P39060 (COIA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XVIII) chain

Cleaved into the following chain:

1. Endostatin

Gene names

Name:

COL18A1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1754 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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) 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	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.10
Sequence similarities	Belongs to the multiplexin collagen family. Contains 1 FZ (frizzled) domain. Contains 1 laminin G-like domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Domain	Collagen Repeat Signal
Ligand	Metal-binding Zinc
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW endothelial cell morphogenesis Inferred from electronic annotation. Source: Compara 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.10. Source: ProtInc positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara visual perception Traceable author statement Ref.10. Source: ProtInc
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara collagen Traceable author statement Ref.10. Source: ProtInc endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		6	EBI-981314,EBI-981314
APP	P05067	2	EBI-2566375,EBI-821758
NCL	P19338	12	EBI-2566375,EBI-346967
TGM2	P21980	2	EBI-2566375,EBI-727668

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 1754

1731

Collagen alpha-1(XVIII) chain

PRO_0000005793

Chain

1572 – 1754

183

Endostatin

PRO_0000005794

Regions

Domain

329 – 446

118

FZ

Domain

456 – 644

189

Laminin G-like

Region

645 – 751

107

Nonhelical region 1 (NC1)

Region

752 – 785

34

Triple-helical region 1 (COL1)

Region

786 – 795

10

Nonhelical region 2 (NC2)

Region

796 – 875

80

Triple-helical region 2 (COL2)

Region

876 – 899

24

Nonhelical region 3 (NC3)

Region

900 – 1021

122

Triple-helical region 3 (COL3)

Region

1022 – 1044

23

Nonhelical region 4 (NC4)

Region

1045 – 1127

83

Triple-helical region 4 (COL4)

Region

1128 – 1141

14

Nonhelical region 5 (NC5)

Region

1142 – 1183

42

Triple-helical region 5 (COL5)

Region

1184 – 1196

13

Nonhelical region 6 (NC6)

Region

1197 – 1269

73

Triple-helical region 6 (COL6)

Region

1270 – 1279

10

Nonhelical region 7 (NC7)

Region

1280 – 1312

33

Triple-helical region 7 (COL7)

Region

1313 – 1324

12

Nonhelical region 8 (NC8)

Region

1325 – 1346

22

Triple-helical region 8 (COL8)

Region

1347 – 1353

7

Nonhelical region 9 (NC9)

Region

1354 – 1411

58

Triple-helical region 9 (COL9)

Region

1412 – 1424

13

Nonhelical region 10 (NC10)

Region

1425 – 1442

18

Triple-helical region 10 (COL10)

Region

1443 – 1754

312

Nonhelical region 11 (NC11)

Motif

1330 – 1332

3

Cell attachment site Potential

Sites

Metal binding

1572

1

Zinc

Metal binding

1574

1

Zinc

Metal binding

1582

1

Zinc

Metal binding

1647

1

Zinc

Amino acid modifications

Glycosylation

68

1

N-linked (GlcNAc...) Potential

Glycosylation

129

1

N-linked (GlcNAc...) Potential

Glycosylation

164

1

N-linked (GlcNAc...) Potential

Glycosylation

926

1

N-linked (GlcNAc...) Potential

Glycosylation

1567

1

O-linked (GalNAc...)

CAR_000150

Disulfide bond

334 ↔ 397

By similarity

Disulfide bond

344 ↔ 390

By similarity

Disulfide bond

381 ↔ 419

By similarity

Disulfide bond

408 ↔ 443

By similarity

Disulfide bond

412 ↔ 432

By similarity

Disulfide bond

1604 ↔ 1744

By similarity

Disulfide bond

1706 ↔ 1736

By similarity

Natural variations

Alternative sequence

1 – 415

415

Missing in isoform 3.

VSP_023130

Alternative sequence

216 – 450

235

Missing in isoform 2.

VSP_023131

Alternative sequence

416 – 450

35

QDACW…IGPAA → MAPRCPWPWPRRRRLLDVLA PLVLLLGVRAASAEP in isoform 3.

VSP_023132

Natural variant

49

1

Q → L. Ref.12

VAR_018053

Natural variant

111

1

G → R. Ref.12

VAR_018054

Natural variant

288

1

A → T.
Corresponds to variant rs11702494 [ dbSNP | Ensembl ].

VAR_059232

Natural variant

379

1

T → M.
Corresponds to variant rs8133886 [ dbSNP | Ensembl ].

VAR_061115

Natural variant

1076

1

V → I. Ref.1 Ref.2 Ref.4 Ref.11 Ref.12

VAR_018055

Natural variant

1121

1

P → R. Ref.5 Ref.12 Ref.13

VAR_018056

Natural variant

1195

1

Q → H.
Corresponds to variant rs2230693 [ dbSNP | Ensembl ].

VAR_059233

Natural variant

1675

1

D → 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.11 Ref.12

VAR_012709

Experimental info

Sequence conflict

299

1

R → K in AAR83296. Ref.2

Sequence conflict

663

1

S → F in AAC39658. Ref.1

Sequence conflict

663

1

S → F in AAC39659. Ref.1

Sequence conflict

1112

1

V → L in AAA51864. Ref.5

Sequence conflict

1147

1

P → R in AAA51864. Ref.5

Sequence conflict

1168

1

R → L in AAA51864. Ref.5

Sequence conflict

1210

1

P → L in AAA51864. Ref.5

Sequence conflict

1299

1

A → P in AAA51864. Ref.5

Sequence conflict

1319

1

L → K in AAA51864. Ref.5

Sequence conflict

1355

1

P → A in AAA51864. Ref.5

Sequence conflict

1358

1

P → A in AAA51864. Ref.5

Sequence conflict

1362 – 1364

3

Missing in AAC39658. Ref.1

Sequence conflict

1362 – 1364

3

Missing in AAC39659. Ref.1

Sequence conflict

1362 – 1364

3

Missing in AAR83296. Ref.2

Sequence conflict

1362 – 1364

3

Missing in AAR83297. Ref.2

Sequence conflict

1362 – 1364

3

Missing in AAR83298. Ref.2

Sequence conflict

1362 – 1364

3

Missing in AAH33715. Ref.4

Sequence conflict

1362 – 1364

3

Missing in AAH63833. Ref.4

Sequence conflict

1362 – 1364

3

Missing in AAA51864. Ref.5

Sequence conflict

1444

1

G → GQ in AAA51864. Ref.5

Sequence conflict

1542

1

R → G in AAA51864. Ref.5

Sequence conflict

1552

1

A → G in AAA51864. Ref.5

Sequence conflict

1561 – 1562

2

LR → CG in AAA51864. Ref.5

Sequence conflict

1681

1

R → T in AAF01310. Ref.7

Sequence conflict

1685

1

W → R in AAK50626. Ref.8

Sequence conflict

1721

1

S → Y in AAF01310. Ref.7

Sequence conflict

1736

1

C → S in AAK50626. Ref.8

Secondary structure

1

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1754

Helix Strand Turn

Details...

Beta strand

1445 – 1450

6

Helix

1451 – 1457

7

Helix

1458 – 1460

3

Beta strand

1466 – 1469

4

Turn

1470 – 1473

4

Beta strand

1474 – 1479

6

Beta strand

1482 – 1486

5

Beta strand

1488 – 1493

6

Beta strand

1581 – 1585

5

Helix

1597 – 1610

14

Beta strand

1617 – 1621

5

Helix

1629 – 1631

3

Helix

1634 – 1636

3

Beta strand

1649 – 1652

4

Helix

1654 – 1657

4

Helix

1679 – 1681

3

Beta strand

1689 – 1691

3

Helix

1706 – 1709

4

Beta strand

1716 – 1722

7

Helix

1723 – 1725

3

Beta strand

1727 – 1729

3

Beta strand

1732 – 1735

4

Beta strand

1743 – 1747

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NC1-728) [UniParc]. Last modified November 25, 2008. Version 5. Checksum: 23A327DCBD3B328D	FASTA	1,754	178,188
	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
	Isoform 2 (Long) (NC-493) [UniParc]. Checksum: 7456050495512DE2	FASTA	1,519	154,018
	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 PPPSSERISE EVGLLQLLGD PPPQQVTQTD 250 260 270 280 290 300 DPDVGLAYVF GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAMVL 310 320 330 340 350 360 LGVKLSGVQD GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVA GGFVALYVDC 370 380 390 400 410 420 EEFQRMPLAR SSRGLELEPG AGLFVAQAGG ADPDKFQGVI AELKVRRDPQ VSPMHCLDEE 430 440 450 460 470 480 GDDSDGASGD SGSGLGDARE LLREETGAAL KPRLPAPPPV TTPPLAGGSS TEDSRSEEVE 490 500 510 520 530 540 EQTTVASLGA QTLPGSDSVS TWDGSVRTPG GRVKEGGLKG QKGEPGVPGP PGRAGPPGSP 550 560 570 580 590 600 CLPGPPGLPC PVSPLGPAGP ALQTVPGPQG PPGPPGRDGT PGRDGEPGDP GEDGKPGDTG 610 620 630 640 650 660 PQGFPGTPGD VGPKGDKGDP GVGERGPPGP QGPPGPPGPS FRHDKLTFID MEGSGFGGDL 670 680 690 700 710 720 EALRGPRGFP GPPGPPGVPG LPGEPGRFGV NSSDVPGPAG LPGVPGREGP PGFPGLPGPP 730 740 750 760 770 780 GPPGREGPPG RTGQKGSLGE AGAPGHKGSK GAPGPAGARG ESGLAGAPGP AGPPGPPGPP 790 800 810 820 830 840 GPPGPGLPAG FDDMEGSGGP FWSTARSADG PQGPPGLPGL KGDPGVPGLP GAKGEVGADG 850 860 870 880 890 900 VPGFPGLPGR EGIAGPQGPK GDRGSRGEKG DPGKDGVGQP GLPGPPGPPG PVVYVSEQDG 910 920 930 940 950 960 SVLSVPGPEG RPGFAGFPGP AGPKGNLGSK GERGSPGPKG EKGEPGSIFS PDGGALGPAQ 970 980 990 1000 1010 1020 KGAKGEPGFR GPPGPYGRPG YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG 1030 1040 1050 1060 1070 1080 PPGPPGPPGP PGTPVYDSNV FAESSRPGPP GLPGNQGPPG PKGAKGEVGP PGPPGQFPFD 1090 1100 1110 1120 1130 1140 FLQLEAEMKG EKGDRGDAGQ KGERGEPGGG GFFGSSLPGP PGPPGPPGPR GYPGIPGPKG 1150 1160 1170 1180 1190 1200 ESIRGQPGPP GPQGPPGIGY EGRQGPPGPP GPPGPPSFPG PHRQTISVPG PPGPPGPPGP 1210 1220 1230 1240 1250 1260 PGTMGASSGV RLWATRQAML GQVHEVPEGW LIFVAEQEEL YVRVQNGFRK VQLEARTPLP 1270 1280 1290 1300 1310 1320 RGTDNEVAAL QPPVVQLHDS NPYPRREHPH PTARPWRADD ILASPPRLPE PQPYPGAPHH 1330 1340 1350 1360 1370 1380 SSYVHLRPAR PTSPPAHSHR DFQPVLHLVA LNSPLSGGMR GIRGADFQCF QQARAVGLAG 1390 1400 1410 1420 1430 1440 TFRAFLSSRL QDLYSIVRRA DRAAVPIVNL KDELLFPSWE ALFSGSEGPL KPGARIFSFD 1450 1460 1470 1480 1490 1500 GKDVLRHPTW PQKSVWHGSD PNGRRLTESY CETWRTEAPS ATGQASSLLG GRLLGQSAAS 1510 CHHAYIVLCI ENSFMTASK
	Isoform 3 (Short) (NC1-303) [UniParc]. Checksum: A8171B3EC21CBBF0	FASTA	1,339	135,761
	10 20 30 40 50 60 MAPRCPWPWP RRRRLLDVLA PLVLLLGVRA ASAEPERISE EVGLLQLLGD PPPQQVTQTD 70 80 90 100 110 120 DPDVGLAYVF GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAMVL 130 140 150 160 170 180 LGVKLSGVQD GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVA GGFVALYVDC 190 200 210 220 230 240 EEFQRMPLAR SSRGLELEPG AGLFVAQAGG ADPDKFQGVI AELKVRRDPQ VSPMHCLDEE 250 260 270 280 290 300 GDDSDGASGD SGSGLGDARE LLREETGAAL KPRLPAPPPV TTPPLAGGSS TEDSRSEEVE 310 320 330 340 350 360 EQTTVASLGA QTLPGSDSVS TWDGSVRTPG GRVKEGGLKG QKGEPGVPGP PGRAGPPGSP 370 380 390 400 410 420 CLPGPPGLPC PVSPLGPAGP ALQTVPGPQG PPGPPGRDGT PGRDGEPGDP GEDGKPGDTG 430 440 450 460 470 480 PQGFPGTPGD VGPKGDKGDP GVGERGPPGP QGPPGPPGPS FRHDKLTFID MEGSGFGGDL 490 500 510 520 530 540 EALRGPRGFP GPPGPPGVPG LPGEPGRFGV NSSDVPGPAG LPGVPGREGP PGFPGLPGPP 550 560 570 580 590 600 GPPGREGPPG RTGQKGSLGE AGAPGHKGSK GAPGPAGARG ESGLAGAPGP AGPPGPPGPP 610 620 630 640 650 660 GPPGPGLPAG FDDMEGSGGP FWSTARSADG PQGPPGLPGL KGDPGVPGLP GAKGEVGADG 670 680 690 700 710 720 VPGFPGLPGR EGIAGPQGPK GDRGSRGEKG DPGKDGVGQP GLPGPPGPPG PVVYVSEQDG 730 740 750 760 770 780 SVLSVPGPEG RPGFAGFPGP AGPKGNLGSK GERGSPGPKG EKGEPGSIFS PDGGALGPAQ 790 800 810 820 830 840 KGAKGEPGFR GPPGPYGRPG YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG 850 860 870 880 890 900 PPGPPGPPGP PGTPVYDSNV FAESSRPGPP GLPGNQGPPG PKGAKGEVGP PGPPGQFPFD 910 920 930 940 950 960 FLQLEAEMKG EKGDRGDAGQ KGERGEPGGG GFFGSSLPGP PGPPGPPGPR GYPGIPGPKG 970 980 990 1000 1010 1020 ESIRGQPGPP GPQGPPGIGY EGRQGPPGPP GPPGPPSFPG PHRQTISVPG PPGPPGPPGP 1030 1040 1050 1060 1070 1080 PGTMGASSGV RLWATRQAML GQVHEVPEGW LIFVAEQEEL YVRVQNGFRK VQLEARTPLP 1090 1100 1110 1120 1130 1140 RGTDNEVAAL QPPVVQLHDS NPYPRREHPH PTARPWRADD ILASPPRLPE PQPYPGAPHH 1150 1160 1170 1180 1190 1200 SSYVHLRPAR PTSPPAHSHR DFQPVLHLVA LNSPLSGGMR GIRGADFQCF QQARAVGLAG 1210 1220 1230 1240 1250 1260 TFRAFLSSRL QDLYSIVRRA DRAAVPIVNL KDELLFPSWE ALFSGSEGPL KPGARIFSFD 1270 1280 1290 1300 1310 1320 GKDVLRHPTW PQKSVWHGSD PNGRRLTESY CETWRTEAPS ATGQASSLLG GRLLGQSAAS 1330 CHHAYIVLCI ENSFMTASK

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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. , 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.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF018081 mRNA. Translation: AAC39658.1.
AF018082 mRNA. Translation: AAC39659.1.
AY484971 , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83296.1.
AY484971 , AY484968, AY484969, AY484970 Genomic DNA. Translation: AAR83297.1.
AY484971 , 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.

IPI

IPI00022822.
IPI00414694.
IPI00783931.

RefSeq

NP_085059.2. NM_030582.3.
NP_569712.2. NM_130445.2.

UniGene

Hs.517356.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BNL	X-ray	2.90	A/B/C/D	1572-1749	[»]
3HON	X-ray	3.00	A	1442-1496	[»]
3HSH	X-ray	1.80	A/B/C/D/E/F	1442-1496	[»]

ProteinModelPortal

P39060.

ModBase

Search...

Protein-protein interaction databases

IntAct

P39060. 13 interactions.

PTM databases

GlycoSuiteDB

P39060.

PhosphoSite

P39060.

Polymorphism databases

DMDM

215274264.

Proteomic databases

PaxDb

P39060.

PRIDE

P39060.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355480; ENSP00000347665; ENSG00000182871.
ENST00000359759; ENSP00000352798; ENSG00000182871.
ENST00000400337; ENSP00000383191; ENSG00000182871.

GeneID

80781.

KEGG

hsa:80781.

Organism-specific databases

CTD

80781.

GeneCards

GC21P046825.

HGNC

HGNC:2195. COL18A1.

HPA

CAB001961.
HPA011025.

MIM

120328. gene.
267750. phenotype.

neXtProt

NX_P39060.

Orphanet

1571. Knobloch syndrome.

PharmGKB

PA26711.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG053241.

InParanoid

P39060.

KO

K06823.

OMA

DCEEFQR.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.

Reactome

REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P39060.

Bgee

P39060.

Genevestigator

P39060.

GermOnline

ENSG00000182871. Homo sapiens.

Family and domain databases

Gene3D

1.10.2000.10. 1 hit.
3.10.100.10. 1 hit.

InterPro

IPR016186. 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]

PANTHER

PTHR24023:SF130. PTHR24023:SF130. 1 hit.

Pfam

PF01391. Collagen. 7 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]

SMART

SM00063. FRI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
SSF63501. Frizzled_Cys-rich. 1 hit.

PROSITE

PS50038. FZ. 1 hit.
PS50025. LAM_G_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

COL18A1. human.

EvolutionaryTrace

P39060.

GenomeRNAi

80781.

NextBio

71187.

SOURCE

Search...

Entry information

Entry name

COIA1_HUMAN

Accession

Primary (citable) accession number: P39060
Secondary accession number(s): A8MVI4 , 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:	May 1, 2013
This is version 145 of the entry and version 5 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.