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Q5KU26

- COL12_HUMAN

UniProt

Q5KU26 - COL12_HUMAN

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Protein
Collectin-12
Gene
COLEC12, CLP1, NSR2, SCARA4, SRCL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid beta in Alzheimer disease.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi644 – 6441Calcium 1; via carbonyl oxygen
Metal bindingi646 – 6461Calcium 1
Metal bindingi650 – 6501Calcium 1
Metal bindingi670 – 6701Calcium 2
Metal bindingi674 – 6741Calcium 2
Binding sitei691 – 6911Carbohydrate By similarity
Metal bindingi694 – 6941Calcium 3
Binding sitei694 – 6941Carbohydrate By similarity
Metal bindingi696 – 6961Calcium 3
Binding sitei696 – 6961Carbohydrate By similarity
Metal bindingi697 – 6971Calcium 2
Metal bindingi706 – 7061Calcium 2; via carbonyl oxygen
Metal bindingi706 – 7061Calcium 3
Binding sitei706 – 7061Carbohydrate By similarity
Metal bindingi707 – 7071Calcium 2
Metal bindingi718 – 7181Calcium 3
Binding sitei718 – 7181Carbohydrate By similarity
Metal bindingi719 – 7191Calcium 3
Binding sitei719 – 7191Carbohydrate; via carbonyl oxygen By similarity
Metal bindingi731 – 7311Calcium 1

GO - Molecular functioni

  1. galactose binding Source: UniProtKB
  2. low-density lipoprotein particle binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. scavenger receptor activity Source: UniProtKB
  5. signaling pattern recognition receptor activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate mediated signaling Source: UniProtKB
  2. defense response Source: UniProtKB
  3. innate immune response Source: UniProtKB
  4. pattern recognition receptor signaling pathway Source: GOC
  5. phagocytosis, recognition Source: UniProtKB
  6. protein homooligomerization Source: UniProtKB
  7. receptor-mediated endocytosis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163699. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Collectin-12
Alternative name(s):
Collectin placenta protein 1
Short name:
CL-P1
Short name:
hCL-P1
Nurse cell scavenger receptor 2
Scavenger receptor class A member 4
Scavenger receptor with C-type lectin
Gene namesi
Name:COLEC12
Synonyms:CLP1, NSR2, SCARA4, SRCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:16016. COLEC12.

Subcellular locationi

Membrane; Single-pass type II membrane protein
Note: Forms clusters on the cell surface.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3737Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei38 – 5821Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini59 – 742684Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. endocytic vesicle membrane Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. integral component of membrane Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Collectin-12
PRO_0000318681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi159 – 1591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi168 – 1681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi271 – 2711N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi607 ↔ 6181 Publication
Disulfide bondi635 ↔ 7301 Publication
Disulfide bondi708 ↔ 7221 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ5KU26.
PaxDbiQ5KU26.
PRIDEiQ5KU26.

PTM databases

PhosphoSiteiQ5KU26.

Expressioni

Tissue specificityi

Expressed in perivascular macrophages. Expressed in plaques-surrounding reactive astrocytes and in perivascular astrocytes associated with cerebral amyloid angiopathy (CAA) in the temporal cortex of Alzheimer patient (at protein level). Strongly expressed in placenta. Moderately expressed in heart, skeletal muscle, small intestine and lung. Weakly expressed in brain, colon, thymus and kidney. Expressed in nurse-like cells. Expressed in reactive astrocytes and vascular/perivascular cells in the brain of Alzheimer patient.4 Publications

Gene expression databases

BgeeiQ5KU26.
CleanExiHS_CLP1.
HS_COLEC12.
GenevestigatoriQ5KU26.

Organism-specific databases

HPAiHPA047917.

Interactioni

Subunit structurei

The extracellular domain forms a stable trimer. The extracellular domain interacts with fibrillar beta amyloid peptide.2 Publications

Protein-protein interaction databases

BioGridi123353. 2 interactions.
IntActiQ5KU26. 1 interaction.
STRINGi9606.ENSP00000383115.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi612 – 6143
Beta strandi617 – 6215
Helixi628 – 63710
Helixi648 – 65710
Beta strandi664 – 6696
Beta strandi671 – 6733
Turni692 – 7009
Beta strandi708 – 7114
Beta strandi717 – 7204
Beta strandi726 – 7338

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OX8X-ray2.50A/B/C/D607-742[»]
ProteinModelPortaliQ5KU26.
SMRiQ5KU26. Positions 607-734.

Miscellaneous databases

EvolutionaryTraceiQ5KU26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 47230Collagen-like 1
Add
BLAST
Domaini473 – 52957Collagen-like 2
Add
BLAST
Domaini530 – 58960Collagen-like 3
Add
BLAST
Domaini614 – 731118C-type lectin
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili73 – 14169 Reviewed prediction
Add
BLAST
Coiled coili215 – 328114 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Collagen, Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG147335.
HOGENOMiHOG000111886.
HOVERGENiHBG107745.
InParanoidiQ5KU26.
KOiK10062.
OMAiEQQWIKK.
OrthoDBiEOG74XS65.
PhylomeDBiQ5KU26.
TreeFamiTF332426.

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.
IPR008160. Collagen.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF00059. 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.

Q5KU26-1 [UniParc]FASTAAdd to Basket

« Hide

MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCALL    50
TITVAILGYK VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK 100
AISTNSELST FRSDILDLRQ QLREITEKTS KNKDTLEKLQ ASGDALVDRQ 150
SQLKETLENN SFLITTVNKT LQAYNGYVTN LQQDTSVLQG NLQNQMYSHN 200
VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND FQNLQQVFLQ 250
AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL NSFTGQMENI 300
TTISQANEQN LKDLQDLHKD AENRTAIKFN QLEERFQLFE TDIVNIISNI 350
SYTAHHLRTL TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR 400
MQQDLMRSRL DTEVANLSVI MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP 450
RGDRGSQGPP GPTGNKGQKG EKGEPGPPGP AGERGPIGPA GPPGERGGKG 500
SKGSQGPKGS RGSPGKPGPQ GSSGDPGPPG PPGKEGLPGP QGPPGFQGLQ 550
GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAVV PLALQNEPTP 600
APEDNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINTREE 650
QQWIKKQMVG RESHWIGLTD SERENEWKWL DGTSPDYKNW KAGQPDNWGH 700
GHGPGEDCAG LIYAGQWNDF QCEDVNNFIC EKDRETVLSS AL 742
Length:742
Mass (Da):81,515
Last modified:May 18, 2010 - v3
Checksum:i85A003C1D6A83949
GO

Sequence cautioni

The sequence BAB39148.1 differs from that shown. Reason: Probable cloning artifact.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911K → E.1 Publication
Corresponds to variant rs17855029 [ dbSNP | Ensembl ].
VAR_038853
Natural varianti487 – 4871I → V.
Corresponds to variant rs8098850 [ dbSNP | Ensembl ].
VAR_038854
Natural varianti522 – 5221S → P.5 Publications
Corresponds to variant rs2305025 [ dbSNP | Ensembl ].
VAR_038855
Natural varianti606 – 6061G → S.3 Publications
Corresponds to variant rs2305027 [ dbSNP | Ensembl ].
VAR_038856

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121Q → P in BAB39148. 1 Publication
Sequence conflicti16 – 161Y → F in BAB39148. 1 Publication
Sequence conflicti22 – 221Q → H in BAB39148. 1 Publication
Sequence conflicti28 – 281T → P in BAB39148. 1 Publication
Sequence conflicti31 – 311K → H in BAB39148. 1 Publication
Sequence conflicti72 – 721M → V in BAD83592. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB038518 mRNA. Translation: BAB39147.1.
AB052103 mRNA. Translation: BAB39148.1. Sequence problems.
AB005145 mRNA. Translation: BAB72147.1.
AB034251 mRNA. Translation: BAD83592.1.
AP000915 Genomic DNA. No translation available.
AP005240 Genomic DNA. No translation available.
BC060789 mRNA. Translation: AAH60789.1.
AL713657 mRNA. Translation: CAD28466.1.
CCDSiCCDS32782.1.
PIRiJC7595.
RefSeqiNP_569057.1. NM_130386.2.
UniGeneiHs.464422.

Genome annotation databases

EnsembliENST00000400256; ENSP00000383115; ENSG00000158270.
GeneIDi81035.
KEGGihsa:81035.
UCSCiuc002kkm.3. human.

Polymorphism databases

DMDMi296439391.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB038518 mRNA. Translation: BAB39147.1 .
AB052103 mRNA. Translation: BAB39148.1 . Sequence problems.
AB005145 mRNA. Translation: BAB72147.1 .
AB034251 mRNA. Translation: BAD83592.1 .
AP000915 Genomic DNA. No translation available.
AP005240 Genomic DNA. No translation available.
BC060789 mRNA. Translation: AAH60789.1 .
AL713657 mRNA. Translation: CAD28466.1 .
CCDSi CCDS32782.1.
PIRi JC7595.
RefSeqi NP_569057.1. NM_130386.2.
UniGenei Hs.464422.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OX8 X-ray 2.50 A/B/C/D 607-742 [» ]
ProteinModelPortali Q5KU26.
SMRi Q5KU26. Positions 607-734.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123353. 2 interactions.
IntActi Q5KU26. 1 interaction.
STRINGi 9606.ENSP00000383115.

PTM databases

PhosphoSitei Q5KU26.

Polymorphism databases

DMDMi 296439391.

Proteomic databases

MaxQBi Q5KU26.
PaxDbi Q5KU26.
PRIDEi Q5KU26.

Protocols and materials databases

DNASUi 81035.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000400256 ; ENSP00000383115 ; ENSG00000158270 .
GeneIDi 81035.
KEGGi hsa:81035.
UCSCi uc002kkm.3. human.

Organism-specific databases

CTDi 81035.
GeneCardsi GC18M000309.
HGNCi HGNC:16016. COLEC12.
HPAi HPA047917.
MIMi 607621. gene.
neXtProti NX_Q5KU26.
PharmGKBi PA26738.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG147335.
HOGENOMi HOG000111886.
HOVERGENi HBG107745.
InParanoidi Q5KU26.
KOi K10062.
OMAi EQQWIKK.
OrthoDBi EOG74XS65.
PhylomeDBi Q5KU26.
TreeFami TF332426.

Enzyme and pathway databases

Reactomei REACT_163699. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSi COLEC12. human.
EvolutionaryTracei Q5KU26.
GenomeRNAii 81035.
NextBioi 71376.
PROi Q5KU26.
SOURCEi Search...

Gene expression databases

Bgeei Q5KU26.
CleanExi HS_CLP1.
HS_COLEC12.
Genevestigatori Q5KU26.

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.
IPR008160. Collagen.
[Graphical view ]
Pfami PF01391. Collagen. 2 hits.
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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family."
    Nakamura K., Funakoshi H., Miyamoto K., Tokunaga F., Nakamura T.
    Biochem. Biophys. Res. Commun. 280:1028-1035(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PRO-522 AND SER-606.
    Tissue: Placenta.
  2. "The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells."
    Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Keshi H., Sakai Y., Fukuoh A., Sakamoto T., Itabe H., Suzutani T., Ogasawara M., Yoshida I., Wakamiya N.
    J. Biol. Chem. 276:44222-44228(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT PRO-522.
    Tissue: Lung and Placenta.
  3. "SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen."
    Yoshida T., Tsuruta Y., Iwasaki M., Yamane S., Ochi T., Suzuki R.
    J. Biochem. 133:271-277(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT PRO-522.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANTS GLU-91; PRO-522 AND SER-606.
    Tissue: Placenta.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-742.
    Tissue: Brain.
  7. "Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene."
    Ohmori H., Makita Y., Funamizu M., Chiba S., Ohtani K., Suzuki Y., Wakamiya N., Hata A.
    J. Hum. Genet. 48:82-85(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-522 AND SER-606.
  8. "Selective binding of the scavenger receptor C-type lectin to Lewis X trisaccharide and related glycan ligands."
    Coombs P.J., Graham S.A., Drickamer K., Taylor M.E.
    J. Biol. Chem. 280:22993-22999(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Possible role of scavenger receptor SRCL in the clearance of amyloid-beta in Alzheimer's disease."
    Nakamura K., Ohya W., Funakoshi H., Sakaguchi G., Kato A., Takeda M., Kudo T., Nakamura T.
    J. Neurosci. Res. 84:874-890(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FIBRILLAR BETA AMYLOID PEPTIDE, FUNCTION IN CLEARANCE OF AMYLOID BETA, TISSUE SPECIFICITY.
  10. "Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis X by a novel mechanism."
    Feinberg H., Taylor M.E., Weis W.I.
    J. Biol. Chem. 282:17250-17258(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 603-742 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.

Entry informationi

Entry nameiCOL12_HUMAN
AccessioniPrimary (citable) accession number: Q5KU26
Secondary accession number(s): Q6P9F2
, Q8TCR2, Q8WZA4, Q9BY85, Q9BYH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 86 of the entry and version 3 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 18
    Human chromosome 18: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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