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P39061

- COIA1_MOUSE

UniProt

P39061 - COIA1_MOUSE

Protein

Collagen alpha-1(XVIII) chain

Gene

Col18a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1591 – 15911Zinc; alternate
    Metal bindingi1593 – 15931Zinc
    Metal bindingi1595 – 15951Zinc; alternate
    Metal bindingi1601 – 16011Zinc
    Metal bindingi1666 – 16661Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. cell adhesion Source: UniProtKB-KW
    3. endothelial cell morphogenesis Source: MGI
    4. extracellular matrix organization Source: MGI
    5. positive regulation of cell migration Source: MGI
    6. positive regulation of cell proliferation Source: MGI
    7. positive regulation of endothelial cell apoptotic process Source: MGI
    8. response to drug Source: Ensembl
    9. response to hydrostatic pressure Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199055. Collagen degradation.
    REACT_202342. Laminin interactions.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XVIII) chain
    Cleaved into the following chain:
    Gene namesi
    Name:Col18a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:88451. Col18a1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. collagen trimer Source: UniProtKB-KW
    3. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1591 – 15911H → A: No effect on zinc binding. 1 Publication
    Mutagenesisi1593 – 15931H → A: Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595. 1 Publication
    Mutagenesisi1595 – 15951D → A: No effect on zinc binding. Abolishes zinc binding; when associated with A-1593. 1 Publication
    Mutagenesisi1666 – 16661D → A: Abolishes zinc binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 17741748Collagen alpha-1(XVIII) chainPRO_0000005795Add
    BLAST
    Chaini1591 – 1774184EndostatinPRO_0000005796Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi370 ↔ 433PROSITE-ProRule annotation
    Disulfide bondi380 ↔ 426PROSITE-ProRule annotation
    Disulfide bondi417 ↔ 455PROSITE-ProRule annotation
    Disulfide bondi444 ↔ 479PROSITE-ProRule annotation
    Disulfide bondi448 ↔ 468PROSITE-ProRule annotation
    Glycosylationi585 – 5851N-linked (GlcNAc...)1 Publication
    Glycosylationi947 – 9471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1623 ↔ 17631 PublicationPROSITE-ProRule annotation
    Disulfide bondi1725 ↔ 17551 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiP39061.
    PaxDbiP39061.
    PRIDEiP39061.

    PTM databases

    PhosphoSiteiP39061.

    Miscellaneous databases

    PMAP-CutDBP39061.

    Expressioni

    Tissue specificityi

    Expressed in liver, kidney, lung, skeletal muscle and testis.1 Publication

    Gene expression databases

    ArrayExpressiP39061.
    BgeeiP39061.
    CleanExiMM_COL18A1.
    GenevestigatoriP39061.

    Interactioni

    Protein-protein interaction databases

    BioGridi198812. 1 interaction.

    Structurei

    Secondary structure

    1
    1774
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1600 – 16045
    Beta strandi1611 – 16144
    Helixi1615 – 162915
    Beta strandi1636 – 16394
    Helixi1647 – 16504
    Helixi1653 – 16553
    Turni1656 – 16583
    Beta strandi1668 – 16714
    Helixi1673 – 16764
    Beta strandi1678 – 16803
    Turni1698 – 17003
    Beta strandi1704 – 17063
    Beta strandi1708 – 17103
    Helixi1725 – 17284
    Beta strandi1736 – 17416
    Helixi1742 – 17443
    Beta strandi1751 – 17544
    Beta strandi1762 – 17654

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DY0X-ray2.20A1587-1774[»]
    1DY1X-ray2.20A1587-1774[»]
    1KOEX-ray1.50A1597-1768[»]
    ProteinModelPortaliP39061.
    SMRiP39061. Positions 376-474, 1463-1514, 1597-1768.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39061.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini365 – 482118FZPROSITE-ProRule annotationAdd
    BLAST
    Domaini522 – 704183Laminin G-likeAdd
    BLAST
    Domaini823 – 87856Collagen-like 1Add
    BLAST
    Domaini953 – 100755Collagen-like 2Add
    BLAST
    Domaini1008 – 104134Collagen-like 3Add
    BLAST
    Domaini1066 – 111752Collagen-like 4Add
    BLAST
    Domaini1118 – 114730Collagen-like 5Add
    BLAST
    Domaini1162 – 120241Collagen-like 6Add
    BLAST
    Domaini1216 – 126449Collagen-like 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 785759Nonhelical region 1 (NC1)Add
    BLAST
    Regioni786 – 81227Triple-helical region 1 (COL1)Add
    BLAST
    Regioni813 – 82210Nonhelical region 2 (NC2)
    Regioni823 – 89674Triple-helical region 2 (COL2)Add
    BLAST
    Regioni897 – 92024Nonhelical region 3 (NC3)Add
    BLAST
    Regioni921 – 1042122Triple-helical region 3 (COL3)Add
    BLAST
    Regioni1043 – 106523Nonhelical region 4 (NC4)Add
    BLAST
    Regioni1066 – 114883Triple-helical region 4 (COL4)Add
    BLAST
    Regioni1149 – 116214Nonhelical region 5 (NC5)Add
    BLAST
    Regioni1163 – 120442Triple-helical region 5 (COL5)Add
    BLAST
    Regioni1205 – 121713Nonhelical region 6 (NC6)Add
    BLAST
    Regioni1218 – 129073Triple-helical region 6 (COL6)Add
    BLAST
    Regioni1291 – 130010Nonhelical region 7 (NC7)
    Regioni1301 – 133333Triple-helical region 7 (COL7)Add
    BLAST
    Regioni1334 – 134512Nonhelical region 8 (NC8)Add
    BLAST
    Regioni1346 – 136924Triple-helical region 8 (COL8)Add
    BLAST
    Regioni1370 – 13767Nonhelical region 9 (NC9)
    Regioni1377 – 142852Triple-helical region 9 (COL9)Add
    BLAST
    Regioni1429 – 144113Nonhelical region 10 (NC10)Add
    BLAST
    Regioni1442 – 145918Triple-helical region 10 (COL10)Add
    BLAST
    Regioni1460 – 1774315Nonhelical region 11 (NC11)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1351 – 13533Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the multiplexin collagen family.Curated
    Contains 7 collagen-like domains.Curated
    Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00710000106713.
    HOVERGENiHBG053241.
    InParanoidiP39061.
    KOiK06823.
    OrthoDBiEOG7NSB2B.
    PhylomeDBiP39061.
    TreeFamiTF315821.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    2.60.120.200. 1 hit.
    3.10.100.10. 1 hit.
    InterProiIPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR026917. COL18A1.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR010363. DUF959_COL18_N.
    IPR020067. Frizzled_dom.
    IPR001791. Laminin_G.
    [Graphical view]
    PANTHERiPTHR24023:SF390. PTHR24023:SF390. 1 hit.
    PfamiPF01391. Collagen. 7 hits.
    PF06121. DUF959. 1 hit.
    PF06482. Endostatin. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view]
    SMARTiSM00063. FRI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 1 hit.
    SSF63501. SSF63501. 1 hit.
    PROSITEiPS50038. FZ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: P39061-3) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE     50
    GPVSKPQNSS PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ 100
    KAGQGGSPAT PAVPIPLVAP AASPDMKEEN VAGVGAKILN VAQGIRSFVQ 150
    LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE LSSAPQGSKT TLWLSSAIPS 200
    SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPG RAFLSSSTDQ 250
    GSSWGNQEPP RQPQHLEGKG FLPMTARSSQ QHRHSDVHSD IHGHVPLLPL 300
    VTGPLVTASL SVHGLLSVPS SDPSGQLSQV AALPGFPGTW VSHVAPSSGT 350
    GLSNDSALAG NGSLTSTSRC LPLPPTLTLC SRLGIGHFWL PNHLHHTDSV 400
    EVEATVQAWG RFLHTNCHPF LAWFFCLLLA PSCGPGPPPP LPPCRQFCEA 450
    LEDECWNYLA GDRLPVVCAS LPSQEDGYCV FIGPAAENVA EEVGLLQLLG 500
    DPLPEKISQI DDPHVGPAYI FGPDSNSGQV AQYHFPKLFF RDFSLLFHVR 550
    PATEAAGVLF AITDAAQVVV SLGVKLSEVR DGQQNISLLY TEPGASQTQT 600
    GASFRLPAFV GQWTHFALSV DGGSVALYVD CEEFQRVPFA RASQGLELER 650
    GAGLFVGQAG TADPDKFQGM ISELKVRKTP RVSPVHCLDE EDDDEDRASG 700
    DFGSGFEESS KSHKEDTSLL PGLPQPPPVT SPPLAGGSTT EDPRTEETEE 750
    DAAVDSIGAE TLPGTGSSGA WDEAIQNPGR GLIKGGMKGQ KGEPGAQGPP 800
    GPAGPQGPAG PVVQSPNSQP VPGAQGPPGP QGPPGKDGTP GRDGEPGDPG 850
    EDGRPGDTGP QGFPGTPGDV GPKGEKGDPG IGPRGPPGPP GPPGPSFRQD 900
    KLTFIDMEGS GFSGDIESLR GPRGFPGPPG PPGVPGLPGE PGRFGINGSY 950
    APGPAGLPGV PGKEGPPGFP GPPGPPGPPG KEGPPGVAGQ KGSVGDVGIP 1000
    GPKGSKGDLG PIGMPGKSGL AGSPGPVGPP GPPGPPGPPG PGFAAGFDDM 1050
    EGSGIPLWTT ARSSDGLQGP PGSPGLKGDP GVAGLPGAKG EVGADGAQGI 1100
    PGPPGREGAA GSPGPKGEKG MPGEKGNPGK DGVGRPGLPG PPGPPGPVIY 1150
    VSSEDKAIVS TPGPEGKPGY AGFPGPAGPK GDLGSKGEQG LPGPKGEKGE 1200
    PGTIFSPDGR ALGHPQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP 1250
    GTNGLKGEKG EPGDASLGFS MRGLPGPPGP PGPPGPPGMP IYDSNAFVES 1300
    GRPGLPGQQG VQGPSGPKGD KGEVGPPGPP GQFPIDLFHL EAEMKGDKGD 1350
    RGDAGQKGER GEPGAPGGGF FSSSVPGPPG PPGYPGIPGP KGESIRGPPG 1400
    PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV PGPPGPPGPP 1450
    GPPGAMGASA GQVRIWATYQ TMLDKIREVP EGWLIFVAER EELYVRVRNG 1500
    FRKVLLEART ALPRGTGNEV AALQPPLVQL HEGSPYTRRE YSYSTARPWR 1550
    ADDILANPPR LPDRQPYPGV PHHHSSYVHL PPARPTLSLA HTHQDFQPVL 1600
    HLVALNTPLS GGMRGIRGAD FQCFQQARAV GLSGTFRAFL SSRLQDLYSI 1650
    VRRADRGSVP IVNLKDEVLS PSWDSLFSGS QGQLQPGARI FSFDGRDVLR 1700
    HPAWPQKSVW HGSDPSGRRL MESYCETWRT ETTGATGQAS SLLSGRLLEQ 1750
    KAASCHNSYI VLCIENSFMT SFSK 1774

    Note: Produced by alternative promoter usage.

    Length:1,774
    Mass (Da):182,172
    Last modified:May 1, 2007 - v4
    Checksum:iBEA79BADD1E34407
    GO
    Isoform 2 (identifier: P39061-1) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,527
    Mass (Da):155,950
    Checksum:iE7AF043EC82D0326
    GO
    Isoform 3 (identifier: P39061-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,315
    Mass (Da):134,204
    Checksum:iB8215602ACE7AD1F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1046 – 10461G → V in AAH66080. (PubMed:15489334)Curated
    Sequence conflicti1147 – 11471P → L in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1194 – 11941P → F in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1211 – 12111A → R in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1347 – 13471D → V in BAC27554. (PubMed:16141072)Curated
    Sequence conflicti1404 – 14041P → R in AAA20657. (PubMed:8188673)Curated
    Sequence conflicti1404 – 14041P → R in AAC52901. (PubMed:8838808)Curated
    Sequence conflicti1404 – 14041P → R in AAC52902. (PubMed:8838808)Curated
    Sequence conflicti1404 – 14041P → R in AAC52903. (PubMed:8838808)Curated
    Sequence conflicti1404 – 14041P → R in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1513 – 15131P → L in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1523 – 15231L → F in AAA19787. (PubMed:8183893)Curated
    Sequence conflicti1684 – 16841L → V in AAA19787. (PubMed:8183893)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 459459Missing in isoform 3. 5 PublicationsVSP_001157Add
    BLAST
    Alternative sequencei240 – 486247Missing in isoform 2. CuratedVSP_008303Add
    BLAST
    Alternative sequencei460 – 48627AGDRL…IGPAA → MAPRWHLLDVLTSLVLLLVA RVSWAEP in isoform 3. 5 PublicationsVSP_001158Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS23953.1. [P39061-2]
    CCDS48604.1. [P39061-1]
    PIRiA56101.
    B56101.
    RefSeqiNP_001103461.1. NM_001109991.1. [P39061-1]
    NP_034059.2. NM_009929.3. [P39061-2]
    UniGeneiMm.4352.

    Genome annotation databases

    EnsembliENSMUST00000081654; ENSMUSP00000080358; ENSMUSG00000001435. [P39061-2]
    ENSMUST00000105409; ENSMUSP00000101049; ENSMUSG00000001435. [P39061-1]
    GeneIDi12822.
    KEGGimmu:12822.
    UCSCiuc007fvg.1. mouse. [P39061-1]
    uc007fvh.2. mouse. [P39061-2]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS23953.1. [P39061-2 ]
    CCDS48604.1. [P39061-1 ]
    PIRi A56101.
    B56101.
    RefSeqi NP_001103461.1. NM_001109991.1. [P39061-1 ]
    NP_034059.2. NM_009929.3. [P39061-2 ]
    UniGenei Mm.4352.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DY0 X-ray 2.20 A 1587-1774 [» ]
    1DY1 X-ray 2.20 A 1587-1774 [» ]
    1KOE X-ray 1.50 A 1597-1768 [» ]
    ProteinModelPortali P39061.
    SMRi P39061. Positions 376-474, 1463-1514, 1597-1768.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198812. 1 interaction.

    PTM databases

    PhosphoSitei P39061.

    Proteomic databases

    MaxQBi P39061.
    PaxDbi P39061.
    PRIDEi P39061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081654 ; ENSMUSP00000080358 ; ENSMUSG00000001435 . [P39061-2 ]
    ENSMUST00000105409 ; ENSMUSP00000101049 ; ENSMUSG00000001435 . [P39061-1 ]
    GeneIDi 12822.
    KEGGi mmu:12822.
    UCSCi uc007fvg.1. mouse. [P39061-1 ]
    uc007fvh.2. mouse. [P39061-2 ]

    Organism-specific databases

    CTDi 80781.
    MGIi MGI:88451. Col18a1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00710000106713.
    HOVERGENi HBG053241.
    InParanoidi P39061.
    KOi K06823.
    OrthoDBi EOG7NSB2B.
    PhylomeDBi P39061.
    TreeFami TF315821.

    Enzyme and pathway databases

    Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199055. Collagen degradation.
    REACT_202342. Laminin interactions.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi COL18A1. mouse.
    EvolutionaryTracei P39061.
    NextBioi 282298.
    PMAP-CutDB P39061.
    PROi P39061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39061.
    Bgeei P39061.
    CleanExi MM_COL18A1.
    Genevestigatori P39061.

    Family and domain databases

    Gene3Di 1.10.2000.10. 1 hit.
    2.60.120.200. 1 hit.
    3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR026917. COL18A1.
    IPR008160. Collagen.
    IPR010515. Collagenase_NC10/endostatin.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR010363. DUF959_COL18_N.
    IPR020067. Frizzled_dom.
    IPR001791. Laminin_G.
    [Graphical view ]
    PANTHERi PTHR24023:SF390. PTHR24023:SF390. 1 hit.
    Pfami PF01391. Collagen. 7 hits.
    PF06121. DUF959. 1 hit.
    PF06482. Endostatin. 1 hit.
    PF01392. Fz. 1 hit.
    [Graphical view ]
    SMARTi SM00063. FRI. 1 hit.
    SM00282. LamG. 1 hit.
    SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF56436. SSF56436. 1 hit.
    SSF63501. SSF63501. 1 hit.
    PROSITEi PS50038. FZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
    3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585.
    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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ENDOSTATIN.
    14. 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.

    Entry informationi

    Entry nameiCOIA1_MOUSE
    AccessioniPrimary (citable) accession number: P39061
    Secondary accession number(s): Q60672
    , Q61434, Q61437, Q62001, Q62002, Q6NZK9, Q6P1Y4, Q8CCZ8, Q9CRT2, Q9JK63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3