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Protein

Leukocyte cell-derived chemotaxin 1

Gene

Lect1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Biological processi

  • cartilage development Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • negative regulation of angiogenesis Source: RGD
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620176. Lect1.

Subcellular locationi

Chondromodulin-1 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei46 – 6621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Chondrosurfactant proteinBy similarityPRO_0000005352Add
BLAST
Propeptidei211 – 2144By similarityPRO_0000005353
Chaini215 – 334120Chondromodulin-1By similarityPRO_0000005354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi132 ↔ 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.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO70367.
PRIDEiO70367.

Expressioni

Tissue specificityi

Detected in cartilage, cardiac valves and valvular interstitial cells (at protein level). Expressed in eye.1 Publication

Developmental stagei

Expression first detected in heart at E9.5 and persisted in the adult.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 20197BRICHOSPROSITE-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.
HOGENOMiHOG000234812.
HOVERGENiHBG004387.
InParanoidiO70367.
PhylomeDBiO70367.

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]

Sequencei

Sequence statusi: Complete.

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

O70367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTENSDKVPI TMVGPEDVEF CSPPAYATVT VKPSGSPTRL LKVGAVVLIS
60 70 80 90 100
GAVLLLFGAI GAFYFWKGND NHIYNVHYTM SINGRLQDAS MEIDAANNLE
110 120 130 140 150
TFKMGSGAEE AIEVNDFQNG ITGIRFAGGE KCYIKAQVKA RIPEVSTGTK
160 170 180 190 200
QSISELEGKI MPVKYEENSL IWVAVDQPVK DNSFLSSKIL EFCGDLPIFW
210 220 230 240 250
LKPMYPKEIP RERREVVRSS APSTTRRPHS EPRGNAGPGR LSNRTRPSVQ
260 270 280 290 300
DDEEPFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL
310 320 330
GGYYPWPYNY QGCRSACRVV MPCSWWVARI LGMV
Length:334
Mass (Da):37,387
Last modified:August 1, 1998 - v1
Checksum:iDB865E515952A4CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051425 mRNA. Translation: AAC05574.1.
RefSeqiNP_110481.1. NM_030854.1.
UniGeneiRn.9900.

Genome annotation databases

GeneIDi81512.
KEGGirno:81512.
UCSCiRGD:620176. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051425 mRNA. Translation: AAC05574.1.
RefSeqiNP_110481.1. NM_030854.1.
UniGeneiRn.9900.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017400.

Proteomic databases

PaxDbiO70367.
PRIDEiO70367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81512.
KEGGirno:81512.
UCSCiRGD:620176. rat.

Organism-specific databases

CTDi11061.
RGDi620176. Lect1.

Phylogenomic databases

eggNOGiENOG410IFAS. Eukaryota.
ENOG410YVHU. LUCA.
HOGENOMiHOG000234812.
HOVERGENiHBG004387.
InParanoidiO70367.
PhylomeDBiO70367.

Miscellaneous databases

PROiO70367.

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...

Publicationsi

  1. "Expression and localization of angiogenic inhibitory factor, chondromodulin-I, in adult rat eye."
    Funaki H., Sawaguchi S., Yaoeda K., Koyama Y., Yaoita E., Funaki S., Shirakashi M., Oshima Y., Shukunami C., Hiraki Y., Abe H., Yamamoto T.
    Invest. Ophthalmol. Vis. Sci. 42:1193-1200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar Kyoto.
    Tissue: Cartilage.
  2. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiLECT1_RAT
AccessioniPrimary (citable) accession number: O70367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.