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P39060

- COIA1_HUMAN

UniProt

P39060 - COIA1_HUMAN

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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

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. 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
Complete GO annotation...

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 matrix Source: UniProtKB
  5. extracellular region Source: Reactome
  6. extracellular space Source: BHF-UCL
  7. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiP39060.
ExpressionAtlasiP39060. baseline and differential.
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. 13 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.
GeneTreeiENSGT00710000106713.
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.
IPR013320. ConA-like_dom.
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) [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

        10         20         30         40         50
MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG
60 70 80 90 100
PLPVQPTADT TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP
110 120 130 140 150
DAPEENIAGV GAEILNVAKG IRSFVQLWND TVPTESLARA ETLVLETPVG
160 170 180 190 200
PLALAGPSST PQENGTTLWP SRGIPSSPGA HTTEAGTLPA PTPSPPSLGR
210 220 230 240 250
PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG LSPAAAAPSQ
260 270 280 290 300
QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD
310 320 330 340 350
SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS
360 370 380 390 400
RFWLPNHLHH ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV
410 420 430 440 450
PPPAPPPCCQ FCEALQDACW SRLGGGRLPV ACASLPTQED GYCVLIGPAA
460 470 480 490 500
ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG LAYVFGPDAN SGQVARYHFP
510 520 530 540 550
SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL SGVQDGHQDI
560 570 580 590 600
SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR
610 620 630 640 650
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH
660 670 680 690 700
CLDEEGDDSD GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL
710 720 730 740 750
AGGSSTEDSR SEEVEEQTTV ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE
760 770 780 790 800
GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP PGLPCPVSPL GPAGPALQTV
810 820 830 840 850
PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP GTPGDVGPKG
860 870 880 890 900
DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG
910 920 930 940 950
PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG
960 970 980 990 1000
LPGPPGPPGR EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA
1010 1020 1030 1040 1050
GAPGPAGPPG PPGPPGPPGP GLPAGFDDME GSGGPFWSTA RSADGPQGPP
1060 1070 1080 1090 1100
GLPGLKGDPG VPGLPGAKGE VGADGVPGFP GLPGREGIAG PQGPKGDRGS
1110 1120 1130 1140 1150
RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV PGPEGRPGFA
1160 1170 1180 1190 1200
GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG
1210 1220 1230 1240 1250
EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM
1260 1270 1280 1290 1300
RGMPGPPGPP GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK
1310 1320 1330 1340 1350
GEVGPPGPPG QFPFDFLQLE AEMKGEKGDR GDAGQKGERG EPGGGGFFGS
1360 1370 1380 1390 1400
SLPGPPGPPG PPGPRGYPGI PGPKGESIRG QPGPPGPQGP PGIGYEGRQG
1410 1420 1430 1440 1450
PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG ASSGVRLWAT
1460 1470 1480 1490 1500
RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN
1510 1520 1530 1540 1550
EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP
1560 1570 1580 1590 1600
GAPHHSSYVH LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA
1610 1620 1630 1640 1650
DFQCFQQARA VGLAGTFRAF LSSRLQDLYS IVRRADRAAV PIVNLKDELL
1660 1670 1680 1690 1700
FPSWEALFSG SEGPLKPGAR IFSFDGKDVL RHPTWPQKSV WHGSDPNGRR
1710 1720 1730 1740 1750
LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY IVLCIENSFM

TASK

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. 13 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.
GeneTreei ENSGT00710000106713.
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

Bgeei P39060.
ExpressionAtlasi P39060. baseline and differential.
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.
IPR013320. ConA-like_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 162 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