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Reviewed, UniProtKB/Swiss-Prot P39060 (COIA1_HUMAN)

Last modified November 25, 2008. Version 96. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Collagen alpha-1(XVIII) chain
Cleaved into the following chain:
    1- Recommended name:
            Endostatin
Gene names
Name: COL18A1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1754 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.

Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.

Subcellular location

Secreted › extracellular space › extracellular matrixBy similarity.

Tissue specificity

Present in multiple organs with highest levels in liver, lung and kidney.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Polymorphism

There is an association between a polymorphism in position 1675 and prostate cancer. Heterozygous Asn-1675 individuals have a 2.5 times increased chance of developing prostate cancer as compared with homozygous Asp-1675 individuals.

Involvement in disease

Defects in COL18A1 are a cause of Knobloch syndrome (KNO) [MIM:267750]. KNO is an autosomal recessive disorder defined by the occurrence of high myopia, vitreoretinal degeneration with retinal detachment, macular abnormalities and occipital encephalocele.

Sequence similarities

Belongs to the multiplexin collagen family.

Contains 1 FZ (frizzled) domain.

Contains 1 TSP N-terminal (TSPN) domain.

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Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39060-3)

Also known as: NC1-728;

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.
Notes: Produced by alternative promoter usage.
Isoform 2 (identifier: P39060-1)

Also known as: Long; NC-493;

The sequence of this isoform differs from the canonical sequence as follows:
     216-450: Missing.
Notes: Produced by alternative splicing of isoform 1.
Isoform 3 (identifier: P39060-2)

Also known as: Short; NC1-303;

The sequence of this isoform differs from the canonical sequence as follows:
     1-415: Missing.
     416-450: QDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAA → MAPRCPWPWPRRRRLLDVLAPLVLLLGVRAASAEP
Notes: Produced by alternative promoter usage.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 17541731Collagen alpha-1(XVIII) chain
PRO_0000005793
Chain1572 – 1754183Endostatin
PRO_0000005794

Regions

Domain329 – 446118FZ
Domain456 – 644189TSP N-terminal
Region645 – 751107Nonhelical region 1 (NC1)
Region752 – 78534Triple-helical region 1 (COL1)
Region786 – 79510Nonhelical region 2 (NC2)
Region796 – 87580Triple-helical region 2 (COL2)
Region876 – 89924Nonhelical region 3 (NC3)
Region900 – 1021122Triple-helical region 3 (COL3)
Region1022 – 104423Nonhelical region 4 (NC4)
Region1045 – 112783Triple-helical region 4 (COL4)
Region1128 – 114114Nonhelical region 5 (NC5)
Region1142 – 118342Triple-helical region 5 (COL5)
Region1184 – 119613Nonhelical region 6 (NC6)
Region1197 – 126973Triple-helical region 6 (COL6)
Region1270 – 127910Nonhelical region 7 (NC7)
Region1280 – 131233Triple-helical region 7 (COL7)
Region1313 – 132412Nonhelical region 8 (NC8)
Region1325 – 134622Triple-helical region 8 (COL8)
Region1347 – 13537Nonhelical region 9 (NC9)
Region1354 – 141158Triple-helical region 9 (COL9)
Region1412 – 142413Nonhelical region 10 (NC10)
Region1425 – 144218Triple-helical region 10 (COL10)
Region1443 – 1754312Nonhelical region 11 (NC11)
Motif1330 – 13323Cell attachment site Potential

Sites

Metal binding15721Zinc
Metal binding15741Zinc
Metal binding15821Zinc
Metal binding16471Zinc

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1291N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation15671O-linked (GalNAc...)
CAR_000150
Disulfide bond334 ↔ 397 By similarity
Disulfide bond344 ↔ 390 By similarity
Disulfide bond381 ↔ 419 By similarity
Disulfide bond408 ↔ 443 By similarity
Disulfide bond412 ↔ 432 By similarity
Disulfide bond1604 ↔ 1744 By similarity
Disulfide bond1706 ↔ 1736 By similarity

Natural variations

Alternative sequence1 – 415415Missing in isoform 3.
VSP_023130
Alternative sequence216 – 450235Missing in isoform 2.
VSP_023131
Alternative sequence416 – 45035QDACW…IGPAA → MAPRCPWPWPRRRRLLDVLA PLVLLLGVRAASAEP in isoform 3.
VSP_023132
Natural variant491Q → L
VAR_018053
Natural variant1111G → R
VAR_018054
Natural variant10761V → I
VAR_018055
Natural variant11211P → R
VAR_018056
Natural variant16751D → N Decreased activity for binding laminin; increased risk of developing prostate cancer; in compound heterozygotes may cause Knobloch syndrome when in combination with a frameshift/truncating mutation.
VAR_012709

Experimental info

Sequence conflict2991R → K in AAR83296. Ref.2
Sequence conflict6631S → F in AAC39658 and AAC39659. Ref.1
Sequence conflict11121V → L in AAA51864. Ref.5
Sequence conflict11471P → R in AAA51864. Ref.5
Sequence conflict11681R → L in AAA51864. Ref.5
Sequence conflict12101P → L in AAA51864. Ref.5
Sequence conflict12991A → P in AAA51864. Ref.5
Sequence conflict13191L → K in AAA51864. Ref.5
Sequence conflict13551P → A in AAA51864. Ref.5
Sequence conflict13581P → A in AAA51864. Ref.5
Sequence conflict1362 – 13643Missing in AAC39658 and AAC39659. Ref.1
Sequence conflict1362 – 13643Missing in AAR83296, AAR83297 and AAR83298. Ref.2
Sequence conflict1362 – 13643Missing in AAH33715 and AAH63833. Ref.4
Sequence conflict1362 – 13643Missing in AAA51864. Ref.5
Sequence conflict14441G → GQ in AAA51864. Ref.5
Sequence conflict15421R → G in AAA51864. Ref.5
Sequence conflict15521A → G in AAA51864. Ref.5
Sequence conflict1561 – 15622LR → CG in AAA51864. Ref.5
Sequence conflict16811R → T in AAF01310. Ref.7
Sequence conflict16851W → R in AAK50626. Ref.8
Sequence conflict17211S → Y in AAF01310. Ref.7
Sequence conflict17361C → S in AAK50626. Ref.8

Secondary structure

1 .............................. 1754
Helix Strand Turn

Details...