-399 [» ]
1XAR X-ray 2.25 A/B 216-399 [» ]
1XPH X-ray 1.41 A 250-399 [» ]
1Z0Y model - A/B/C/D 85-399 [» ]
3JQH X-ray 2.20 A 101-264 [» ]
ProteinModelPortali Q9H2X3.
SMRi Q9H2X3. Positions 71-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115615. 5 interactions.
IntActi Q9H2X3. 2 interactions.
MINTi MINT-1489134.

Chemistry

ChEMBLi CHEMBL2176858.

PTM databases

PhosphoSitei Q9H2X3.

Polymorphism databases

DMDMi 46395990.

Proteomic databases

PaxDbi Q9H2X3.
PRIDEi Q9H2X3.

Protocols and materials databases

DNASUi 10332.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327325 ; ENSP00000316228 ; ENSG00000104938 . [Q9H2X3-1 ]
ENST00000357361 ; ENSP00000349924 ; ENSG00000104938 . [Q9H2X3-3 ]
ENST00000359059 ; ENSP00000351954 ; ENSG00000104938 . [Q9H2X3-5 ]
ENST00000595496 ; ENSP00000470132 ; ENSG00000104938 . [Q9H2X3-7 ]
ENST00000596363 ; ENSP00000471125 ; ENSG00000104938 . [Q9H2X3-9 ]
ENST00000597522 ; ENSP00000471132 ; ENSG00000104938 . [Q9H2X3-4 ]
GeneIDi 10332.
KEGGi hsa:10332.
UCSCi uc002mhy.2. human. [Q9H2X3-10 ]
uc002mhz.3. human. [Q9H2X3-4 ]
uc002mia.3. human. [Q9H2X3-7 ]
uc002mic.3. human. [Q9H2X3-9 ]
uc002mih.3. human. [Q9H2X3-8 ]
uc010xjw.2. human. [Q9H2X3-5 ]

Organism-specific databases

CTDi 10332.
GeneCardsi GC19P007828.
HGNCi HGNC:13523. CLEC4M.
HPAi CAB033689.
CAB033691.
HPA042661.
MIMi 605872. gene.
neXtProti NX_Q9H2X3.
PharmGKBi PA26200.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314197.
HOVERGENi HBG050992.
InParanoidi Q9H2X3.
KOi K06563.
OMAi DNYWICK.
OrthoDBi EOG7DFXC9.
PhylomeDBi Q9H2X3.
TreeFami TF333341.

Miscellaneous databases

EvolutionaryTracei Q9H2X3.
GeneWikii CLEC4M.
GenomeRNAii 10332.
NextBioi 39173.
PROi Q9H2X3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H2X3.
Bgeei Q9H2X3.
Genevestigatori Q9H2X3.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
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Publicationsi

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  1. "Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank."
    Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.
    Gene 228:161-167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
    Tissue: Liver.
  2. "DC-SIGN, a related gene, DC-SIGNR, and CD23 form a cluster on 19p13."
    Soilleux E.J., Barten R., Trowsdale J.
    J. Immunol. 165:2937-2942(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  3. "Extensive repertoire of membrane-bound and soluble dendritic cell-specific ICAM-3-grabbing nonintegrin 1 (DC-SIGN1) and DC-SIGN2 isoforms. Inter-individual variation in expression of DC-SIGN transcripts."
    Mummidi S., Catano G., Lam L., Hoefle A., Telles V., Begum K., Jimenez F., Ahuja S.S., Ahuja S.K.
    J. Biol. Chem. 276:33196-33212(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6 AND 7), ALTERNATIVE SPLICING (ISOFORM 3), POLYMORPHISM, VARIANT GLN-164.
  4. "A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection."
    Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.
    J. Exp. Med. 193:671-678(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH ICAM3 AND HIV-1 GP120, POLYMORPHISM.
  5. "L-SIGN interaction with HIV-1."
    Bruen S., Bashirova A., Carrington M., KewalRamani V.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-291.
  6. "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] (ISOFORMS 8 AND 10).
    Tissue: Placenta and Testis.
  7. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Brain.
  9. "DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans."
    Poehlmann S., Soilleux E.J., Baribaud F., Leslie G.J., Morris L.S., Trowsdale J., Lee B., Coleman N., Doms R.W.
    Proc. Natl. Acad. Sci. U.S.A. 98:2670-2675(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH HIV-1 GP120, ROLE IN HIV-1 INFECTION.
  10. "A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands."
    Mitchell D.A., Fadden A.J., Drickamer K.
    J. Biol. Chem. 276:28939-28945(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, LIGAND-BINDING.
  11. "Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR."
    Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J., Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.
    J. Virol. 77:1337-1346(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 GP120; HIV-2 GP120; SIV GP120 AND EBOLA GLYCOPROTEINS.
  12. "L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus."
    Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C., Olson W.C., Gardner J.P., Dragic T.
    Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV E2 GLYCOPROTEIN.
  13. Cited for: INTERACTION WITH SARS CORONAVIRUS S PROTEIN, TISSUE SPECIFICITY.
  14. "Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR."
    Feinberg H., Mitchell D.A., Drickamer K., Weis W.I.
    Science 294:2163-2166(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 265-394 IN COMPLEX WITH GLCNAC(2)-MAN(3) PENTASACCHARIDE.
  15. "Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR."
    Feinberg H., Guo Y., Mitchell D.A., Drickamer K., Weis W.I.
    J. Biol. Chem. 280:1327-1335(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 216-399, DISULFIDE BONDS.
  16. "The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer."
    Snyder G.A., Colonna M., Sun P.D.
    J. Mol. Biol. 347:979-989(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 250-399, DISULFIDE BONDS.

Entry informationi

Entry nameiCLC4M_HUMAN
AccessioniPrimary (citable) accession number: Q9H2X3
Secondary accession number(s): A6NKI4
, A8K8B3, Q69F40, Q969M4, Q96QP3, Q96QP4, Q96QP5, Q96QP6, Q9BXS3, Q9H2Q9, Q9H8F0, Q9Y2A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 134 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

Miscellaneous

In vitro, is a receptor for HIV-1 and transmits HIV-1 to permissive T-cells.

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 19
    Human chromosome 19: 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
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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