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P39061

- COIA1_MOUSE

UniProt

P39061 - COIA1_MOUSE

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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

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
Complete GO annotation...

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_199046. Assembly of collagen fibrils and other multimeric structures.
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
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

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

BgeeiP39061.
CleanExiMM_COL18A1.
ExpressionAtlasiP39061. baseline and differential.
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 – 16045Combined sources
Beta strandi1611 – 16144Combined sources
Helixi1615 – 162915Combined sources
Beta strandi1636 – 16394Combined sources
Helixi1647 – 16504Combined sources
Helixi1653 – 16553Combined sources
Turni1656 – 16583Combined sources
Beta strandi1668 – 16714Combined sources
Helixi1673 – 16764Combined sources
Beta strandi1678 – 16803Combined sources
Turni1698 – 17003Combined sources
Beta strandi1704 – 17063Combined sources
Beta strandi1708 – 17103Combined sources
Helixi1725 – 17284Combined sources
Beta strandi1736 – 17416Combined sources
Helixi1742 – 17443Combined sources
Beta strandi1751 – 17544Combined sources
Beta strandi1762 – 17654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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: 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

        10         20         30         40         50
MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE
60 70 80 90 100
GPVSKPQNSS PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ
110 120 130 140 150
KAGQGGSPAT PAVPIPLVAP AASPDMKEEN VAGVGAKILN VAQGIRSFVQ
160 170 180 190 200
LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE LSSAPQGSKT TLWLSSAIPS
210 220 230 240 250
SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPG RAFLSSSTDQ
260 270 280 290 300
GSSWGNQEPP RQPQHLEGKG FLPMTARSSQ QHRHSDVHSD IHGHVPLLPL
310 320 330 340 350
VTGPLVTASL SVHGLLSVPS SDPSGQLSQV AALPGFPGTW VSHVAPSSGT
360 370 380 390 400
GLSNDSALAG NGSLTSTSRC LPLPPTLTLC SRLGIGHFWL PNHLHHTDSV
410 420 430 440 450
EVEATVQAWG RFLHTNCHPF LAWFFCLLLA PSCGPGPPPP LPPCRQFCEA
460 470 480 490 500
LEDECWNYLA GDRLPVVCAS LPSQEDGYCV FIGPAAENVA EEVGLLQLLG
510 520 530 540 550
DPLPEKISQI DDPHVGPAYI FGPDSNSGQV AQYHFPKLFF RDFSLLFHVR
560 570 580 590 600
PATEAAGVLF AITDAAQVVV SLGVKLSEVR DGQQNISLLY TEPGASQTQT
610 620 630 640 650
GASFRLPAFV GQWTHFALSV DGGSVALYVD CEEFQRVPFA RASQGLELER
660 670 680 690 700
GAGLFVGQAG TADPDKFQGM ISELKVRKTP RVSPVHCLDE EDDDEDRASG
710 720 730 740 750
DFGSGFEESS KSHKEDTSLL PGLPQPPPVT SPPLAGGSTT EDPRTEETEE
760 770 780 790 800
DAAVDSIGAE TLPGTGSSGA WDEAIQNPGR GLIKGGMKGQ KGEPGAQGPP
810 820 830 840 850
GPAGPQGPAG PVVQSPNSQP VPGAQGPPGP QGPPGKDGTP GRDGEPGDPG
860 870 880 890 900
EDGRPGDTGP QGFPGTPGDV GPKGEKGDPG IGPRGPPGPP GPPGPSFRQD
910 920 930 940 950
KLTFIDMEGS GFSGDIESLR GPRGFPGPPG PPGVPGLPGE PGRFGINGSY
960 970 980 990 1000
APGPAGLPGV PGKEGPPGFP GPPGPPGPPG KEGPPGVAGQ KGSVGDVGIP
1010 1020 1030 1040 1050
GPKGSKGDLG PIGMPGKSGL AGSPGPVGPP GPPGPPGPPG PGFAAGFDDM
1060 1070 1080 1090 1100
EGSGIPLWTT ARSSDGLQGP PGSPGLKGDP GVAGLPGAKG EVGADGAQGI
1110 1120 1130 1140 1150
PGPPGREGAA GSPGPKGEKG MPGEKGNPGK DGVGRPGLPG PPGPPGPVIY
1160 1170 1180 1190 1200
VSSEDKAIVS TPGPEGKPGY AGFPGPAGPK GDLGSKGEQG LPGPKGEKGE
1210 1220 1230 1240 1250
PGTIFSPDGR ALGHPQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP
1260 1270 1280 1290 1300
GTNGLKGEKG EPGDASLGFS MRGLPGPPGP PGPPGPPGMP IYDSNAFVES
1310 1320 1330 1340 1350
GRPGLPGQQG VQGPSGPKGD KGEVGPPGPP GQFPIDLFHL EAEMKGDKGD
1360 1370 1380 1390 1400
RGDAGQKGER GEPGAPGGGF FSSSVPGPPG PPGYPGIPGP KGESIRGPPG
1410 1420 1430 1440 1450
PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV PGPPGPPGPP
1460 1470 1480 1490 1500
GPPGAMGASA GQVRIWATYQ TMLDKIREVP EGWLIFVAER EELYVRVRNG
1510 1520 1530 1540 1550
FRKVLLEART ALPRGTGNEV AALQPPLVQL HEGSPYTRRE YSYSTARPWR
1560 1570 1580 1590 1600
ADDILANPPR LPDRQPYPGV PHHHSSYVHL PPARPTLSLA HTHQDFQPVL
1610 1620 1630 1640 1650
HLVALNTPLS GGMRGIRGAD FQCFQQARAV GLSGTFRAFL SSRLQDLYSI
1660 1670 1680 1690 1700
VRRADRGSVP IVNLKDEVLS PSWDSLFSGS QGQLQPGARI FSFDGRDVLR
1710 1720 1730 1740 1750
HPAWPQKSVW HGSDPSGRRL MESYCETWRT ETTGATGQAS SLLSGRLLEQ
1760 1770
KAASCHNSYI VLCIENSFMT SFSK

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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_199046. Assembly of collagen fibrils and other multimeric structures.
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

Bgeei P39061.
CleanExi MM_COL18A1.
ExpressionAtlasi P39061. baseline and differential.
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.
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 ]
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Publicationsi

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  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: November 26, 2014
This is version 151 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