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Protein

Collectin-12

Gene

COLEC12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi644Calcium 1; via carbonyl oxygen1
Metal bindingi646Calcium 11
Metal bindingi650Calcium 11
Metal bindingi670Calcium 21
Metal bindingi674Calcium 21
Binding sitei691CarbohydrateBy similarity1
Metal bindingi694Calcium 31
Binding sitei694CarbohydrateBy similarity1
Metal bindingi696Calcium 31
Binding sitei696CarbohydrateBy similarity1
Metal bindingi697Calcium 21
Metal bindingi706Calcium 2; via carbonyl oxygen1
Metal bindingi706Calcium 31
Binding sitei706CarbohydrateBy similarity1
Metal bindingi707Calcium 21
Metal bindingi718Calcium 31
Binding sitei718CarbohydrateBy similarity1
Metal bindingi719Calcium 31
Binding sitei719Carbohydrate; via carbonyl oxygenBy similarity1
Metal bindingi731Calcium 11

GO - Molecular functioni

  • galactose binding Source: UniProtKB
  • low-density lipoprotein particle binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • scavenger receptor activity Source: UniProtKB
  • signaling pattern recognition receptor activity Source: UniProtKB

GO - Biological processi

  • carbohydrate mediated signaling Source: UniProtKB
  • cellular response to exogenous dsRNA Source: UniProtKB
  • defense response Source: UniProtKB
  • innate immune response Source: UniProtKB
  • phagocytosis, recognition Source: UniProtKB
  • positive regulation of cell adhesion molecule production Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • receptor-mediated endocytosis Source: Reactome
  • toll-like receptor 3 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-3000480. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:16016. COLEC12.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 37CytoplasmicSequence analysisAdd BLAST37
Transmembranei38 – 58Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini59 – 742ExtracellularSequence analysisAdd BLAST684

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • endocytic vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi81035.
OpenTargetsiENSG00000158270.
PharmGKBiPA26738.

Polymorphism and mutation databases

BioMutaiCOLEC12.
DMDMi296439391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003186811 – 742Collectin-12Add BLAST742

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...)Sequence analysis1
Glycosylationi159N-linked (GlcNAc...)Sequence analysis1
Glycosylationi168N-linked (GlcNAc...)Sequence analysis1
Glycosylationi271N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi607 ↔ 618PROSITE-ProRule annotation1 Publication
Disulfide bondi635 ↔ 730PROSITE-ProRule annotation1 Publication
Disulfide bondi708 ↔ 722PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ5KU26.
MaxQBiQ5KU26.
PaxDbiQ5KU26.
PeptideAtlasiQ5KU26.
PRIDEiQ5KU26.

PTM databases

iPTMnetiQ5KU26.
PhosphoSitePlusiQ5KU26.

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

BgeeiENSG00000158270.
CleanExiHS_CLP1.
HS_COLEC12.
GenevisibleiQ5KU26. HS.

Organism-specific databases

HPAiHPA047917.
HPA071056.

Interactioni

Subunit structurei

The extracellular domain forms a stable trimer. The extracellular domain interacts with fibrillar beta amyloid peptide.3 Publications

Protein-protein interaction databases

BioGridi123353. 32 interactors.
IntActiQ5KU26. 1 interactor.
STRINGi9606.ENSP00000383115.

Structurei

Secondary structure

1742
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi612 – 614Combined sources3
Beta strandi617 – 621Combined sources5
Helixi628 – 637Combined sources10
Helixi648 – 657Combined sources10
Beta strandi664 – 669Combined sources6
Beta strandi671 – 673Combined sources3
Turni692 – 700Combined sources9
Beta strandi708 – 711Combined sources4
Beta strandi717 – 720Combined sources4
Beta strandi726 – 733Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OX8X-ray2.50A/B/C/D607-742[»]
ProteinModelPortaliQ5KU26.
SMRiQ5KU26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5KU26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini443 – 472Collagen-like 1Add BLAST30
Domaini473 – 529Collagen-like 2Add BLAST57
Domaini530 – 589Collagen-like 3Add BLAST60
Domaini614 – 731C-type lectinPROSITE-ProRule annotationAdd BLAST118

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili73 – 141Sequence analysisAdd BLAST69
Coiled coili215 – 328Sequence analysisAdd BLAST114

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 3 collagen-like domains.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IIUI. Eukaryota.
ENOG41101BT. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111886.
HOVERGENiHBG107745.
InParanoidiQ5KU26.
KOiK10062.
OMAiEQQWIKK.
OrthoDBiEOG091G0OLC.
PhylomeDBiQ5KU26.
TreeFamiTF332426.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR008160. Collagen.
IPR016187. CTDL_fold.
[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

        10         20         30         40         50
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCALL
60 70 80 90 100
TITVAILGYK VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK
110 120 130 140 150
AISTNSELST FRSDILDLRQ QLREITEKTS KNKDTLEKLQ ASGDALVDRQ
160 170 180 190 200
SQLKETLENN SFLITTVNKT LQAYNGYVTN LQQDTSVLQG NLQNQMYSHN
210 220 230 240 250
VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND FQNLQQVFLQ
260 270 280 290 300
AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL NSFTGQMENI
310 320 330 340 350
TTISQANEQN LKDLQDLHKD AENRTAIKFN QLEERFQLFE TDIVNIISNI
360 370 380 390 400
SYTAHHLRTL TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR
410 420 430 440 450
MQQDLMRSRL DTEVANLSVI MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP
460 470 480 490 500
RGDRGSQGPP GPTGNKGQKG EKGEPGPPGP AGERGPIGPA GPPGERGGKG
510 520 530 540 550
SKGSQGPKGS RGSPGKPGPQ GSSGDPGPPG PPGKEGLPGP QGPPGFQGLQ
560 570 580 590 600
GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAVV PLALQNEPTP
610 620 630 640 650
APEDNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINTREE
660 670 680 690 700
QQWIKKQMVG RESHWIGLTD SERENEWKWL DGTSPDYKNW KAGQPDNWGH
710 720 730 740
GHGPGEDCAG LIYAGQWNDF QCEDVNNFIC EKDRETVLSS AL
Length:742
Mass (Da):81,515
Last modified:May 18, 2010 - v3
Checksum:i85A003C1D6A83949
GO

Sequence cautioni

The sequence BAB39148 differs from that shown. Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12Q → P in BAB39148 (PubMed:11162630).Curated1
Sequence conflicti16Y → F in BAB39148 (PubMed:11162630).Curated1
Sequence conflicti22Q → H in BAB39148 (PubMed:11162630).Curated1
Sequence conflicti28T → P in BAB39148 (PubMed:11162630).Curated1
Sequence conflicti31K → H in BAB39148 (PubMed:11162630).Curated1
Sequence conflicti72M → V in BAD83592 (PubMed:12761161).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03885391K → E.1 PublicationCorresponds to variant rs17855029dbSNPEnsembl.1
Natural variantiVAR_038854487I → V.Corresponds to variant rs8098850dbSNPEnsembl.1
Natural variantiVAR_038855522S → P.5 PublicationsCorresponds to variant rs2305025dbSNPEnsembl.1
Natural variantiVAR_038856606G → S.3 PublicationsCorresponds to variant rs2305027dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OX8X-ray2.50A/B/C/D607-742[»]
ProteinModelPortaliQ5KU26.
SMRiQ5KU26.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123353. 32 interactors.
IntActiQ5KU26. 1 interactor.
STRINGi9606.ENSP00000383115.

PTM databases

iPTMnetiQ5KU26.
PhosphoSitePlusiQ5KU26.

Polymorphism and mutation databases

BioMutaiCOLEC12.
DMDMi296439391.

Proteomic databases

EPDiQ5KU26.
MaxQBiQ5KU26.
PaxDbiQ5KU26.
PeptideAtlasiQ5KU26.
PRIDEiQ5KU26.

Protocols and materials databases

DNASUi81035.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000400256; ENSP00000383115; ENSG00000158270.
GeneIDi81035.
KEGGihsa:81035.
UCSCiuc002kkm.4. human.

Organism-specific databases

CTDi81035.
DisGeNETi81035.
GeneCardsiCOLEC12.
HGNCiHGNC:16016. COLEC12.
HPAiHPA047917.
HPA071056.
MIMi607621. gene.
neXtProtiNX_Q5KU26.
OpenTargetsiENSG00000158270.
PharmGKBiPA26738.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIUI. Eukaryota.
ENOG41101BT. LUCA.
GeneTreeiENSGT00820000126981.
HOGENOMiHOG000111886.
HOVERGENiHBG107745.
InParanoidiQ5KU26.
KOiK10062.
OMAiEQQWIKK.
OrthoDBiEOG091G0OLC.
PhylomeDBiQ5KU26.
TreeFamiTF332426.

Enzyme and pathway databases

ReactomeiR-HSA-3000480. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSiCOLEC12. human.
EvolutionaryTraceiQ5KU26.
GenomeRNAii81035.
PROiQ5KU26.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158270.
CleanExiHS_CLP1.
HS_COLEC12.
GenevisibleiQ5KU26. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR008160. Collagen.
IPR016187. CTDL_fold.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 108 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

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.