P39061 (COIA1_MOUSE) 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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1774 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	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	Expressed in liver, kidney, lung, skeletal muscle and testis. Ref.7
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.
Sequence similarities	Belongs to the multiplexin collagen family. Contains 1 FZ (frizzled) domain. Contains 1 TSP N-terminal (TSPN) domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative promoter usage Alternative splicing
Domain	Collagen Repeat Signal
Ligand	Metal-binding Zinc
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from direct assay. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW endothelial cell morphogenesis Inferred from direct assay. Source: MGI extracellular matrix organization Inferred from mutant phenotype. Source: MGI positive regulation of apoptotic process Inferred from direct assay. Source: MGI positive regulation of cell migration Inferred from direct assay. Source: MGI positive regulation of cell proliferation Inferred from direct assay. Source: MGI
Cellular component	basement membrane Inferred from direct assay. Source: MGI collagen Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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: P39061-3)

Also known as: NC1-764;

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: P39061-1)

Also known as: Long; NC1-517;

The sequence of this isoform differs from the canonical sequence as follows:
     240-486: Missing.

Note: Produced by alternative splicing of isoform 1.

Isoform 3 (identifier: P39061-2)

Also known as: Short; NC1-301;

The sequence of this isoform differs from the canonical sequence as follows:
     1-459: Missing.
     460-486: AGDRLPVVCASLPSQEDGYCVFIGPAA → MAPRWHLLDVLTSLVLLLVARVSWAEP

Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 1774

1748

Collagen alpha-1(XVIII) chain

PRO_0000005795

Chain

1591 – 1774

184

Endostatin

PRO_0000005796

Regions

Domain

245 – 433

189

TSP N-terminal

Domain

365 – 482

118

FZ

Region

27 – 785

759

Nonhelical region 1 (NC1)

Region

786 – 812

27

Triple-helical region 1 (COL1)

Region

813 – 822

10

Nonhelical region 2 (NC2)

Region

823 – 896

74

Triple-helical region 2 (COL2)

Region

897 – 920

24

Nonhelical region 3 (NC3)

Region

921 – 1042

122

Triple-helical region 3 (COL3)

Region

1043 – 1065

23

Nonhelical region 4 (NC4)

Region

1066 – 1148

83

Triple-helical region 4 (COL4)

Region

1149 – 1162

14

Nonhelical region 5 (NC5)

Region

1163 – 1204

42

Triple-helical region 5 (COL5)

Region

1205 – 1217

13

Nonhelical region 6 (NC6)

Region

1218 – 1290

73

Triple-helical region 6 (COL6)

Region

1291 – 1300

10

Nonhelical region 7 (NC7)

Region

1301 – 1333

33

Triple-helical region 7 (COL7)

Region

1334 – 1345

12

Nonhelical region 8 (NC8)

Region

1346 – 1369

24

Triple-helical region 8 (COL8)

Region

1370 – 1376

7

Nonhelical region 9 (NC9)

Region

1377 – 1428

52

Triple-helical region 9 (COL9)

Region

1429 – 1441

13

Nonhelical region 10 (NC10)

Region

1442 – 1459

18

Triple-helical region 10 (COL10)

Region

1460 – 1774

315

Nonhelical region 11 (NC11)

Motif

1351 – 1353

3

Cell attachment site Potential

Sites

Metal binding

1591

1

Zinc; alternate

Metal binding

1593

1

Zinc

Metal binding

1595

1

Zinc; alternate

Metal binding

1601

1

Zinc

Metal binding

1666

1

Zinc

Amino acid modifications

Glycosylation

354

1

N-linked (GlcNAc...) Potential

Glycosylation

361

1

N-linked (GlcNAc...) Potential

Glycosylation

585

1

N-linked (GlcNAc...) Ref.12

Glycosylation

947

1

N-linked (GlcNAc...) Potential

Disulfide bond

370 ↔ 433

By similarity

Disulfide bond

380 ↔ 426

By similarity

Disulfide bond

417 ↔ 455

By similarity

Disulfide bond

444 ↔ 479

By similarity

Disulfide bond

448 ↔ 468

By similarity

Disulfide bond

1623 ↔ 1763

Ref.14

Disulfide bond

1725 ↔ 1755

Ref.14

Natural variations

Alternative sequence

1 – 459

459

Missing in isoform 3.

VSP_001157

Alternative sequence

240 – 486

247

Missing in isoform 2.

VSP_008303

Alternative sequence

460 – 486

27

AGDRL…IGPAA → MAPRWHLLDVLTSLVLLLVA RVSWAEP in isoform 3.

VSP_001158

Experimental info

Mutagenesis

1591

1

H → A: No effect on zinc binding. Ref.14

Mutagenesis

1593

1

H → A: Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595. Ref.14

Mutagenesis

1595

1

D → A: No effect on zinc binding. Abolishes zinc binding; when associated with A-1593. Ref.14

Mutagenesis

1666

1

D → A: Abolishes zinc binding. Ref.14

Sequence conflict

1046

1

G → V in AAH66080. Ref.4

Sequence conflict

1147

1

P → L in AAA19787. Ref.8

Sequence conflict

1194

1

P → F in AAA19787. Ref.8

Sequence conflict

1211

1

A → R in AAA19787. Ref.8

Sequence conflict

1347

1

D → V in BAC27554. Ref.6

Sequence conflict

1404

1

P → R in AAA20657. Ref.1

Sequence conflict

1404

1

P → R in AAC52901. Ref.2

Sequence conflict

1404

1

P → R in AAC52902. Ref.2

Sequence conflict

1404

1

P → R in AAC52903. Ref.2

Sequence conflict

1404

1

P → R in AAA19787. Ref.8

Sequence conflict

1513

1

P → L in AAA19787. Ref.8

Sequence conflict

1523

1

L → F in AAA19787. Ref.8

Sequence conflict

1684

1

L → V in AAA19787. Ref.8

Secondary structure

1

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1774

Helix Strand Turn

Details...

Beta strand

1600 – 1604

5

Beta strand

1611 – 1614

4

Helix

1615 – 1628

14

Turn

1629 – 1631

3

Beta strand

1636 – 1639

4

Helix

1647 – 1650

4

Helix

1653 – 1655

3

Turn

1656 – 1658

3

Beta strand

1668 – 1671

4

Helix

1673 – 1676

4

Beta strand

1678 – 1680

3

Turn

1698 – 1700

3

Beta strand

1704 – 1706

3

Beta strand

1708 – 1710

3

Helix

1725 – 1728

4

Beta strand

1736 – 1741

6

Helix

1742 – 1744

3

Beta strand

1751 – 1754

4

Beta strand

1762 – 1767

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NC1-764) [UniParc]. Last modified May 1, 2007. Version 4. Checksum: BEA79BADD1E34407	FASTA	1,774	182,172
	10 20 30 40 50 60 MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE GPVSKPQNSS 70 80 90 100 110 120 PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ KAGQGGSPAT PAVPIPLVAP 130 140 150 160 170 180 AASPDMKEEN VAGVGAKILN VAQGIRSFVQ LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE 190 200 210 220 230 240 LSSAPQGSKT TLWLSSAIPS SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPG 250 260 270 280 290 300 RAFLSSSTDQ GSSWGNQEPP RQPQHLEGKG FLPMTARSSQ QHRHSDVHSD IHGHVPLLPL 310 320 330 340 350 360 VTGPLVTASL SVHGLLSVPS SDPSGQLSQV AALPGFPGTW VSHVAPSSGT GLSNDSALAG 370 380 390 400 410 420 NGSLTSTSRC LPLPPTLTLC SRLGIGHFWL PNHLHHTDSV EVEATVQAWG RFLHTNCHPF 430 440 450 460 470 480 LAWFFCLLLA PSCGPGPPPP LPPCRQFCEA LEDECWNYLA GDRLPVVCAS LPSQEDGYCV 490 500 510 520 530 540 FIGPAAENVA EEVGLLQLLG DPLPEKISQI DDPHVGPAYI FGPDSNSGQV AQYHFPKLFF 550 560 570 580 590 600 RDFSLLFHVR PATEAAGVLF AITDAAQVVV SLGVKLSEVR DGQQNISLLY TEPGASQTQT 610 620 630 640 650 660 GASFRLPAFV GQWTHFALSV DGGSVALYVD CEEFQRVPFA RASQGLELER GAGLFVGQAG 670 680 690 700 710 720 TADPDKFQGM ISELKVRKTP RVSPVHCLDE EDDDEDRASG DFGSGFEESS KSHKEDTSLL 730 740 750 760 770 780 PGLPQPPPVT SPPLAGGSTT EDPRTEETEE DAAVDSIGAE TLPGTGSSGA WDEAIQNPGR 790 800 810 820 830 840 GLIKGGMKGQ KGEPGAQGPP GPAGPQGPAG PVVQSPNSQP VPGAQGPPGP QGPPGKDGTP 850 860 870 880 890 900 GRDGEPGDPG EDGRPGDTGP QGFPGTPGDV GPKGEKGDPG IGPRGPPGPP GPPGPSFRQD 910 920 930 940 950 960 KLTFIDMEGS GFSGDIESLR GPRGFPGPPG PPGVPGLPGE PGRFGINGSY APGPAGLPGV 970 980 990 1000 1010 1020 PGKEGPPGFP GPPGPPGPPG KEGPPGVAGQ KGSVGDVGIP GPKGSKGDLG PIGMPGKSGL 1030 1040 1050 1060 1070 1080 AGSPGPVGPP GPPGPPGPPG PGFAAGFDDM EGSGIPLWTT ARSSDGLQGP PGSPGLKGDP 1090 1100 1110 1120 1130 1140 GVAGLPGAKG EVGADGAQGI PGPPGREGAA GSPGPKGEKG MPGEKGNPGK DGVGRPGLPG 1150 1160 1170 1180 1190 1200 PPGPPGPVIY VSSEDKAIVS TPGPEGKPGY AGFPGPAGPK GDLGSKGEQG LPGPKGEKGE 1210 1220 1230 1240 1250 1260 PGTIFSPDGR ALGHPQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GTNGLKGEKG 1270 1280 1290 1300 1310 1320 EPGDASLGFS MRGLPGPPGP PGPPGPPGMP IYDSNAFVES GRPGLPGQQG VQGPSGPKGD 1330 1340 1350 1360 1370 1380 KGEVGPPGPP GQFPIDLFHL EAEMKGDKGD RGDAGQKGER GEPGAPGGGF FSSSVPGPPG 1390 1400 1410 1420 1430 1440 PPGYPGIPGP KGESIRGPPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV 1450 1460 1470 1480 1490 1500 PGPPGPPGPP GPPGAMGASA GQVRIWATYQ TMLDKIREVP EGWLIFVAER EELYVRVRNG 1510 1520 1530 1540 1550 1560 FRKVLLEART ALPRGTGNEV AALQPPLVQL HEGSPYTRRE YSYSTARPWR ADDILANPPR 1570 1580 1590 1600 1610 1620 LPDRQPYPGV PHHHSSYVHL PPARPTLSLA HTHQDFQPVL HLVALNTPLS GGMRGIRGAD 1630 1640 1650 1660 1670 1680 FQCFQQARAV GLSGTFRAFL SSRLQDLYSI VRRADRGSVP IVNLKDEVLS PSWDSLFSGS 1690 1700 1710 1720 1730 1740 QGQLQPGARI FSFDGRDVLR HPAWPQKSVW HGSDPSGRRL MESYCETWRT ETTGATGQAS 1750 1760 1770 SLLSGRLLEQ KAASCHNSYI VLCIENSFMT SFSK
	Isoform 2 (Long) (NC1-517) [UniParc]. Checksum: E7AF043EC82D0326	FASTA	1,527	155,950
	10 20 30 40 50 60 MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE GPVSKPQNSS 70 80 90 100 110 120 PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ KAGQGGSPAT PAVPIPLVAP 130 140 150 160 170 180 AASPDMKEEN VAGVGAKILN VAQGIRSFVQ LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE 190 200 210 220 230 240 LSSAPQGSKT TLWLSSAIPS SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPE 250 260 270 280 290 300 NVAEEVGLLQ LLGDPLPEKI SQIDDPHVGP AYIFGPDSNS GQVAQYHFPK LFFRDFSLLF 310 320 330 340 350 360 HVRPATEAAG VLFAITDAAQ VVVSLGVKLS EVRDGQQNIS LLYTEPGASQ TQTGASFRLP 370 380 390 400 410 420 AFVGQWTHFA LSVDGGSVAL YVDCEEFQRV PFARASQGLE LERGAGLFVG QAGTADPDKF 430 440 450 460 470 480 QGMISELKVR KTPRVSPVHC LDEEDDDEDR ASGDFGSGFE ESSKSHKEDT SLLPGLPQPP 490 500 510 520 530 540 PVTSPPLAGG STTEDPRTEE TEEDAAVDSI GAETLPGTGS SGAWDEAIQN PGRGLIKGGM 550 560 570 580 590 600 KGQKGEPGAQ GPPGPAGPQG PAGPVVQSPN SQPVPGAQGP PGPQGPPGKD GTPGRDGEPG 610 620 630 640 650 660 DPGEDGRPGD TGPQGFPGTP GDVGPKGEKG DPGIGPRGPP GPPGPPGPSF RQDKLTFIDM 670 680 690 700 710 720 EGSGFSGDIE SLRGPRGFPG PPGPPGVPGL PGEPGRFGIN GSYAPGPAGL PGVPGKEGPP 730 740 750 760 770 780 GFPGPPGPPG PPGKEGPPGV AGQKGSVGDV GIPGPKGSKG DLGPIGMPGK SGLAGSPGPV 790 800 810 820 830 840 GPPGPPGPPG PPGPGFAAGF DDMEGSGIPL WTTARSSDGL QGPPGSPGLK GDPGVAGLPG 850 860 870 880 890 900 AKGEVGADGA QGIPGPPGRE GAAGSPGPKG EKGMPGEKGN PGKDGVGRPG LPGPPGPPGP 910 920 930 940 950 960 VIYVSSEDKA IVSTPGPEGK PGYAGFPGPA GPKGDLGSKG EQGLPGPKGE KGEPGTIFSP 970 980 990 1000 1010 1020 DGRALGHPQK GAKGEPGFRG PPGPYGRPGH KGEIGFPGRP GRPGTNGLKG EKGEPGDASL 1030 1040 1050 1060 1070 1080 GFSMRGLPGP PGPPGPPGPP GMPIYDSNAF VESGRPGLPG QQGVQGPSGP KGDKGEVGPP 1090 1100 1110 1120 1130 1140 GPPGQFPIDL FHLEAEMKGD KGDRGDAGQK GERGEPGAPG GGFFSSSVPG PPGPPGYPGI 1150 1160 1170 1180 1190 1200 PGPKGESIRG PPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQT VSVPGPPGPP 1210 1220 1230 1240 1250 1260 GPPGPPGAMG ASAGQVRIWA TYQTMLDKIR EVPEGWLIFV AEREELYVRV RNGFRKVLLE 1270 1280 1290 1300 1310 1320 ARTALPRGTG NEVAALQPPL VQLHEGSPYT RREYSYSTAR PWRADDILAN PPRLPDRQPY 1330 1340 1350 1360 1370 1380 PGVPHHHSSY VHLPPARPTL SLAHTHQDFQ PVLHLVALNT PLSGGMRGIR GADFQCFQQA 1390 1400 1410 1420 1430 1440 RAVGLSGTFR AFLSSRLQDL YSIVRRADRG SVPIVNLKDE VLSPSWDSLF SGSQGQLQPG 1450 1460 1470 1480 1490 1500 ARIFSFDGRD VLRHPAWPQK SVWHGSDPSG RRLMESYCET WRTETTGATG QASSLLSGRL 1510 1520 LEQKAASCHN SYIVLCIENS FMTSFSK
	Isoform 3 (Short) (NC1-301) [UniParc]. Checksum: B8215602ACE7AD1F	FASTA	1,315	134,204
	10 20 30 40 50 60 MAPRWHLLDV LTSLVLLLVA RVSWAEPENV AEEVGLLQLL GDPLPEKISQ IDDPHVGPAY 70 80 90 100 110 120 IFGPDSNSGQ VAQYHFPKLF FRDFSLLFHV RPATEAAGVL FAITDAAQVV VSLGVKLSEV 130 140 150 160 170 180 RDGQQNISLL YTEPGASQTQ TGASFRLPAF VGQWTHFALS VDGGSVALYV DCEEFQRVPF 190 200 210 220 230 240 ARASQGLELE RGAGLFVGQA GTADPDKFQG MISELKVRKT PRVSPVHCLD EEDDDEDRAS 250 260 270 280 290 300 GDFGSGFEES SKSHKEDTSL LPGLPQPPPV TSPPLAGGST TEDPRTEETE EDAAVDSIGA 310 320 330 340 350 360 ETLPGTGSSG AWDEAIQNPG RGLIKGGMKG QKGEPGAQGP PGPAGPQGPA GPVVQSPNSQ 370 380 390 400 410 420 PVPGAQGPPG PQGPPGKDGT PGRDGEPGDP GEDGRPGDTG PQGFPGTPGD VGPKGEKGDP 430 440 450 460 470 480 GIGPRGPPGP PGPPGPSFRQ DKLTFIDMEG SGFSGDIESL RGPRGFPGPP GPPGVPGLPG 490 500 510 520 530 540 EPGRFGINGS YAPGPAGLPG VPGKEGPPGF PGPPGPPGPP GKEGPPGVAG QKGSVGDVGI 550 560 570 580 590 600 PGPKGSKGDL GPIGMPGKSG LAGSPGPVGP PGPPGPPGPP GPGFAAGFDD MEGSGIPLWT 610 620 630 640 650 660 TARSSDGLQG PPGSPGLKGD PGVAGLPGAK GEVGADGAQG IPGPPGREGA AGSPGPKGEK 670 680 690 700 710 720 GMPGEKGNPG KDGVGRPGLP GPPGPPGPVI YVSSEDKAIV STPGPEGKPG YAGFPGPAGP 730 740 750 760 770 780 KGDLGSKGEQ GLPGPKGEKG EPGTIFSPDG RALGHPQKGA KGEPGFRGPP GPYGRPGHKG 790 800 810 820 830 840 EIGFPGRPGR PGTNGLKGEK GEPGDASLGF SMRGLPGPPG PPGPPGPPGM PIYDSNAFVE 850 860 870 880 890 900 SGRPGLPGQQ GVQGPSGPKG DKGEVGPPGP PGQFPIDLFH LEAEMKGDKG DRGDAGQKGE 910 920 930 940 950 960 RGEPGAPGGG FFSSSVPGPP GPPGYPGIPG PKGESIRGPP GPPGPQGPPG IGYEGRQGPP 970 980 990 1000 1010 1020 GPPGPPGPPS FPGPHRQTVS VPGPPGPPGP PGPPGAMGAS AGQVRIWATY QTMLDKIREV 1030 1040 1050 1060 1070 1080 PEGWLIFVAE REELYVRVRN GFRKVLLEAR TALPRGTGNE VAALQPPLVQ LHEGSPYTRR 1090 1100 1110 1120 1130 1140 EYSYSTARPW RADDILANPP RLPDRQPYPG VPHHHSSYVH LPPARPTLSL AHTHQDFQPV 1150 1160 1170 1180 1190 1200 LHLVALNTPL SGGMRGIRGA DFQCFQQARA VGLSGTFRAF LSSRLQDLYS IVRRADRGSV 1210 1220 1230 1240 1250 1260 PIVNLKDEVL SPSWDSLFSG SQGQLQPGAR IFSFDGRDVL RHPAWPQKSV WHGSDPSGRR 1270 1280 1290 1300 1310 LMESYCETWR TETTGATGQA SSLLSGRLLE QKAASCHNSY IVLCIENSFM TSFSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the alpha 1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the alpha 1(XVIII) chain with its homologue, the alpha 1(XV) collagen chain." Rehn M.V., Hintikka E., Pihlajaniemi T. J. Biol. Chem. 269:13929-13935(1994) [PubMed: 8188673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3). Strain: BALB/c. Tissue: Liver.
[2]	"Characterization of the mouse gene for the alpha-1 chain of type XVIII collagen (COL18A1) reveals that the three variant N-terminal polypeptide forms are transcribed from two widely separated promoters." Rehn M., Hintikka E., Pihlajaniemi T. Genomics 32:436-446(1996) [PubMed: 8838808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Strain: C57BL/6. Tissue: Brain and Embryo.
[5]	"Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen." Rehn M.V., Pihlajaniemi T. Proc. Natl. Acad. Sci. U.S.A. 91:4234-4238(1994) [PubMed: 8183894] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1387 (ISOFORM 3).
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1347 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1615-1774. Strain: C57BL/6J. Tissue: Head.
[7]	"Identification of three N-terminal ends of type XVIII collagen chains and tissue-specific differences in the expression of the corresponding transcripts. The longest form contains a novel motif homologous to rat and Drosophila frizzled proteins." Rehn M., Pihlajaniemi T. J. Biol. Chem. 270:4705-4711(1995) [PubMed: 7876242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-562 (ISOFORMS 1 AND 3), TISSUE SPECIFICITY.
[8]	"Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins." Oh S.P., Kamagata Y., Muragaki Y., Timmons S., Ooshima A., Olsen B.R. Proc. Natl. Acad. Sci. U.S.A. 91:4229-4233(1994) [PubMed: 8183893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 487-1774. Tissue: Liver.
[9]	"Identification of a novel collagen chain represented by extensive interruptions in the triple-helical region." Abe N., Muragaki Y., Yoshioka H., Inoue H., Ninomiya Y. Biochem. Biophys. Res. Commun. 196:576-582(1993) [PubMed: 8240330] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 635-1774. Tissue: Embryo.
[10]	"Anticancer treatment of endostatin gene therapy by targeting tumor neovasculature in C57/BL mice." Jia S., Zhu F., Li H., He F., Xiu R.-J. Clin. Hemorheol. Microcirc. 23:251-257(2000) [PubMed: 11321448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1591-1774.
[11]	"Endostatin: an endogenous inhibitor of angiogenesis and tumor growth." O'Reilly M.S., Boehm T., Shing Y., Fukai N., Vasios G., Lane W.S., Flynn E., Birkhead J.R., Olsen B.R., Folkman J. Cell 88:277-285(1997) [PubMed: 9008168] [Abstract] Cited for: CHARACTERIZATION OF ENDOSTATIN, PROTEIN SEQUENCE OF 1591-1610.
[12]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585, MASS SPECTROMETRY.
[13]	"Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A resolution." Hohenester E., Sasaki T., Olsen B.R., Timpl R. EMBO J. 17:1656-1664(1998) [PubMed: 9501087] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ENDOSTATIN.
[14]	"Variable zinc coordination in endostatin." Hohenester E., Sasaki T., Mann K., Timpl R. J. Mol. Biol. 297:1-6(2000) [PubMed: 10704302] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1589-1774, DISULFIDE BONDS, MUTAGENESIS OF HIS-1591; HIS-1593; ASP-1595 AND ASP-1666, ZINC-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U03714 mRNA. Translation: AAA20657.1.
U03715 , U34606, U34608, U34609, U34610, U34611, U34612, U34613, U03716, U03718 Genomic DNA. Translation: AAC52901.1.
U03715 , U34607, U34608, U34609, U34610, U34611, U34612, U34613, U03716, U03718 Genomic DNA. Translation: AAC52902.1.
U03715 , U03716, U03718, U34607, U34608, U34609, U34610, U34611, U34612, U34613 Genomic DNA. Translation: AAC52903.1.
AC055777 Genomic DNA. No translation available.
AC159334 Genomic DNA. No translation available.
BC064817 mRNA. Translation: AAH64817.1.
BC066080 mRNA. Translation: AAH66080.1.
L16898 mRNA. Translation: AAA37434.1.
AK031798 mRNA. Translation: BAC27554.1.
AK014292 mRNA. Translation: BAB29249.1.
U11636 mRNA. Translation: AAC52178.1.
U11637 mRNA. Translation: AAC52179.1.
L22545 mRNA. Translation: AAA19787.1.
D17546 mRNA. Translation: BAA04483.1.
AF257775 mRNA. Translation: AAF69009.1.

IPI

IPI00131476.
IPI00230616.
IPI00284816.

PIR

A56101.
B56101.

RefSeq

NP_001103461.1. NM_001109991.1.
NP_034059.2. NM_009929.3.

UniGene

Mm.4352.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DY0	X-ray	2.20	A	1589-1774	[»]
1DY1	X-ray	2.20	A	1589-1774	[»]
1KOE	X-ray	1.50	A	1597-1768	[»]

ProteinModelPortal

P39061.

SMR

P39061. Positions 368-491, 1463-1514, 1597-1768.

ModBase

Search...

Protein-protein interaction databases

STRING

P39061.

Proteomic databases

PRIDE

P39061.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000081654; ENSMUSP00000080358; ENSMUSG00000001435.
ENSMUST00000105409; ENSMUSP00000101049; ENSMUSG00000001435.

GeneID

12822.

KEGG

mmu:12822.

UCSC

uc007fvg.1. mouse.
uc007fvh.2. mouse.

Organism-specific databases

CTD

80781.

MGI

MGI:88451. Col18a1.

Phylogenomic databases

eggNOG

maNOG04248.

GeneTree

ENSGT00530000063925.

HOVERGEN

HBG053241.

InParanoid

P39061.

OrthoDB

EOG4BVRTD.

Gene expression databases

ArrayExpress

P39061.

Bgee

P39061.

CleanEx

MM_COL18A1.

Genevestigator

P39061.

GermOnline

ENSMUSG00000001435. Mus musculus.

Family and domain databases

InterPro

IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR001791. Laminin_G.
IPR003129. Laminin_G_thrombospondin_N.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
G3DSA:1.10.2000.10. Frizzled_Cys-rich. 1 hit.

KO

K06823.

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.
[Graphical view]

ProtoNet

Search...

Other

NextBio

282298.

PMAP-CutDB

P39061.

SOURCE

Search...

Entry information

Entry name

COIA1_MOUSE

Accession

Primary (citable) accession number: P39061
Secondary accession number(s): Q60672 , Q61434, Q61437, Q62001, Q62002, Q6NZK9, Q6P1Y4, Q8CCZ8, Q9CRT2, Q9JK63

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 1, 2007
Last modified:	December 14, 2011
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program