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P39060 (COIA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XVIII) chain

Cleaved into the following chain:

  1. Endostatin
Gene names
Name:COL18A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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

Secretedextracellular spaceextracellular matrix By 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) of the triple-helical regions are hydroxylated.

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

Knobloch syndrome 1 (KNO1) [MIM:267750]: A developmental disorder primarily characterized by typical eye abnormalities, including high myopia, cataracts, dislocated lens, vitreoretinal degeneration, and retinal detachment, with occipital skull defects, which can range from occipital encephalocele to occult cutis aplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11

Sequence similarities

Belongs to the multiplexin collagen family.

Contains 1 FZ (frizzled) domain.

Contains 1 laminin G-like domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainCollagen
Repeat
Signal
   LigandMetal-binding
Zinc
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

collagen catabolic process

Traceable author statement. Source: Reactome

endothelial cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Traceable author statement PubMed 9008168. Source: ProtInc

organ morphogenesis

Traceable author statement Ref.11. Source: ProtInc

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to hydrostatic pressure

Inferred from electronic annotation. Source: Ensembl

visual perception

Traceable author statement Ref.11. Source: ProtInc

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

collagen trimer

Traceable author statement Ref.11. Source: ProtInc

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 16269408. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17615292PubMed 19542224PubMed 19877579PubMed 24117177. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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.
Note: 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.
Note: 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
Note: Produced by alternative promoter usage.

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 – 644189Laminin G-like
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. Ref.13
Corresponds to variant rs61735029 [ dbSNP | Ensembl ].
VAR_018053
Natural variant1111G → R. Ref.13
Corresponds to variant rs114139997 [ dbSNP | Ensembl ].
VAR_018054
Natural variant2881A → T.
Corresponds to variant rs11702494 [ dbSNP | Ensembl ].
VAR_059232
Natural variant3791T → M.
Corresponds to variant rs8133886 [ dbSNP | Ensembl ].
VAR_061115
Natural variant10761V → I. Ref.1 Ref.2 Ref.4 Ref.12 Ref.13
Corresponds to variant rs62000962 [ dbSNP | Ensembl ].
VAR_018055
Natural variant11211P → R. Ref.5 Ref.13 Ref.14
Corresponds to variant rs79980197 [ dbSNP | Ensembl ].
VAR_018056
Natural variant11951Q → H.
Corresponds to variant rs2230693 [ dbSNP | Ensembl ].
VAR_059233
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. Ref.2 Ref.7 Ref.12 Ref.13
Corresponds to variant rs12483377 [ dbSNP | Ensembl ].
VAR_012709

Experimental info

Sequence conflict2991R → K in AAR83296. Ref.2
Sequence conflict6631S → F in AAC39658. Ref.1
Sequence conflict6631S → F in 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. Ref.1
Sequence conflict1362 – 13643Missing in AAC39659. Ref.1
Sequence conflict1362 – 13643Missing in AAR83296. Ref.2
Sequence conflict1362 – 13643Missing in AAR83297. Ref.2
Sequence conflict1362 – 13643Missing in AAR83298. Ref.2
Sequence conflict1362 – 13643Missing in AAH33715. Ref.4
Sequence conflict1362 – 13643Missing in 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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NC1-728) [UniParc].

Last modified November 25, 2008. Version 5.
Checksum: 23A327DCBD3B328D

FASTA1,754178,188
        10         20         30         40         50         60 
MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG PLPVQPTADT 

        70         80         90        100        110        120 
TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP DAPEENIAGV GAEILNVAKG 

       130        140        150        160        170        180 
IRSFVQLWND TVPTESLARA ETLVLETPVG PLALAGPSST PQENGTTLWP SRGIPSSPGA 

       190        200        210        220        230        240 
HTTEAGTLPA PTPSPPSLGR PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG 

       250        260        270        280        290        300 
LSPAAAAPSQ QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD 

       310        320        330        340        350        360 
SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS RFWLPNHLHH 

       370        380        390        400        410        420 
ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV PPPAPPPCCQ FCEALQDACW 

       430        440        450        460        470        480 
SRLGGGRLPV ACASLPTQED GYCVLIGPAA ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG 

       490        500        510        520        530        540 
LAYVFGPDAN SGQVARYHFP SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL 

       550        560        570        580        590        600 
SGVQDGHQDI SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR 

       610        620        630        640        650        660 
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH CLDEEGDDSD 

       670        680        690        700        710        720 
GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL AGGSSTEDSR SEEVEEQTTV 

       730        740        750        760        770        780 
ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP 

       790        800        810        820        830        840 
PGLPCPVSPL GPAGPALQTV PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP 

       850        860        870        880        890        900 
GTPGDVGPKG DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG 

       910        920        930        940        950        960 
PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG LPGPPGPPGR 

       970        980        990       1000       1010       1020 
EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA GAPGPAGPPG PPGPPGPPGP 

      1030       1040       1050       1060       1070       1080 
GLPAGFDDME GSGGPFWSTA RSADGPQGPP GLPGLKGDPG VPGLPGAKGE VGADGVPGFP 

      1090       1100       1110       1120       1130       1140 
GLPGREGIAG PQGPKGDRGS RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV 

      1150       1160       1170       1180       1190       1200 
PGPEGRPGFA GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG 

      1210       1220       1230       1240       1250       1260 
EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM RGMPGPPGPP 

      1270       1280       1290       1300       1310       1320 
GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK GEVGPPGPPG QFPFDFLQLE 

      1330       1340       1350       1360       1370       1380 
AEMKGEKGDR GDAGQKGERG EPGGGGFFGS SLPGPPGPPG PPGPRGYPGI PGPKGESIRG 

      1390       1400       1410       1420       1430       1440 
QPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG 

      1450       1460       1470       1480       1490       1500 
ASSGVRLWAT RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN 

      1510       1520       1530       1540       1550       1560 
EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP GAPHHSSYVH 

      1570       1580       1590       1600       1610       1620 
LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA DFQCFQQARA VGLAGTFRAF 

      1630       1640       1650       1660       1670       1680 
LSSRLQDLYS IVRRADRAAV PIVNLKDELL FPSWEALFSG SEGPLKPGAR IFSFDGKDVL 

      1690       1700       1710       1720       1730       1740 
RHPTWPQKSV WHGSDPNGRR LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY 

      1750 
IVLCIENSFM TASK 

« Hide

Isoform 2 (Long) (NC-493) [UniParc].

Checksum: 7456050495512DE2
Show »

FASTA1,519154,018
Isoform 3 (Short) (NC1-303) [UniParc].

Checksum: A8171B3EC21CBBF0
Show »

FASTA1,339135,761

References

« Hide 'large scale' references
[1]"Complete primary structure of two variant forms of human type XVIII collagen and tissue-specific differences in the expression of the corresponding transcripts."
Saarela J., Ylikarppa R., Rehn M., Purmonen S., Pihlajaniemi T.
Matrix Biol. 16:319-328(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT ILE-1076.
[2]"Characterization of the human type XVIII collagen gene and proteolytic processing and tissue location of the variant containing a frizzled motif."
Elamaa H., Snellman A., Rehn M., Autio-Harmainen H., Pihlajaniemi T.
Matrix Biol. 22:427-442(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANTS ILE-1076 AND ASN-1675.
[3]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ILE-1076.
Tissue: Kidney and PNS.
[5]"Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21."
Oh S.P., Warman M.L., Seldin M.F., Cheng S., Knoll J.H., Timmons S., Olsen B.R.
Genomics 19:494-499(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1069-1754, VARIANT ARG-1121.
[6]"Inhibition effect in vitro of purified endostatin expressed in Pichia pastoris."
Feng Y., Cui L.B., Liu C.X., Ma Q.J.
Sheng Wu Gong Cheng Xue Bao 17:278-282(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1568-1754.
[7]"Cloning and expression of human endostatin gene in Escherichia coli."
Zhi-Yong H., Biao L., Wei-Jie Z., Xiang-Fu W.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1572-1754, VARIANT ASN-1675.
Tissue: Placenta.
[8]"Endostatin promotes delayed secondary damage following traumatic brain injury."
Deininger M.H., Trautmann K., Schluesener H.J.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1642-1743.
[9]"No evidence for locus heterogeneity in Knobloch syndrome."
Aldahmesh M.A., Khan A.O., Mohamed J.Y., Levin A.V., Wuthisiri W., Lynch S., McCreery K., Alkuraya F.S.
J. Med. Genet. 50:565-566(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN KNO1.
[10]"Zinc-dependent dimers observed in crystals of human endostatin."
Ding Y.-H., Javaherian K., Lo K.-M., Chopra R., Boehm T., Lanciotti J., Harris B.A., Li Y., Shapiro R., Hohenester E., Timpl R., Folkman J., Wiley D.C.
Proc. Natl. Acad. Sci. U.S.A. 95:10443-10448(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1572-1749, ZINC-BINDING SITE.
[11]"Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure."
Sertie A.L., Sossi V., Camargo A.A., Zatz M., Brahe C., Passos-Bueno M.R.
Hum. Mol. Genet. 9:2051-2058(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN KNO1.
[12]"A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma."
Iughetti P., Suzuki O., Godoi P.H., Alves V.A., Sertie A.L., Zorick T., Soares F., Camargo A.A., Moreira E.S., di Loreto C., Moreira-Filho C.A., Simpson A., Oliva G., Passos-Bueno M.R.
Cancer Res. 61:7375-7378(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-1076 AND ASN-1675.
[13]"Knobloch syndrome: novel mutations in COL18A1, evidence for genetic heterogeneity, and a functionally impaired polymorphism in endostatin."
Menzel O., Bekkeheien R.C.J., Reymond A., Fukai N., Boye E., Kosztolanyi G., Aftimos S., Deutsch S., Scott H.S., Olsen B.R., Antonarakis S.E., Guipponi M.
Hum. Mutat. 23:77-84(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-49; ARG-111; ILE-1076 AND ARG-1121, CHARACTERIZATION OF VARIANT ASN-1675.
[14]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1121.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF018081 mRNA. Translation: AAC39658.1.
AF018082 mRNA. Translation: AAC39659.1.
AY484971 expand/collapse EMBL AC list , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83296.1.
AY484971 expand/collapse EMBL AC list , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83297.1.
AY484971 expand/collapse EMBL AC list , AY484967, AY484969, AY484970 Genomic DNA. Translation: AAR83298.1.
AL163302 Genomic DNA. Translation: CAB90482.1.
BX322561 Genomic DNA. No translation available.
BC033715 mRNA. Translation: AAH33715.1.
BC063833 mRNA. Translation: AAH63833.1.
L22548 mRNA. Translation: AAA51864.1.
AF416592 mRNA. Translation: AAL37720.1.
AF184060 mRNA. Translation: AAF01310.1.
AF333247 mRNA. Translation: AAK50626.1.
RefSeqNP_085059.2. NM_030582.3.
NP_569712.2. NM_130445.2.
UniGeneHs.517356.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BNLX-ray2.90A/B/C/D1572-1749[»]
3HONX-ray3.00A1441-1496[»]
3HSHX-ray1.80A/B/C/D/E/F1441-1496[»]
ProteinModelPortalP39060.
SMRP39060. Positions 338-444, 1441-1496, 1572-1749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123311. 4 interactions.
IntActP39060. 14 interactions.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP39060.
UniCarbKBP39060.

Polymorphism databases

DMDM215274264.

Proteomic databases

MaxQBP39060.
PaxDbP39060.
PRIDEP39060.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355480; ENSP00000347665; ENSG00000182871. [P39060-1]
ENST00000359759; ENSP00000352798; ENSG00000182871. [P39060-3]
ENST00000400337; ENSP00000383191; ENSG00000182871. [P39060-2]
GeneID80781.
KEGGhsa:80781.

Organism-specific databases

CTD80781.
GeneCardsGC21P046825.
HGNCHGNC:2195. COL18A1.
HPACAB001961.
HPA011025.
MIM120328. gene.
267750. phenotype.
neXtProtNX_P39060.
Orphanet1571. Knobloch syndrome.
PharmGKBPA26711.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG053241.
InParanoidP39060.
KOK06823.
OMAPFWSTAR.
OrthoDBEOG7NSB2B.
PhylomeDBP39060.
TreeFamTF315821.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP39060.
BgeeP39060.
GenevestigatorP39060.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
3.10.100.10. 1 hit.
InterProIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR026917. COL18A1.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR008985. ConA-like_lec_gl_sf.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR001791. Laminin_G.
[Graphical view]
PANTHERPTHR24023:SF390. PTHR24023:SF390. 1 hit.
PfamPF01391. Collagen. 7 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
SMARTSM00063. FRI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL18A1. human.
EvolutionaryTraceP39060.
GeneWikiCollagen,_type_XVIII,_alpha_1.
GenomeRNAi80781.
NextBio71187.
PROP39060.
SOURCESearch...

Entry information

Entry nameCOIA1_HUMAN
AccessionPrimary (citable) accession number: P39060
Secondary accession number(s): A8MVI4 expand/collapse secondary AC list , Q58EX6, Q6RZ39, Q6RZ40, Q6RZ41, Q8N4S4, Q8WXI5, Q96T70, Q9UK38, Q9Y6Q7, Q9Y6Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 159 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM