O75829 (LECT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leukocyte cell-derived chemotaxin 1

Cleaved into the following 2 chains:

1. Chondrosurfactant protein
   Short name=CH-SP
2. Chondromodulin-1
   Alternative name(s):
   Chondromodulin-I
   Short name=ChM-I

Gene names

Name:	LECT1
Synonyms:	CHMI

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subcellular location	Chondromodulin-1: Secreted. Note: Accumulated in the inter-territorial matrix of cartilage. Chondrosurfactant protein: Endomembrane system; Single-pass membrane protein Potential.
Tissue specificity	Cartilage specific. Weakly expressed in chondrosarcoma.
Developmental stage	Expressed at 9 weeks in developing cartilagenous bone rudiments.
Post-translational modification	After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein.
Sequence similarities	Belongs to the chondromodulin-1 family. Contains 1 BRICHOS domain.

Ontologies

Keywords
Biological process	Chondrogenesis Differentiation
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cartilage development Inferred from electronic annotation. Source: UniProtKB-KW proteoglycan metabolic process Traceable author statement. Source: ProtInc
Cellular component	endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75829-1)

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.

Isoform 2 (identifier: O75829-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 210	210	Chondrosurfactant protein By similarity		PRO_0000005346
	Propeptide	211 – 214	4	Potential		PRO_0000005347
	Chain	215 – 334	120	Chondromodulin-1		PRO_0000005348
Regions
	Transmembrane	45 – 65	21	Helical; Potential
	Domain	104 – 201	98	BRICHOS
Amino acid modifications
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Disulfide bond	282 ↔ 286		By similarity
	Disulfide bond	283 ↔ 323		By similarity
Natural variations
	Alternative sequence	264	1	Missing in isoform 2.		VSP_038380
	Natural variant	116	1	F → L. Corresponds to variant rs3742298 [ dbSNP | Ensembl ].		VAR_048719
	Natural variant	175	1	V → I. Corresponds to variant rs7330220 [ dbSNP | Ensembl ].		VAR_024413

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 9E2393111F9D4FE5	FASTA	334	37,102
	10 20 30 40 50 60 MTENSDKVPI ALVGPDDVEF CSPPAYATLT VKPSSPARLL KVGAVVLISG AVLLLFGAIG 70 80 90 100 110 120 AFYFWKGSDS HIYNVHYTMS INGKLQDGSM EIDAGNNLET FKMGSGAEEA IAVNDFQNGI 130 140 150 160 170 180 TGIRFAGGEK CYIKAQVKAR IPEVGAVTKQ SISSKLEGKI MPVKYEENSL IWVAVDQPVK 190 200 210 220 230 240 DNSFLSSKVL ELCGDLPIFW LKPTYPKEIQ RERREVVRKI VPTTTKRPHS GPRSNPGAGR 250 260 270 280 290 300 LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL 310 320 330 GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV
	Isoform 2 [UniParc]. Checksum: 40A81C68ADC65FDC	FASTA	333	36,974
	10 20 30 40 50 60 MTENSDKVPI ALVGPDDVEF CSPPAYATLT VKPSSPARLL KVGAVVLISG AVLLLFGAIG 70 80 90 100 110 120 AFYFWKGSDS HIYNVHYTMS INGKLQDGSM EIDAGNNLET FKMGSGAEEA IAVNDFQNGI 130 140 150 160 170 180 TGIRFAGGEK CYIKAQVKAR IPEVGAVTKQ SISSKLEGKI MPVKYEENSL IWVAVDQPVK 190 200 210 220 230 240 DNSFLSSKVL ELCGDLPIFW LKPTYPKEIQ RERREVVRKI VPTTTKRPHS GPRSNPGAGR 250 260 270 280 290 300 LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG 310 320 330 GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of cartilage-specific functional matrix chondromodulin-I mRNA in rabbit growth plate chondrocytes and its responsiveness to growth stimuli in vitro." Shukunami C., Hiraki Y. Biochem. Biophys. Res. Commun. 249:885-890(1998) [PubMed: 9731231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Chondrosarcoma.
[2]	"Molecular cloning of human chondromodulin-I, a cartilage-derived growth modulating factor, and its expression in Chinese hamster ovary cells." Hiraki Y., Mitsui K., Endo N., Takahashi K., Hayami T., Inoue H., Shukunami C., Tokunaga K., Kono T., Yamada M., Takahashi H.E., Kondo J. Eur. J. Biochem. 260:869-878(1999) [PubMed: 10103018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Chondrosarcoma.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	"Human chondromodulin-1 gene promoter." Ozono K. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[7]	"Specific loss of chondromodulin-I gene expression in chondrosarcoma and the suppression of tumor angiogenesis and growth by its recombinant protein in vivo." Hayami T., Shukunami C., Mitsui K., Endo N., Tokunaga K., Kondo J., Takahashi H.E., Hiraki Y. FEBS Lett. 458:436-440(1999) [PubMed: 10570955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 215-334 (ISOFORM 1).
[8]	"Chondromodulin-I as a novel cartilage-specific growth-modulating factor." Hiraki Y., Shukunami C. Pediatr. Nephrol. 14:602-605(2000) [PubMed: 10912526] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00027162. IPI00553085.
RefSeq	NP_001011705.1. NM_001011705.1. NP_008946.1. NM_007015.2.
UniGene	Hs.421391.
3D structure databases
ProteinModelPortal	O75829.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75829. 2 interactions.
STRING	O75829.
Proteomic databases
PRIDE	O75829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377962; ENSP00000367198; ENSG00000136110.
GeneID	11061.
KEGG	hsa:11061.
UCSC	uc001vhf.1. human.
Organism-specific databases
CTD	11061.
GeneCards	GC13M053277.
HGNC	HGNC:17005. LECT1.
HPA	HPA010510.
MIM	605147. gene.
neXtProt	NX_O75829.
PharmGKB	PA134897668.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05074.
GeneTree	ENSGT00480000042679.
HOGENOM	HBG444203.
HOVERGEN	HBG004387.
InParanoid	O75829.
OMA	EGEGMTF.
OrthoDB	EOG461446.
PhylomeDB	O75829.
Gene expression databases
ArrayExpress	O75829.
Bgee	O75829.
CleanEx	HS_LECT1.
Genevestigator	O75829.
GermOnline	ENSG00000136110. Homo sapiens.
Family and domain databases
InterPro	IPR007084. BRICHOS_dom. [Graphical view]
Pfam	PF04089. BRICHOS. 1 hit. [Graphical view]
SMART	SM01039. BRICHOS. 1 hit. [Graphical view]
PROSITE	PS50869. BRICHOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	42031.
PMAP-CutDB	O75829.
SOURCE	Search...

Entry information

Entry name

LECT1_HUMAN

Accession

Primary (citable) accession number: O75829
Secondary accession number(s): Q5TAM4, Q8TAY6, Q9UM18

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.