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Protein

Leukocyte cell-derived chemotaxin 1

Gene

LECT1

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

Functioni

Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization.1 Publication

GO - Biological processi

  • cartilage development Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • negative regulation of angiogenesis Source: UniProtKB
  • proteoglycan metabolic process Source: ProtInc
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Chondrogenesis, Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Leukocyte cell-derived chemotaxin 1
Cleaved into the following 2 chains:
Chondrosurfactant protein
Short name:
CH-SP
Alternative name(s):
Chondromodulin-I
Short name:
ChM-I
Gene namesi
Name:LECT1
Synonyms:CHMI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17005. LECT1.

Subcellular locationi

Chondromodulin-1 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei45 – 6521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134897668.

Polymorphism and mutation databases

BioMutaiLECT1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Chondrosurfactant proteinBy similarityPRO_0000005346Add
BLAST
Propeptidei211 – 2144Sequence analysisPRO_0000005347
Chaini215 – 334120Chondromodulin-1PRO_0000005348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi131 ↔ 193By similarity
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi282 ↔ 286By similarity
Disulfide bondi283 ↔ 323By similarity
Disulfide bondi293 ↔ 317By similarity
Disulfide bondi297 ↔ 313By similarity

Post-translational modificationi

After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO75829.
PeptideAtlasiO75829.
PRIDEiO75829.

PTM databases

iPTMnetiO75829.
PhosphoSiteiO75829.

Miscellaneous databases

PMAP-CutDBO75829.

Expressioni

Tissue specificityi

Detected in cartilage and cardiac valves (at protein level). Detected in the laminae fibrosa, spongiosa and ventricularis layers of normal cardiac valves (at protein level). Expression is decreased cardiac valves of patients with valvular heart disease (at protein level). Weakly expressed in chondrosarcoma.1 Publication

Developmental stagei

Expressed at 9 weeks in developing cartilagenous bone rudiments.

Gene expression databases

BgeeiENSG00000136110.
CleanExiHS_LECT1.
ExpressionAtlasiO75829. baseline and differential.
GenevisibleiO75829. HS.

Organism-specific databases

HPAiHPA010510.

Interactioni

Protein-protein interaction databases

BioGridi116245. 5 interactions.
IntActiO75829. 5 interactions.
STRINGi9606.ENSP00000367198.

Structurei

3D structure databases

ProteinModelPortaliO75829.
SMRiO75829. Positions 96-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 20198BRICHOSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the chondromodulin-1 family.Curated
Contains 1 BRICHOS domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFAS. Eukaryota.
ENOG410YVHU. LUCA.
GeneTreeiENSGT00480000042679.
HOGENOMiHOG000234812.
HOVERGENiHBG004387.
InParanoidiO75829.
OMAiIMPCSWW.
OrthoDBiEOG091G09DW.
PhylomeDBiO75829.
TreeFamiTF329712.

Family and domain databases

InterProiIPR007084. BRICHOS_dom.
[Graphical view]
PfamiPF04089. BRICHOS. 1 hit.
[Graphical view]
SMARTiSM01039. BRICHOS. 1 hit.
[Graphical view]
PROSITEiPS50869. BRICHOS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75829-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MTENSDKVPI ALVGPDDVEF CSPPAYATLT VKPSSPARLL KVGAVVLISG
60 70 80 90 100
AVLLLFGAIG AFYFWKGSDS HIYNVHYTMS INGKLQDGSM EIDAGNNLET
110 120 130 140 150
FKMGSGAEEA IAVNDFQNGI TGIRFAGGEK CYIKAQVKAR IPEVGAVTKQ
160 170 180 190 200
SISSKLEGKI MPVKYEENSL IWVAVDQPVK DNSFLSSKVL ELCGDLPIFW
210 220 230 240 250
LKPTYPKEIQ RERREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ
260 270 280 290 300
EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL
310 320 330
GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV
Length:334
Mass (Da):37,102
Last modified:November 1, 1998 - v1
Checksum:i9E2393111F9D4FE5
GO
Isoform 2 (identifier: O75829-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     264-264: Missing.

Note: No experimental confirmation available.
Show »
Length:333
Mass (Da):36,974
Checksum:i40A81C68ADC65FDC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161F → L.
Corresponds to variant rs3742298 [ dbSNP | Ensembl ].
VAR_048719
Natural varianti175 – 1751V → I.
Corresponds to variant rs7330220 [ dbSNP | Ensembl ].
VAR_024413

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei264 – 2641Missing in isoform 2. 1 PublicationVSP_038380

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006000 mRNA. Translation: BAA33443.1.
AF050147 Genomic DNA. Translation: AAC98971.1.
CR541910 mRNA. Translation: CAG46708.1.
AL139085, AL139089 Genomic DNA. Translation: CAI14108.1.
AL139089, AL139085 Genomic DNA. Translation: CAI17074.1.
BC025659 mRNA. Translation: AAH25659.1.
AB021290 Genomic DNA. Translation: BAA77384.1.
AB005999 mRNA. Translation: BAA86262.1.
CCDSiCCDS45051.1. [O75829-2]
CCDS9437.1. [O75829-1]
RefSeqiNP_001011705.1. NM_001011705.1. [O75829-2]
NP_008946.1. NM_007015.2. [O75829-1]
UniGeneiHs.421391.

Genome annotation databases

EnsembliENST00000377962; ENSP00000367198; ENSG00000136110. [O75829-1]
ENST00000448904; ENSP00000388576; ENSG00000136110. [O75829-2]
GeneIDi11061.
KEGGihsa:11061.
UCSCiuc001vhf.4. human. [O75829-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006000 mRNA. Translation: BAA33443.1.
AF050147 Genomic DNA. Translation: AAC98971.1.
CR541910 mRNA. Translation: CAG46708.1.
AL139085, AL139089 Genomic DNA. Translation: CAI14108.1.
AL139089, AL139085 Genomic DNA. Translation: CAI17074.1.
BC025659 mRNA. Translation: AAH25659.1.
AB021290 Genomic DNA. Translation: BAA77384.1.
AB005999 mRNA. Translation: BAA86262.1.
CCDSiCCDS45051.1. [O75829-2]
CCDS9437.1. [O75829-1]
RefSeqiNP_001011705.1. NM_001011705.1. [O75829-2]
NP_008946.1. NM_007015.2. [O75829-1]
UniGeneiHs.421391.

3D structure databases

ProteinModelPortaliO75829.
SMRiO75829. Positions 96-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116245. 5 interactions.
IntActiO75829. 5 interactions.
STRINGi9606.ENSP00000367198.

PTM databases

iPTMnetiO75829.
PhosphoSiteiO75829.

Polymorphism and mutation databases

BioMutaiLECT1.

Proteomic databases

PaxDbiO75829.
PeptideAtlasiO75829.
PRIDEiO75829.

Protocols and materials databases

DNASUi11061.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377962; ENSP00000367198; ENSG00000136110. [O75829-1]
ENST00000448904; ENSP00000388576; ENSG00000136110. [O75829-2]
GeneIDi11061.
KEGGihsa:11061.
UCSCiuc001vhf.4. human. [O75829-1]

Organism-specific databases

CTDi11061.
GeneCardsiLECT1.
HGNCiHGNC:17005. LECT1.
HPAiHPA010510.
MIMi605147. gene.
neXtProtiNX_O75829.
PharmGKBiPA134897668.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFAS. Eukaryota.
ENOG410YVHU. LUCA.
GeneTreeiENSGT00480000042679.
HOGENOMiHOG000234812.
HOVERGENiHBG004387.
InParanoidiO75829.
OMAiIMPCSWW.
OrthoDBiEOG091G09DW.
PhylomeDBiO75829.
TreeFamiTF329712.

Miscellaneous databases

GeneWikiiLECT1.
GenomeRNAii11061.
PMAP-CutDBO75829.
PROiO75829.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136110.
CleanExiHS_LECT1.
ExpressionAtlasiO75829. baseline and differential.
GenevisibleiO75829. HS.

Family and domain databases

InterProiIPR007084. BRICHOS_dom.
[Graphical view]
PfamiPF04089. BRICHOS. 1 hit.
[Graphical view]
SMARTiSM01039. BRICHOS. 1 hit.
[Graphical view]
PROSITEiPS50869. BRICHOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLECT1_HUMAN
AccessioniPrimary (citable) accession number: O75829
Secondary accession number(s): Q5TAM4, Q8TAY6, Q9UM18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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.