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Protein

C-type lectin domain family 11 member A

Gene

CLEC11A

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

Functioni

Stimulates the proliferation and differentiation of hematopoietic precursor cells from various lineages, including erythrocytes, lymphocytes, granulocytes and macrophages. Acts synergistically with other cytokines, including IL-3, GCSF, GMCSF and FLT3 ligand. Suppresses SCF-stimulated erythrocyte proliferation.1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • growth factor activity Source: UniProtKB

GO - Biological processi

  • positive regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 11 member A
Alternative name(s):
C-type lectin superfamily member 3
Lymphocyte secreted C-type lectin
Stem cell growth factor
p47
Gene namesi
Name:CLEC11A
Synonyms:CLECSF3, LSLCL, SCGF
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10576. CLEC11A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34996.

Polymorphism and mutation databases

BioMutaiCLEC11A.
DMDMi34223087.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 323302C-type lectin domain family 11 member APRO_0000017468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi204 ↔ 319PROSITE-ProRule annotation
Disulfide bondi296 ↔ 311PROSITE-ProRule annotation

Post-translational modificationi

O-glycosylated. Probably sulfated on the O-glycans.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9Y240.
MaxQBiQ9Y240.
PaxDbiQ9Y240.
PeptideAtlasiQ9Y240.
PRIDEiQ9Y240.

PTM databases

iPTMnetiQ9Y240.
PhosphoSiteiQ9Y240.

Expressioni

Tissue specificityi

Expressed in skeletal tissues including bone marrow, chondrocytes, primary ossification center-associated cells, the perichondrium and periosteum. Lower levels of expression were detected in spleen, thymus, appendix and fetal liver.4 Publications

Developmental stagei

In the bone marrow, expression is limited to immature neutrophils. Expression was not detected in circulating mature neutrophils.1 Publication

Gene expression databases

BgeeiQ9Y240.
CleanExiHS_CLEC11A.
ExpressionAtlasiQ9Y240. baseline and differential.
GenevisibleiQ9Y240. HS.

Organism-specific databases

HPAiHPA042690.

Interactioni

GO - Molecular functioni

  • growth factor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112226. 36 interactions.
IntActiQ9Y240. 1 interaction.
STRINGi9606.ENSP00000250340.

Structurei

3D structure databases

ProteinModelPortaliQ9Y240.
SMRiQ9Y240. Positions 132-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 320138C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi61 – 633Cell attachment siteSequence analysis

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00610000086061.
HOGENOMiHOG000273889.
HOVERGENiHBG052365.
InParanoidiQ9Y240.
KOiK17521.
OMAiFAWHRSP.
PhylomeDBiQ9Y240.
TreeFamiTF330481.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAAWLLGAL VVPQLLGFGH GARGAEREWE GGWGGAQEEE REREALMLKH
60 70 80 90 100
LQEALGLPAG RGDENPAGTV EGKEDWEMEE DQGEEEEEEA TPTPSSGPSP
110 120 130 140 150
SPTPEDIVTY ILGRLAGLDA GLHQLHVRLH ALDTRVVELT QGLRQLRNAA
160 170 180 190 200
GDTRDAVQAL QEAQGRAERE HGRLEGCLKG LRLGHKCFLL SRDFEAQAAA
210 220 230 240 250
QARCTARGGS LAQPADRQQM EALTRYLRAA LAPYNWPVWL GVHDRRAEGL
260 270 280 290 300
YLFENGQRVS FFAWHRSPRP ELGAQPSASP HPLSPDQPNG GTLENCVAQA
310 320
SDDGSWWDHD CQRRLYYVCE FPF
Length:323
Mass (Da):35,695
Last modified:November 1, 1999 - v1
Checksum:iD13604CDAF087427
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041P → R.
Corresponds to variant rs2303688 [ dbSNP | Ensembl ].
VAR_050116

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020044 mRNA. Translation: AAC39569.1.
AB009244 mRNA. Translation: BAA32404.1.
AF087658 Genomic DNA. Translation: AAD26533.1.
AK314141 mRNA. Translation: BAG36831.1.
CH471135 Genomic DNA. Translation: EAW71896.1.
BC005810 mRNA. Translation: AAH05810.1.
CCDSiCCDS12800.1.
RefSeqiNP_002966.1. NM_002975.2.
UniGeneiHs.512680.

Genome annotation databases

EnsembliENST00000250340; ENSP00000250340; ENSG00000105472.
GeneIDi6320.
KEGGihsa:6320.
UCSCiuc002psy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Stem cell growth factor

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020044 mRNA. Translation: AAC39569.1.
AB009244 mRNA. Translation: BAA32404.1.
AF087658 Genomic DNA. Translation: AAD26533.1.
AK314141 mRNA. Translation: BAG36831.1.
CH471135 Genomic DNA. Translation: EAW71896.1.
BC005810 mRNA. Translation: AAH05810.1.
CCDSiCCDS12800.1.
RefSeqiNP_002966.1. NM_002975.2.
UniGeneiHs.512680.

3D structure databases

ProteinModelPortaliQ9Y240.
SMRiQ9Y240. Positions 132-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112226. 36 interactions.
IntActiQ9Y240. 1 interaction.
STRINGi9606.ENSP00000250340.

PTM databases

iPTMnetiQ9Y240.
PhosphoSiteiQ9Y240.

Polymorphism and mutation databases

BioMutaiCLEC11A.
DMDMi34223087.

Proteomic databases

EPDiQ9Y240.
MaxQBiQ9Y240.
PaxDbiQ9Y240.
PeptideAtlasiQ9Y240.
PRIDEiQ9Y240.

Protocols and materials databases

DNASUi6320.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250340; ENSP00000250340; ENSG00000105472.
GeneIDi6320.
KEGGihsa:6320.
UCSCiuc002psy.4. human.

Organism-specific databases

CTDi6320.
GeneCardsiCLEC11A.
HGNCiHGNC:10576. CLEC11A.
HPAiHPA042690.
MIMi604713. gene.
neXtProtiNX_Q9Y240.
PharmGKBiPA34996.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00610000086061.
HOGENOMiHOG000273889.
HOVERGENiHBG052365.
InParanoidiQ9Y240.
KOiK17521.
OMAiFAWHRSP.
PhylomeDBiQ9Y240.
TreeFamiTF330481.

Miscellaneous databases

GeneWikiiCLEC11A.
GenomeRNAii6320.
PROiQ9Y240.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y240.
CleanExiHS_CLEC11A.
ExpressionAtlasiQ9Y240. baseline and differential.
GenevisibleiQ9Y240. HS.

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. "Molecular cloning of a new secreted sulfated mucin-like protein with a C-type lectin domain that is expressed in lymphoblastic cells."
    Bannwarth S., Giordanengo V., Lesimple J., Lefebvre J.-C.
    J. Biol. Chem. 273:1911-1916(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39; 229-243 AND 314-323, TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: Bone marrow1 Publication.
  2. "Isolation and characterization of a cDNA for human, mouse, and rat full-length stem cell growth factor, a new member of C-type lectin superfamily."
    Mio H., Kagami N., Yokokawa S., Kawai H., Nakagawa S., Takeuchi K., Sekine S., Hiraoka A.
    Biochem. Biophys. Res. Commun. 249:124-130(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Bone marrow1 Publication.
  3. "Cloning, mapping, and genomic organization of the LSLCL gene, encoding a new lymphocytic secreted mucin-like protein with a C-type lectin domain: a new model of exon shuffling."
    Bannwarth S., Giordanengo V., Grosgeorge J., Turc-Carel C., Lefebvre J.-C.
    Genomics 57:316-317(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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].
    Tissue: Heart.
  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: Skin1 Publication.
  7. "Stem cell growth factor: in situ hybridization analysis on the gene expression, molecular characterization and in vitro proliferative activity of a recombinant preparation on primitive hematopoietic progenitor cells."
    Hiraoka A., Yano K., Kagami N., Takeshige K., Mio H., Anazawa H., Sugimoto S.
    Hematol. J. 2:307-315(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Expression of LSLCL, a new C-type lectin, is closely restricted, in bone marrow, to immature neutrophils."
    Perrin C., Bayle J., Bannwarth S., Michiels J.-F., Heudier P., Lefebvre J.-C., Giordanengo V.
    C. R. Acad. Sci. III, Sci. Vie 324:1125-1132(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLC11_HUMAN
AccessioniPrimary (citable) accession number: Q9Y240
Secondary accession number(s): B2RAD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 126 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.