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Protein

Collagen alpha-1(XVIII) chain

Gene

COL18A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi1572Zinc1
Metal bindingi1574Zinc1
Metal bindingi1582Zinc1
Metal bindingi1647Zinc1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • structural molecule activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-32313-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
SIGNORiP39060.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:2195. COL18A1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: Ensembl
  • collagen trimer Source: ProtInc
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Knobloch syndrome 1 (KNO1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:267750

Organism-specific databases

DisGeNETi80781.
MalaCardsiCOL18A1.
MIMi267750. phenotype.
OpenTargetsiENSG00000182871.
Orphaneti1571. Knobloch syndrome.
PharmGKBiPA26711.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL18A1.
DMDMi215274264.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000579324 – 1754Collagen alpha-1(XVIII) chainAdd BLAST1731
ChainiPRO_00000057941572 – 1754EndostatinAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi68N-linked (GlcNAc...)Sequence analysis1
Glycosylationi129N-linked (GlcNAc...)Sequence analysis1
Glycosylationi164N-linked (GlcNAc...)Sequence analysis1
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
Modified residuei696PhosphothreonineCombined sources1
Glycosylationi926N-linked (GlcNAc...)Sequence analysis1
GlycosylationiCAR_0001501567O-linked (GalNAc...)1
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, Phosphoprotein

Proteomic databases

EPDiP39060.
PaxDbiP39060.
PeptideAtlasiP39060.
PRIDEiP39060.

PTM databases

iPTMnetiP39060.
PhosphoSitePlusiP39060.
UniCarbKBiP39060.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000182871.
ExpressionAtlasiP39060. baseline and differential.
GenevisibleiP39060. HS.

Organism-specific databases

HPAiCAB001961.
HPA011025.
HPA036104.

Interactioni

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi123311. 23 interactors.
IntActiP39060. 15 interactors.
STRINGi9606.ENSP00000347665.

Structurei

Secondary structure

11754
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1445 – 1450Combined sources6
Helixi1451 – 1457Combined sources7
Helixi1458 – 1460Combined sources3
Beta strandi1466 – 1469Combined sources4
Turni1470 – 1473Combined sources4
Beta strandi1474 – 1479Combined sources6
Beta strandi1482 – 1486Combined sources5
Beta strandi1488 – 1493Combined sources6
Beta strandi1581 – 1585Combined sources5
Helixi1597 – 1610Combined sources14
Beta strandi1617 – 1621Combined sources5
Helixi1629 – 1631Combined sources3
Helixi1634 – 1636Combined sources3
Beta strandi1649 – 1652Combined sources4
Helixi1654 – 1657Combined sources4
Helixi1679 – 1681Combined sources3
Beta strandi1689 – 1691Combined sources3
Helixi1706 – 1709Combined sources4
Beta strandi1716 – 1722Combined sources7
Helixi1723 – 1725Combined sources3
Beta strandi1727 – 1729Combined sources3
Beta strandi1732 – 1735Combined sources4
Beta strandi1743 – 1747Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39060.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini329 – 446FZPROSITE-ProRule annotationAdd BLAST118
Domaini456 – 644Laminin G-likeAdd BLAST189

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni645 – 751Nonhelical region 1 (NC1)Add BLAST107
Regioni752 – 785Triple-helical region 1 (COL1)Add BLAST34
Regioni786 – 795Nonhelical region 2 (NC2)10
Regioni796 – 875Triple-helical region 2 (COL2)Add BLAST80
Regioni876 – 899Nonhelical region 3 (NC3)Add BLAST24
Regioni900 – 1021Triple-helical region 3 (COL3)Add BLAST122
Regioni1022 – 1044Nonhelical region 4 (NC4)Add BLAST23
Regioni1045 – 1127Triple-helical region 4 (COL4)Add BLAST83
Regioni1128 – 1141Nonhelical region 5 (NC5)Add BLAST14
Regioni1142 – 1183Triple-helical region 5 (COL5)Add BLAST42
Regioni1184 – 1196Nonhelical region 6 (NC6)Add BLAST13
Regioni1197 – 1269Triple-helical region 6 (COL6)Add BLAST73
Regioni1270 – 1279Nonhelical region 7 (NC7)10
Regioni1280 – 1312Triple-helical region 7 (COL7)Add BLAST33
Regioni1313 – 1324Nonhelical region 8 (NC8)Add BLAST12
Regioni1325 – 1346Triple-helical region 8 (COL8)Add BLAST22
Regioni1347 – 1353Nonhelical region 9 (NC9)7
Regioni1354 – 1411Triple-helical region 9 (COL9)Add BLAST58
Regioni1412 – 1424Nonhelical region 10 (NC10)Add BLAST13
Regioni1425 – 1442Triple-helical region 10 (COL10)Add BLAST18
Regioni1443 – 1754Nonhelical region 11 (NC11)Add BLAST312

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1330 – 1332Cell attachment siteSequence analysis3

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

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOVERGENiHBG053241.
InParanoidiP39060.
KOiK06823.
OMAiGQWTRFA.
OrthoDBiEOG091G013X.
PhylomeDBiP39060.
TreeFamiTF315821.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di1.10.2000.10. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR016187. CTDL_fold.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 5 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
SMARTiSM00063. FRI. 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. AlignAdd to basket

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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti299R → K in AAR83296 (PubMed:14614989).Curated1
Sequence conflicti663S → F in AAC39658 (PubMed:9503365).Curated1
Sequence conflicti663S → F in AAC39659 (PubMed:9503365).Curated1
Sequence conflicti1112V → L in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1147P → R in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1168R → L in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1210P → L in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1299A → P in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1319L → K in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1355P → A in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1358P → A in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1362 – 1364Missing in AAC39658 (PubMed:9503365).Curated3
Sequence conflicti1362 – 1364Missing in AAC39659 (PubMed:9503365).Curated3
Sequence conflicti1362 – 1364Missing in AAR83296 (PubMed:14614989).Curated3
Sequence conflicti1362 – 1364Missing in AAR83297 (PubMed:14614989).Curated3
Sequence conflicti1362 – 1364Missing in AAR83298 (PubMed:14614989).Curated3
Sequence conflicti1362 – 1364Missing in AAH33715 (PubMed:15489334).Curated3
Sequence conflicti1362 – 1364Missing in AAH63833 (PubMed:15489334).Curated3
Sequence conflicti1362 – 1364Missing in AAA51864 (PubMed:8188291).Curated3
Sequence conflicti1444G → GQ in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1542R → G in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1552A → G in AAA51864 (PubMed:8188291).Curated1
Sequence conflicti1561 – 1562LR → CG in AAA51864 (PubMed:8188291).Curated2
Sequence conflicti1681R → T in AAF01310 (Ref. 7) Curated1
Sequence conflicti1685W → R in AAK50626 (Ref. 8) Curated1
Sequence conflicti1721S → Y in AAF01310 (Ref. 7) Curated1
Sequence conflicti1736C → S in AAK50626 (Ref. 8) Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01805349Q → L.1 PublicationCorresponds to variant rs61735029dbSNPEnsembl.1
Natural variantiVAR_018054111G → R.1 PublicationCorresponds to variant rs114139997dbSNPEnsembl.1
Natural variantiVAR_059232288A → T.Corresponds to variant rs11702494dbSNPEnsembl.1
Natural variantiVAR_061115379T → M.Corresponds to variant rs8133886dbSNPEnsembl.1
Natural variantiVAR_0180551076V → I.5 PublicationsCorresponds to variant rs62000962dbSNPEnsembl.1
Natural variantiVAR_0180561121P → R.3 PublicationsCorresponds to variant rs79980197dbSNPEnsembl.1
Natural variantiVAR_0592331195Q → H.Corresponds to variant rs2230693dbSNPEnsembl.1
Natural variantiVAR_0127091675D → N Functional polymorphism; associated with increased risk for prostate cancer; may cause Knobloch syndrome in compound heterozygotes carrying a frameshift/truncating mutation; results in decreased affinity for laminin. 4 PublicationsCorresponds to variant rs12483377dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0231301 – 415Missing in isoform 3. 2 PublicationsAdd BLAST415
Alternative sequenceiVSP_023131216 – 450Missing in isoform 2. 1 PublicationAdd BLAST235
Alternative sequenceiVSP_023132416 – 450QDACW…IGPAA → MAPRCPWPWPRRRRLLDVLA PLVLLLGVRAASAEP in isoform 3. 2 PublicationsAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_569711.2. NM_130444.2.
NP_569712.2. NM_130445.3.
UniGeneiHs.517356.

Genome annotation databases

EnsembliENST00000355480; ENSP00000347665; ENSG00000182871. [P39060-1]
ENST00000359759; ENSP00000352798; ENSG00000182871. [P39060-3]
ENST00000400337; ENSP00000383191; ENSG00000182871. [P39060-2]
GeneIDi80781.
KEGGihsa:80781.
UCSCiuc062awf.1. human. [P39060-3]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_569711.2. NM_130444.2.
NP_569712.2. NM_130445.3.
UniGeneiHs.517356.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123311. 23 interactors.
IntActiP39060. 15 interactors.
STRINGi9606.ENSP00000347665.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP39060.
PhosphoSitePlusiP39060.
UniCarbKBiP39060.

Polymorphism and mutation databases

BioMutaiCOL18A1.
DMDMi215274264.

Proteomic databases

EPDiP39060.
PaxDbiP39060.
PeptideAtlasiP39060.
PRIDEiP39060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355480; ENSP00000347665; ENSG00000182871. [P39060-1]
ENST00000359759; ENSP00000352798; ENSG00000182871. [P39060-3]
ENST00000400337; ENSP00000383191; ENSG00000182871. [P39060-2]
GeneIDi80781.
KEGGihsa:80781.
UCSCiuc062awf.1. human. [P39060-3]

Organism-specific databases

CTDi80781.
DisGeNETi80781.
GeneCardsiCOL18A1.
HGNCiHGNC:2195. COL18A1.
HPAiCAB001961.
HPA011025.
HPA036104.
MalaCardsiCOL18A1.
MIMi120328. gene.
267750. phenotype.
neXtProtiNX_P39060.
OpenTargetsiENSG00000182871.
Orphaneti1571. Knobloch syndrome.
PharmGKBiPA26711.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOVERGENiHBG053241.
InParanoidiP39060.
KOiK06823.
OMAiGQWTRFA.
OrthoDBiEOG091G013X.
PhylomeDBiP39060.
TreeFamiTF315821.

Enzyme and pathway databases

BioCyciZFISH:G66-32313-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
SIGNORiP39060.

Miscellaneous databases

ChiTaRSiCOL18A1. human.
EvolutionaryTraceiP39060.
GeneWikiiCollagen,_type_XVIII,_alpha_1.
GenomeRNAii80781.
PROiP39060.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182871.
ExpressionAtlasiP39060. baseline and differential.
GenevisibleiP39060. HS.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di1.10.2000.10. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR016187. CTDL_fold.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 5 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
SMARTiSM00063. FRI. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.