Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P39060

- COIA1_HUMAN

UniProt

P39060 - COIA1_HUMAN

Protein

Collagen alpha-1(XVIII) chain

Gene

COL18A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 5 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1572 – 15721Zinc
    Metal bindingi1574 – 15741Zinc
    Metal bindingi1582 – 15821Zinc
    Metal bindingi1647 – 16471Zinc

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. structural molecule activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. collagen catabolic process Source: Reactome
    4. endothelial cell morphogenesis Source: Ensembl
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. negative regulation of cell proliferation Source: ProtInc
    8. organ morphogenesis Source: ProtInc
    9. positive regulation of cell migration Source: Ensembl
    10. positive regulation of cell proliferation Source: Ensembl
    11. positive regulation of endothelial cell apoptotic process Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to hydrostatic pressure Source: Ensembl
    14. visual perception Source: ProtInc

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_169262. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XVIII) chain
    Cleaved into the following chain:
    Gene namesi
    Name:COL18A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:2195. COL18A1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. collagen trimer Source: ProtInc
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular space Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi267750. phenotype.
    Orphaneti1571. Knobloch syndrome.
    PharmGKBiPA26711.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 17541731Collagen alpha-1(XVIII) chainPRO_0000005793Add
    BLAST
    Chaini1572 – 1754183EndostatinPRO_0000005794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi334 ↔ 397PROSITE-ProRule annotation
    Disulfide bondi344 ↔ 390PROSITE-ProRule annotation
    Disulfide bondi381 ↔ 419PROSITE-ProRule annotation
    Disulfide bondi408 ↔ 443PROSITE-ProRule annotation
    Disulfide bondi412 ↔ 432PROSITE-ProRule annotation
    Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1567 – 15671O-linked (GalNAc...)CAR_000150
    Disulfide bondi1604 ↔ 1744PROSITE-ProRule annotation
    Disulfide bondi1706 ↔ 1736PROSITE-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

    MaxQBiP39060.
    PaxDbiP39060.
    PRIDEiP39060.

    PTM databases

    PhosphoSiteiP39060.
    UniCarbKBiP39060.

    Expressioni

    Tissue specificityi

    Present in multiple organs with highest levels in liver, lung and kidney.

    Gene expression databases

    ArrayExpressiP39060.
    BgeeiP39060.
    GenevestigatoriP39060.

    Organism-specific databases

    HPAiCAB001961.
    HPA011025.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-981314,EBI-981314
    APPP050672EBI-2566375,EBI-821758
    NCLP1933812EBI-2566375,EBI-346967
    PCOLCEQ151134EBI-2566375,EBI-8869614
    TGM2P219802EBI-2566375,EBI-727668

    Protein-protein interaction databases

    BioGridi123311. 4 interactions.
    IntActiP39060. 14 interactions.

    Structurei

    Secondary structure

    1
    1754
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1445 – 14506
    Helixi1451 – 14577
    Helixi1458 – 14603
    Beta strandi1466 – 14694
    Turni1470 – 14734
    Beta strandi1474 – 14796
    Beta strandi1482 – 14865
    Beta strandi1488 – 14936
    Beta strandi1581 – 15855
    Helixi1597 – 161014
    Beta strandi1617 – 16215
    Helixi1629 – 16313
    Helixi1634 – 16363
    Beta strandi1649 – 16524
    Helixi1654 – 16574
    Helixi1679 – 16813
    Beta strandi1689 – 16913
    Helixi1706 – 17094
    Beta strandi1716 – 17227
    Helixi1723 – 17253
    Beta strandi1727 – 17293
    Beta strandi1732 – 17354
    Beta strandi1743 – 17475

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BNLX-ray2.90A/B/C/D1572-1749[»]
    3HONX-ray3.00A1441-1496[»]
    3HSHX-ray1.80A/B/C/D/E/F1441-1496[»]
    ProteinModelPortaliP39060.
    SMRiP39060. Positions 338-444, 1441-1496, 1572-1749.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39060.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini329 – 446118FZPROSITE-ProRule annotationAdd
    BLAST
    Domaini456 – 644189Laminin G-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni645 – 751107Nonhelical region 1 (NC1)Add
    BLAST
    Regioni752 – 78534Triple-helical region 1 (COL1)Add
    BLAST
    Regioni786 – 79510Nonhelical region 2 (NC2)
    Regioni796 – 87580Triple-helical region 2 (COL2)Add
    BLAST
    Regioni876 – 89924Nonhelical region 3 (NC3)Add
    BLAST
    Regioni900 – 1021122Triple-helical region 3 (COL3)Add
    BLAST
    Regioni1022 – 104423Nonhelical region 4 (NC4)Add
    BLAST
    Regioni1045 – 112783Triple-helical region 4 (COL4)Add
    BLAST
    Regioni1128 – 114114Nonhelical region 5 (NC5)Add
    BLAST
    Regioni1142 – 118342Triple-helical region 5 (COL5)Add
    BLAST
    Regioni1184 – 119613Nonhelical region 6 (NC6)Add
    BLAST
    Regioni1197 – 126973Triple-helical region 6 (COL6)Add
    BLAST
    Regioni1270 – 127910Nonhelical region 7 (NC7)
    Regioni1280 – 131233Triple-helical region 7 (COL7)Add
    BLAST
    Regioni1313 – 132412Nonhelical region 8 (NC8)Add
    BLAST
    Regioni1325 – 134622Triple-helical region 8 (COL8)Add
    BLAST
    Regioni1347 – 13537Nonhelical region 9 (NC9)
    Regioni1354 – 141158Triple-helical region 9 (COL9)Add
    BLAST
    Regioni1412 – 142413Nonhelical region 10 (NC10)Add
    BLAST
    Regioni1425 – 144218Triple-helical region 10 (COL10)Add
    BLAST
    Regioni1443 – 1754312Nonhelical region 11 (NC11)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1330 – 13323Cell attachment siteSequence Analysis

    Sequence similaritiesi

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

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG053241.
    InParanoidiP39060.
    KOiK06823.
    OMAiPFWSTAR.
    OrthoDBiEOG7NSB2B.
    PhylomeDBiP39060.
    TreeFamiTF315821.

    Family and domain databases

    Gene3Di1.10.2000.10. 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.
    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: P39060-3) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG     50
    PLPVQPTADT TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP 100
    DAPEENIAGV GAEILNVAKG IRSFVQLWND TVPTESLARA ETLVLETPVG 150
    PLALAGPSST PQENGTTLWP SRGIPSSPGA HTTEAGTLPA PTPSPPSLGR 200
    PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG LSPAAAAPSQ 250
    QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD 300
    SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS 350
    RFWLPNHLHH ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV 400
    PPPAPPPCCQ FCEALQDACW SRLGGGRLPV ACASLPTQED GYCVLIGPAA 450
    ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG LAYVFGPDAN SGQVARYHFP 500
    SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL SGVQDGHQDI 550
    SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR 600
    MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH 650
    CLDEEGDDSD GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL 700
    AGGSSTEDSR SEEVEEQTTV ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE 750
    GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP PGLPCPVSPL GPAGPALQTV 800
    PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP GTPGDVGPKG 850
    DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG 900
    PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG 950
    LPGPPGPPGR EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA 1000
    GAPGPAGPPG PPGPPGPPGP GLPAGFDDME GSGGPFWSTA RSADGPQGPP 1050
    GLPGLKGDPG VPGLPGAKGE VGADGVPGFP GLPGREGIAG PQGPKGDRGS 1100
    RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV PGPEGRPGFA 1150
    GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG 1200
    EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM 1250
    RGMPGPPGPP GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK 1300
    GEVGPPGPPG QFPFDFLQLE AEMKGEKGDR GDAGQKGERG EPGGGGFFGS 1350
    SLPGPPGPPG PPGPRGYPGI PGPKGESIRG QPGPPGPQGP PGIGYEGRQG 1400
    PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG ASSGVRLWAT 1450
    RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN 1500
    EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP 1550
    GAPHHSSYVH LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA 1600
    DFQCFQQARA VGLAGTFRAF LSSRLQDLYS IVRRADRAAV PIVNLKDELL 1650
    FPSWEALFSG SEGPLKPGAR IFSFDGKDVL RHPTWPQKSV WHGSDPNGRR 1700
    LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY IVLCIENSFM 1750
    TASK 1754

    Note: Produced by alternative promoter usage.

    Length:1,754
    Mass (Da):178,188
    Last modified:November 25, 2008 - v5
    Checksum:i23A327DCBD3B328D
    GO
    Isoform 2 (identifier: P39060-1) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,519
    Mass (Da):154,018
    Checksum:i7456050495512DE2
    GO
    Isoform 3 (identifier: P39060-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,339
    Mass (Da):135,761
    Checksum:iA8171B3EC21CBBF0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti299 – 2991R → K in AAR83296. (PubMed:14614989)Curated
    Sequence conflicti663 – 6631S → F in AAC39658. (PubMed:9503365)Curated
    Sequence conflicti663 – 6631S → F in AAC39659. (PubMed:9503365)Curated
    Sequence conflicti1112 – 11121V → L in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1147 – 11471P → R in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1168 – 11681R → L in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1210 – 12101P → L in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1299 – 12991A → P in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1319 – 13191L → K in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1355 – 13551P → A in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1358 – 13581P → A in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1362 – 13643Missing in AAC39658. (PubMed:9503365)Curated
    Sequence conflicti1362 – 13643Missing in AAC39659. (PubMed:9503365)Curated
    Sequence conflicti1362 – 13643Missing in AAR83296. (PubMed:14614989)Curated
    Sequence conflicti1362 – 13643Missing in AAR83297. (PubMed:14614989)Curated
    Sequence conflicti1362 – 13643Missing in AAR83298. (PubMed:14614989)Curated
    Sequence conflicti1362 – 13643Missing in AAH33715. (PubMed:15489334)Curated
    Sequence conflicti1362 – 13643Missing in AAH63833. (PubMed:15489334)Curated
    Sequence conflicti1362 – 13643Missing in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1444 – 14441G → GQ in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1542 – 15421R → G in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1552 – 15521A → G in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1561 – 15622LR → CG in AAA51864. (PubMed:8188291)Curated
    Sequence conflicti1681 – 16811R → T in AAF01310. 1 PublicationCurated
    Sequence conflicti1685 – 16851W → R in AAK50626. 1 PublicationCurated
    Sequence conflicti1721 – 17211S → Y in AAF01310. 1 PublicationCurated
    Sequence conflicti1736 – 17361C → S in AAK50626. 1 PublicationCurated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491Q → L.1 Publication
    Corresponds to variant rs61735029 [ dbSNP | Ensembl ].
    VAR_018053
    Natural varianti111 – 1111G → R.1 Publication
    Corresponds to variant rs114139997 [ dbSNP | Ensembl ].
    VAR_018054
    Natural varianti288 – 2881A → T.
    Corresponds to variant rs11702494 [ dbSNP | Ensembl ].
    VAR_059232
    Natural varianti379 – 3791T → M.
    Corresponds to variant rs8133886 [ dbSNP | Ensembl ].
    VAR_061115
    Natural varianti1076 – 10761V → I.5 Publications
    Corresponds to variant rs62000962 [ dbSNP | Ensembl ].
    VAR_018055
    Natural varianti1121 – 11211P → R.3 Publications
    Corresponds to variant rs79980197 [ dbSNP | Ensembl ].
    VAR_018056
    Natural varianti1195 – 11951Q → H.
    Corresponds to variant rs2230693 [ dbSNP | Ensembl ].
    VAR_059233
    Natural varianti1675 – 16751D → 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. 3 Publications
    Corresponds to variant rs12483377 [ dbSNP | Ensembl ].
    VAR_012709

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 415415Missing in isoform 3. 2 PublicationsVSP_023130Add
    BLAST
    Alternative sequencei216 – 450235Missing in isoform 2. 1 PublicationVSP_023131Add
    BLAST
    Alternative sequencei416 – 45035QDACW…IGPAA → MAPRCPWPWPRRRRLLDVLA PLVLLLGVRAASAEP in isoform 3. 2 PublicationsVSP_023132Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_085059.2. NM_030582.3.
    NP_569712.2. NM_130445.2.
    UniGeneiHs.517356.

    Genome annotation databases

    EnsembliENST00000355480; ENSP00000347665; ENSG00000182871. [P39060-1]
    ENST00000359759; ENSP00000352798; ENSG00000182871. [P39060-3]
    ENST00000400337; ENSP00000383191; ENSG00000182871. [P39060-2]
    GeneIDi80781.
    KEGGihsa:80781.

    Polymorphism databases

    DMDMi215274264.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_085059.2. NM_030582.3.
    NP_569712.2. NM_130445.2.
    UniGenei Hs.517356.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BNL X-ray 2.90 A/B/C/D 1572-1749 [» ]
    3HON X-ray 3.00 A 1441-1496 [» ]
    3HSH X-ray 1.80 A/B/C/D/E/F 1441-1496 [» ]
    ProteinModelPortali P39060.
    SMRi P39060. Positions 338-444, 1441-1496, 1572-1749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123311. 4 interactions.
    IntActi P39060. 14 interactions.

    Chemistry

    ChEMBLi CHEMBL2364188.

    PTM databases

    PhosphoSitei P39060.
    UniCarbKBi P39060.

    Polymorphism databases

    DMDMi 215274264.

    Proteomic databases

    MaxQBi P39060.
    PaxDbi P39060.
    PRIDEi P39060.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355480 ; ENSP00000347665 ; ENSG00000182871 . [P39060-1 ]
    ENST00000359759 ; ENSP00000352798 ; ENSG00000182871 . [P39060-3 ]
    ENST00000400337 ; ENSP00000383191 ; ENSG00000182871 . [P39060-2 ]
    GeneIDi 80781.
    KEGGi hsa:80781.

    Organism-specific databases

    CTDi 80781.
    GeneCardsi GC21P046825.
    HGNCi HGNC:2195. COL18A1.
    HPAi CAB001961.
    HPA011025.
    MIMi 120328. gene.
    267750. phenotype.
    neXtProti NX_P39060.
    Orphaneti 1571. Knobloch syndrome.
    PharmGKBi PA26711.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG053241.
    InParanoidi P39060.
    KOi K06823.
    OMAi PFWSTAR.
    OrthoDBi EOG7NSB2B.
    PhylomeDBi P39060.
    TreeFami TF315821.

    Enzyme and pathway databases

    Reactomei REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi COL18A1. human.
    EvolutionaryTracei P39060.
    GeneWikii Collagen,_type_XVIII,_alpha_1.
    GenomeRNAii 80781.
    NextBioi 71187.
    PROi P39060.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39060.
    Bgeei P39060.
    Genevestigatori P39060.

    Family and domain databases

    Gene3Di 1.10.2000.10. 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.
    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. "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. Cited for: INVOLVEMENT IN KNO1.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1572-1749, ZINC-BINDING SITE.
    11. "Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure."
      Sertie A.L., Sossi V., Camargo A.A., Zatz M., Brahe C., Passos-Bueno M.R.
      Hum. Mol. Genet. 9:2051-2058(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN KNO1.
    12. "A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma."
      Iughetti P., Suzuki O., Godoi P.H., Alves V.A., Sertie A.L., Zorick T., Soares F., Camargo A.A., Moreira E.S., di Loreto C., Moreira-Filho C.A., Simpson A., Oliva G., Passos-Bueno M.R.
      Cancer Res. 61:7375-7378(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-1076 AND ASN-1675.
    13. "Knobloch syndrome: novel mutations in COL18A1, evidence for genetic heterogeneity, and a functionally impaired polymorphism in endostatin."
      Menzel O., Bekkeheien R.C.J., Reymond A., Fukai N., Boye E., Kosztolanyi G., Aftimos S., Deutsch S., Scott H.S., Olsen B.R., Antonarakis S.E., Guipponi M.
      Hum. Mutat. 23:77-84(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-49; ARG-111; ILE-1076 AND ARG-1121, CHARACTERIZATION OF VARIANT ASN-1675.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1121.

    Entry informationi

    Entry nameiCOIA1_HUMAN
    AccessioniPrimary (citable) accession number: P39060
    Secondary accession number(s): A8MVI4
    , Q58EX6, Q6RZ39, Q6RZ40, Q6RZ41, Q8N4S4, Q8WXI5, Q96T70, Q9UK38, Q9Y6Q7, Q9Y6Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 161 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3