COIA1_MOUSE
ID COIA1_MOUSE Reviewed; 1774 AA.
AC P39061; Q60672; Q61434; Q61437; Q62001; Q62002; Q6NZK9; Q6P1Y4; Q8CCZ8;
AC Q9CRT2; Q9JK63;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Collagen alpha-1(XVIII) chain {ECO:0000305};
DE Contains:
DE RecName: Full=Endostatin {ECO:0000305};
DE Contains:
DE RecName: Full=Non-collagenous domain 1 {ECO:0000305};
DE Short=NC1;
DE Flags: Precursor;
GN Name=Col18a1 {ECO:0000312|MGI:MGI:88451};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8188673; DOI=10.1016/s0021-9258(17)36737-6;
RA Rehn M.V., Hintikka E., Pihlajaniemi T.;
RT "Primary structure of the alpha 1 chain of mouse type XVIII collagen,
RT partial structure of the corresponding gene, and comparison of the alpha
RT 1(XVIII) chain with its homologue, the alpha 1(XV) collagen chain.";
RL J. Biol. Chem. 269:13929-13935(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=8838808; DOI=10.1006/geno.1996.0139;
RA Rehn M., Hintikka E., Pihlajaniemi T.;
RT "Characterization of the mouse gene for the alpha-1 chain of type XVIII
RT collagen (COL18A1) reveals that the three variant N-terminal polypeptide
RT forms are transcribed from two widely separated promoters.";
RL Genomics 32:436-446(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1387 (ISOFORM 3).
RX PubMed=8183894; DOI=10.1073/pnas.91.10.4234;
RA Rehn M.V., Pihlajaniemi T.;
RT "Alpha 1(XVIII), a collagen chain with frequent interruptions in the
RT collagenous sequence, a distinct tissue distribution, and homology with
RT type XV collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4234-4238(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1347 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1615-1774.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-562 (ISOFORMS 1 AND 3), AND TISSUE
RP SPECIFICITY.
RX PubMed=7876242; DOI=10.1074/jbc.270.9.4705;
RA Rehn M., Pihlajaniemi T.;
RT "Identification of three N-terminal ends of type XVIII collagen chains and
RT tissue-specific differences in the expression of the corresponding
RT transcripts. The longest form contains a novel motif homologous to rat and
RT Drosophila frizzled proteins.";
RL J. Biol. Chem. 270:4705-4711(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-1774.
RC TISSUE=Liver;
RX PubMed=8183893; DOI=10.1073/pnas.91.10.4229;
RA Oh S.P., Kamagata Y., Muragaki Y., Timmons S., Ooshima A., Olsen B.R.;
RT "Isolation and sequencing of cDNAs for proteins with multiple domains of
RT Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4229-4233(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 635-1774.
RC TISSUE=Embryo;
RX PubMed=8240330; DOI=10.1006/bbrc.1993.2288;
RA Abe N., Muragaki Y., Yoshioka H., Inoue H., Ninomiya Y.;
RT "Identification of a novel collagen chain represented by extensive
RT interruptions in the triple-helical region.";
RL Biochem. Biophys. Res. Commun. 196:576-582(1993).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1591-1774.
RX PubMed=11321448;
RA Jia S., Zhu F., Li H., He F., Xiu R.-J.;
RT "Anticancer treatment of endostatin gene therapy by targeting tumor
RT neovasculature in C57/BL mice.";
RL Clin. Hemorheol. Microcirc. 23:251-257(2000).
RN [11]
RP CHARACTERIZATION OF ENDOSTATIN, AND PROTEIN SEQUENCE OF 1591-1610.
RX PubMed=9008168; DOI=10.1016/s0092-8674(00)81848-6;
RA O'Reilly M.S., Boehm T., Shing Y., Fukai N., Vasios G., Lane W.S.,
RA Flynn E., Birkhead J.R., Olsen B.R., Folkman J.;
RT "Endostatin: an endogenous inhibitor of angiogenesis and tumor growth.";
RL Cell 88:277-285(1997).
RN [12]
RP PROTEOLYTIC CLEAVAGE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9687493; DOI=10.1093/emboj/17.15.4249;
RA Sasaki T., Fukai N., Mann K., Goehring W., Olsen B.R., Timpl R.;
RT "Structure, function and tissue forms of the C-terminal globular domain of
RT collagen XVIII containing the angiogenesis inhibitor endostatin.";
RL EMBO J. 17:4249-4256(1998).
RN [13]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=10626789;
RA Wen W., Moses M.A., Wiederschain D., Arbiser J.L., Folkman J.;
RT "The generation of endostatin is mediated by elastase.";
RL Cancer Res. 59:6052-6056(1999).
RN [14]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=10716919; DOI=10.1093/emboj/19.6.1187;
RA Felbor U., Dreier L., Bryant R.A., Ploegh H.L., Olsen B.R., Mothes W.;
RT "Secreted cathepsin L generates endostatin from collagen XVIII.";
RL EMBO J. 19:1187-1194(2000).
RN [15]
RP SUBUNIT.
RX PubMed=10966814; DOI=10.1006/jmbi.2000.3996;
RA Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., Timpl R.;
RT "Endostatins derived from collagens XV and XVIII differ in structural and
RT binding properties, tissue distribution and anti-angiogenic activity.";
RL J. Mol. Biol. 301:1179-1190(2000).
RN [16]
RP FUNCTION, AND INTERACTION WITH ITGA5:ITGB1.
RX PubMed=11158588; DOI=10.1073/pnas.98.3.1024;
RA Rehn M., Veikkola T., Kukk-Valdre E., Nakamura H., Ilmonen M., Lombardo C.,
RA Pihlajaniemi T., Alitalo K., Vuori K.;
RT "Interaction of endostatin with integrins implicated in angiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1024-1029(2001).
RN [17]
RP FUNCTION, AND INTERACTION WITH KDR.
RX PubMed=12029087; DOI=10.1074/jbc.m202771200;
RA Kim Y.M., Hwang S., Kim Y.M., Pyun B.J., Kim T.Y., Lee S.T., Gho Y.S.,
RA Kwon Y.G.;
RT "Endostatin blocks vascular endothelial growth factor-mediated signaling
RT via direct interaction with KDR/Flk-1.";
RL J. Biol. Chem. 277:27872-27879(2002).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ENDOSTATIN.
RX PubMed=9501087; DOI=10.1093/emboj/17.6.1656;
RA Hohenester E., Sasaki T., Olsen B.R., Timpl R.;
RT "Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A
RT resolution.";
RL EMBO J. 17:1656-1664(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1589-1774, DISULFIDE BONDS,
RP MUTAGENESIS OF HIS-1591; HIS-1593; ASP-1595 AND ASP-1666, AND ZINC-BINDING
RP SITES.
RX PubMed=10704302; DOI=10.1006/jmbi.2000.3553;
RA Hohenester E., Sasaki T., Mann K., Timpl R.;
RT "Variable zinc coordination in endostatin.";
RL J. Mol. Biol. 297:1-6(2000).
CC -!- FUNCTION: Probably plays a major role in determining the retinal
CC structure as well as in the closure of the neural tube.
CC {ECO:0000250|UniProtKB:P39060}.
CC -!- FUNCTION: [Non-collagenous domain 1]: May regulate extracellular
CC matrix-dependent motility and morphogenesis of endothelial and non-
CC endothelial cells; the function requires homotrimerization and
CC implicates MAPK signaling. {ECO:0000250|UniProtKB:P39060}.
CC -!- FUNCTION: [Endostatin]: Potently inhibits endothelial cell
CC proliferation and angiogenesis. May inhibit angiogenesis by binding to
CC the heparan sulfate proteoglycans involved in growth factor signaling
CC (PubMed:9008168). Inhibits VEGFA isoform VEGF165-induced endothelial
CC cell proliferation and migration. Seems to inhibit VEGFA-mediated
CC signaling by blocking the interaction of VEGFA to its receptor
CC KDR/VEGFR2 (PubMed:12029087). Modulates endothelial cell migration in
CC an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a
CC lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (PubMed:11158588). May
CC negatively regulate the activity of homotrimeric non-collagenous domain
CC 1 (By similarity). {ECO:0000250|UniProtKB:P39060,
CC ECO:0000269|PubMed:11158588, ECO:0000269|PubMed:9008168}.
CC -!- SUBUNIT: [Non-collagenous domain 1]: Forms homotrimers. Recombinant
CC non-collagenous domain 1 has stronger affinity to NID1, HSPG2 and
CC laminin-1:NID1 complex and lower affinity to FBLN1 and FBLN2 than
CC endostatin (PubMed:10966814). {ECO:0000269|PubMed:10966814}.
CC -!- SUBUNIT: [Endostatin]: Monomeric (PubMed:9687493). Interacts with
CC KDR/VEGFR2 (PubMed:12029087). Interacts with the ITGA5:ITGB1 complex
CC (PubMed:11158588). Interacts with NID1, HSPG2, laminin-1:NID1 complex,
CC FBLN1 and FBLN2 (PubMed:10966814, PubMed:11158588, PubMed:12029087).
CC {ECO:0000269|PubMed:10966814, ECO:0000269|PubMed:11158588,
CC ECO:0000269|PubMed:12029087, ECO:0000269|PubMed:9687493}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:9687493}.
CC -!- SUBCELLULAR LOCATION: [Non-collagenous domain 1]: Secreted,
CC extracellular space, extracellular matrix, basement membrane
CC {ECO:0000305|PubMed:9687493}. Secreted {ECO:0000269|PubMed:10626789}.
CC -!- SUBCELLULAR LOCATION: [Endostatin]: Secreted
CC {ECO:0000269|PubMed:10626789, ECO:0000305|PubMed:9008168}. Secreted,
CC extracellular space, extracellular matrix, basement membrane
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NC1-764;
CC IsoId=P39061-3; Sequence=Displayed;
CC Name=2; Synonyms=Long, NC1-517;
CC IsoId=P39061-1; Sequence=VSP_008303;
CC Name=3; Synonyms=Short, NC1-301;
CC IsoId=P39061-2; Sequence=VSP_001157, VSP_001158;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, lung, skeletal muscle
CC and testis. {ECO:0000269|PubMed:7876242}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) of the triple-helical regions are hydroxylated.
CC -!- PTM: Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-
CC like proteases to generate both non-collagenous domain 1 trimers and
CC endostatin monomers (PubMed:10716919). In tissue extracts (brain,
CC skeletal muscle, heart, kidney, testis and liver) predominantly bands
CC of approximately 38 kDa are detected; recombinant non-collagenous
CC domain 1 shows similar mobility. In vitro, several proteolytic cleavage
CC sites in the non-collagenous domain 1 hinge region generating different
CC endostatin-like peptides are reported. {ECO:0000250|UniProtKB:P39060,
CC ECO:0000269|PubMed:10626789, ECO:0000269|PubMed:10716919,
CC ECO:0000305|PubMed:9687493}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family. {ECO:0000305}.
CC -!- CAUTION: Non-collagenous domain 1 seems to be the predominant tissue
CC form from which endostatin is cleaved. However, the proteolytic
CC cleavage site to generate non-collagenous domain 1 is not known.
CC Soluble recombinant non-collagenous domain 1 amenable to biochemical
CC studies has been used instead; its molecular weight corresponds to
CC probable non-collagenous domain 1 immunoblot bands seen in tissue
CC extracts. {ECO:0000305}.
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DR EMBL; U03714; AAA20657.1; -; mRNA.
DR EMBL; U03715; AAC52901.1; -; Genomic_DNA.
DR EMBL; U34606; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34608; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34609; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34610; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34611; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34612; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U34613; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U03716; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U03718; AAC52901.1; JOINED; Genomic_DNA.
DR EMBL; U03715; AAC52902.1; -; Genomic_DNA.
DR EMBL; U34607; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34608; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34609; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34610; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34611; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34612; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U34613; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U03716; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U03718; AAC52902.1; JOINED; Genomic_DNA.
DR EMBL; U03715; AAC52903.1; -; Genomic_DNA.
DR EMBL; U03716; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U03718; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34607; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34608; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34609; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34610; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34611; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34612; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; U34613; AAC52903.1; JOINED; Genomic_DNA.
DR EMBL; AC055777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064817; AAH64817.1; -; mRNA.
DR EMBL; BC066080; AAH66080.1; -; mRNA.
DR EMBL; L16898; AAA37434.1; -; mRNA.
DR EMBL; AK031798; BAC27554.1; -; mRNA.
DR EMBL; AK014292; BAB29249.1; -; mRNA.
DR EMBL; U11636; AAC52178.1; -; mRNA.
DR EMBL; U11637; AAC52179.1; -; mRNA.
DR EMBL; L22545; AAA19787.1; -; mRNA.
DR EMBL; D17546; BAA04483.1; -; mRNA.
DR EMBL; AF257775; AAF69009.1; -; mRNA.
DR CCDS; CCDS23953.1; -. [P39061-2]
DR CCDS; CCDS48604.1; -. [P39061-1]
DR PIR; A56101; A56101.
DR PIR; B56101; B56101.
DR RefSeq; NP_001103461.1; NM_001109991.1. [P39061-1]
DR RefSeq; NP_034059.2; NM_009929.3. [P39061-2]
DR PDB; 1DY0; X-ray; 2.20 A; A=1587-1774.
DR PDB; 1DY1; X-ray; 2.20 A; A=1587-1774.
DR PDB; 1KOE; X-ray; 1.50 A; A=1597-1768.
DR PDBsum; 1DY0; -.
DR PDBsum; 1DY1; -.
DR PDBsum; 1KOE; -.
DR AlphaFoldDB; P39061; -.
DR SMR; P39061; -.
DR BioGRID; 198812; 5.
DR ComplexPortal; CPX-2996; Collagen type XVIII trimer.
DR GlyGen; P39061; 4 sites.
DR iPTMnet; P39061; -.
DR PhosphoSitePlus; P39061; -.
DR jPOST; P39061; -.
DR MaxQB; P39061; -.
DR PaxDb; P39061; -.
DR PeptideAtlas; P39061; -.
DR PRIDE; P39061; -.
DR ProteomicsDB; 285239; -. [P39061-3]
DR ProteomicsDB; 285240; -. [P39061-1]
DR ProteomicsDB; 285241; -. [P39061-2]
DR Antibodypedia; 2814; 606 antibodies from 37 providers.
DR DNASU; 12822; -.
DR Ensembl; ENSMUST00000081654; ENSMUSP00000080358; ENSMUSG00000001435. [P39061-2]
DR Ensembl; ENSMUST00000105409; ENSMUSP00000101049; ENSMUSG00000001435. [P39061-1]
DR GeneID; 12822; -.
DR KEGG; mmu:12822; -.
DR UCSC; uc007fvg.1; mouse. [P39061-1]
DR UCSC; uc007fvh.2; mouse. [P39061-2]
DR CTD; 80781; -.
DR MGI; MGI:88451; Col18a1.
DR VEuPathDB; HostDB:ENSMUSG00000001435; -.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158212; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; P39061; -.
DR PhylomeDB; P39061; -.
DR TreeFam; TF315821; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12822; 3 hits in 59 CRISPR screens.
DR ChiTaRS; Col18a1; mouse.
DR EvolutionaryTrace; P39061; -.
DR PRO; PR:P39061; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P39061; protein.
DR Bgee; ENSMUSG00000001435; Expressed in aorta tunica media and 274 other tissues.
DR ExpressionAtlas; P39061; baseline and differential.
DR Genevisible; P39061; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IDA:MGI.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IDA:MGI.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IDA:MGI.
DR GO; GO:0101023; P:vascular endothelial cell proliferation; IDA:MGI.
DR CDD; cd07455; CRD_Collagen_XVIII; 1.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR035523; Collagen_XVIII_Fz.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Basement membrane; Cell adhesion; Collagen; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1774
FT /note="Collagen alpha-1(XVIII) chain"
FT /id="PRO_0000005795"
FT CHAIN 1591..1774
FT /note="Endostatin"
FT /id="PRO_0000005796"
FT CHAIN ?..1774
FT /note="Non-collagenous domain 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441862"
FT DOMAIN 365..482
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 522..704
FT /note="Laminin G-like"
FT DOMAIN 823..878
FT /note="Collagen-like 1"
FT DOMAIN 953..1007
FT /note="Collagen-like 2"
FT DOMAIN 1008..1041
FT /note="Collagen-like 3"
FT DOMAIN 1066..1117
FT /note="Collagen-like 4"
FT DOMAIN 1118..1147
FT /note="Collagen-like 5"
FT DOMAIN 1162..1202
FT /note="Collagen-like 6"
FT DOMAIN 1216..1264
FT /note="Collagen-like 7"
FT REGION 27..785
FT /note="Nonhelical region 1 (NC1)"
FT REGION 47..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..812
FT /note="Triple-helical region 1 (COL1)"
FT REGION 813..822
FT /note="Nonhelical region 2 (NC2)"
FT REGION 823..896
FT /note="Triple-helical region 2 (COL2)"
FT REGION 897..920
FT /note="Nonhelical region 3 (NC3)"
FT REGION 921..1042
FT /note="Triple-helical region 3 (COL3)"
FT REGION 1043..1065
FT /note="Nonhelical region 4 (NC4)"
FT REGION 1066..1148
FT /note="Triple-helical region 4 (COL4)"
FT REGION 1149..1162
FT /note="Nonhelical region 5 (NC5)"
FT REGION 1163..1204
FT /note="Triple-helical region 5 (COL5)"
FT REGION 1205..1217
FT /note="Nonhelical region 6 (NC6)"
FT REGION 1218..1290
FT /note="Triple-helical region 6 (COL6)"
FT REGION 1291..1300
FT /note="Nonhelical region 7 (NC7)"
FT REGION 1301..1333
FT /note="Triple-helical region 7 (COL7)"
FT REGION 1334..1345
FT /note="Nonhelical region 8 (NC8)"
FT REGION 1346..1369
FT /note="Triple-helical region 8 (COL8)"
FT REGION 1370..1376
FT /note="Nonhelical region 9 (NC9)"
FT REGION 1377..1428
FT /note="Triple-helical region 9 (COL9)"
FT REGION 1429..1441
FT /note="Nonhelical region 10 (NC10)"
FT REGION 1442..1459
FT /note="Triple-helical region 10 (COL10)"
FT REGION 1460..1774
FT /note="Nonhelical region 11 (NC11)"
FT REGION 1474..1519
FT /note="Non-collagenous domain 1 association domain"
FT /evidence="ECO:0000305|PubMed:10966814"
FT REGION 1520..1590
FT /note="Non-collagenous domain 1 hinge region"
FT /evidence="ECO:0000305|PubMed:10966814"
FT MOTIF 1351..1353
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 50..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1042
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1591
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 1666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P39060"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 370..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 380..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 417..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 444..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 448..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 1623..1763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:10704302"
FT DISULFID 1725..1755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:10704302"
FT VAR_SEQ 1..459
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7876242,
FT ECO:0000303|PubMed:8183894, ECO:0000303|PubMed:8188673"
FT /id="VSP_001157"
FT VAR_SEQ 240..486
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008303"
FT VAR_SEQ 460..486
FT /note="AGDRLPVVCASLPSQEDGYCVFIGPAA -> MAPRWHLLDVLTSLVLLLVAR
FT VSWAEP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7876242,
FT ECO:0000303|PubMed:8183894, ECO:0000303|PubMed:8188673"
FT /id="VSP_001158"
FT MUTAGEN 1591
FT /note="H->A: No effect on zinc binding."
FT /evidence="ECO:0000269|PubMed:10704302"
FT MUTAGEN 1593
FT /note="H->A: Reduces zinc binding by 60%. Abolishes zinc
FT binding; when associated with A-1595."
FT /evidence="ECO:0000269|PubMed:10704302"
FT MUTAGEN 1595
FT /note="D->A: No effect on zinc binding. Abolishes zinc
FT binding; when associated with A-1593."
FT /evidence="ECO:0000269|PubMed:10704302"
FT MUTAGEN 1666
FT /note="D->A: Abolishes zinc binding."
FT /evidence="ECO:0000269|PubMed:10704302"
FT CONFLICT 1046
FT /note="G -> V (in Ref. 4; AAH66080)"
FT /evidence="ECO:0000305"
FT CONFLICT 1147
FT /note="P -> L (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1194
FT /note="P -> F (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1211
FT /note="A -> R (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1347
FT /note="D -> V (in Ref. 6; BAC27554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1404
FT /note="P -> R (in Ref. 1; AAA20657, 2; AAC52901/AAC52902/
FT AAC52903 and 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="P -> L (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="L -> F (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT CONFLICT 1684
FT /note="L -> V (in Ref. 8; AAA19787)"
FT /evidence="ECO:0000305"
FT STRAND 1600..1604
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1611..1614
FT /evidence="ECO:0007829|PDB:1DY0"
FT HELIX 1615..1629
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1636..1639
FT /evidence="ECO:0007829|PDB:1KOE"
FT HELIX 1647..1650
FT /evidence="ECO:0007829|PDB:1KOE"
FT HELIX 1653..1655
FT /evidence="ECO:0007829|PDB:1KOE"
FT TURN 1656..1658
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1668..1671
FT /evidence="ECO:0007829|PDB:1KOE"
FT HELIX 1673..1676
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1678..1680
FT /evidence="ECO:0007829|PDB:1KOE"
FT TURN 1698..1700
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1704..1706
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1708..1710
FT /evidence="ECO:0007829|PDB:1KOE"
FT HELIX 1725..1728
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1736..1741
FT /evidence="ECO:0007829|PDB:1KOE"
FT HELIX 1742..1744
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1751..1754
FT /evidence="ECO:0007829|PDB:1KOE"
FT STRAND 1762..1765
FT /evidence="ECO:0007829|PDB:1KOE"
SQ SEQUENCE 1774 AA; 182172 MW; BEA79BADD1E34407 CRC64;
MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE GPVSKPQNSS
PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ KAGQGGSPAT PAVPIPLVAP
AASPDMKEEN VAGVGAKILN VAQGIRSFVQ LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE
LSSAPQGSKT TLWLSSAIPS SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPG
RAFLSSSTDQ GSSWGNQEPP RQPQHLEGKG FLPMTARSSQ QHRHSDVHSD IHGHVPLLPL
VTGPLVTASL SVHGLLSVPS SDPSGQLSQV AALPGFPGTW VSHVAPSSGT GLSNDSALAG
NGSLTSTSRC LPLPPTLTLC SRLGIGHFWL PNHLHHTDSV EVEATVQAWG RFLHTNCHPF
LAWFFCLLLA PSCGPGPPPP LPPCRQFCEA LEDECWNYLA GDRLPVVCAS LPSQEDGYCV
FIGPAAENVA EEVGLLQLLG DPLPEKISQI DDPHVGPAYI FGPDSNSGQV AQYHFPKLFF
RDFSLLFHVR PATEAAGVLF AITDAAQVVV SLGVKLSEVR DGQQNISLLY TEPGASQTQT
GASFRLPAFV GQWTHFALSV DGGSVALYVD CEEFQRVPFA RASQGLELER GAGLFVGQAG
TADPDKFQGM ISELKVRKTP RVSPVHCLDE EDDDEDRASG DFGSGFEESS KSHKEDTSLL
PGLPQPPPVT SPPLAGGSTT EDPRTEETEE DAAVDSIGAE TLPGTGSSGA WDEAIQNPGR
GLIKGGMKGQ KGEPGAQGPP GPAGPQGPAG PVVQSPNSQP VPGAQGPPGP QGPPGKDGTP
GRDGEPGDPG EDGRPGDTGP QGFPGTPGDV GPKGEKGDPG IGPRGPPGPP GPPGPSFRQD
KLTFIDMEGS GFSGDIESLR GPRGFPGPPG PPGVPGLPGE PGRFGINGSY APGPAGLPGV
PGKEGPPGFP GPPGPPGPPG KEGPPGVAGQ KGSVGDVGIP GPKGSKGDLG PIGMPGKSGL
AGSPGPVGPP GPPGPPGPPG PGFAAGFDDM EGSGIPLWTT ARSSDGLQGP PGSPGLKGDP
GVAGLPGAKG EVGADGAQGI PGPPGREGAA GSPGPKGEKG MPGEKGNPGK DGVGRPGLPG
PPGPPGPVIY VSSEDKAIVS TPGPEGKPGY AGFPGPAGPK GDLGSKGEQG LPGPKGEKGE
PGTIFSPDGR ALGHPQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GTNGLKGEKG
EPGDASLGFS MRGLPGPPGP PGPPGPPGMP IYDSNAFVES GRPGLPGQQG VQGPSGPKGD
KGEVGPPGPP GQFPIDLFHL EAEMKGDKGD RGDAGQKGER GEPGAPGGGF FSSSVPGPPG
PPGYPGIPGP KGESIRGPPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV
PGPPGPPGPP GPPGAMGASA GQVRIWATYQ TMLDKIREVP EGWLIFVAER EELYVRVRNG
FRKVLLEART ALPRGTGNEV AALQPPLVQL HEGSPYTRRE YSYSTARPWR ADDILANPPR
LPDRQPYPGV PHHHSSYVHL PPARPTLSLA HTHQDFQPVL HLVALNTPLS GGMRGIRGAD
FQCFQQARAV GLSGTFRAFL SSRLQDLYSI VRRADRGSVP IVNLKDEVLS PSWDSLFSGS
QGQLQPGARI FSFDGRDVLR HPAWPQKSVW HGSDPSGRRL MESYCETWRT ETTGATGQAS
SLLSGRLLEQ KAASCHNSYI VLCIENSFMT SFSK
