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Protein

Collagen alpha-1(XVIII) chain

Gene

Col18a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.By similarity
Non-collagenous domain 1: May regulate extracellular matrix-dependent motility and morphogenesis of endothelial and non-endothelial cells; the function requires homotrimerization and implicates MAPK signaling.By similarity
Endostatin: Potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (PubMed:9008168). Inhibits VEGFA isoform VEGF165-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2 (PubMed:12029087). Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (PubMed:11158588). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1591Zinc; alternate1
Metal bindingi1593Zinc1
Metal bindingi1595Zinc; alternate1
Metal bindingi1601Zinc1
Metal bindingi1666Zinc1

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • cell adhesion Source: UniProtKB-KW
  • endothelial cell morphogenesis Source: MGI
  • extracellular matrix organization Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of endothelial cell apoptotic process Source: MGI
  • response to drug Source: Ensembl
  • response to hydrostatic pressure Source: Ensembl

Keywordsi

Biological processCell adhesion
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1592389. Activation of Matrix Metalloproteinases.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000157. Laminin interactions.
R-MMU-8948216. Collagen chain trimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XVIII) chain
Cleaved into the following 2 chains:
Gene namesi
Name:Col18a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88451. Col18a1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1591H → A: No effect on zinc binding. 1 Publication1
Mutagenesisi1593H → A: Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595. 1 Publication1
Mutagenesisi1595D → A: No effect on zinc binding. Abolishes zinc binding; when associated with A-1593. 1 Publication1
Mutagenesisi1666D → A: Abolishes zinc binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000441862? – 1774Non-collagenous domain 1Curated
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000000579527 – 1774Collagen alpha-1(XVIII) chainAdd BLAST1748
ChainiPRO_00000057961591 – 1774EndostatinAdd BLAST184

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi354N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi361N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi585N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei730PhosphothreonineBy similarity1
Glycosylationi947N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1623 ↔ 1763PROSITE-ProRule annotation1 Publication
Disulfide bondi1725 ↔ 1755PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.
Undergoes proteolytic processing by cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers. In tissue extracts (brain, skeletal muscle, heart, kidney, testis and liver) predominantly bands of approximately 38 kDa are detected; recombinant non-collagenous domain 1 shows similar mobility. In vitro, several proteolytic cleavage sites in the non-collagenous domain 1 hinge region generating different endostatin-like peptides are reported.By similarity1 Publication2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiP39061.
PeptideAtlasiP39061.
PRIDEiP39061.

PTM databases

iPTMnetiP39061.
PhosphoSitePlusiP39061.

Miscellaneous databases

PMAP-CutDBiP39061.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000001435.
CleanExiMM_COL18A1.
ExpressionAtlasiP39061. baseline and differential.
GenevisibleiP39061. MM.

Interactioni

Subunit structurei

Non-collagenous domain 1 forms homotrimers. Endostatin is monomeric (PubMed:9687493). Recombinant non-collagenous domain 1 has stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex and lower affinity to FBLN1 and FBLN2 than endostatin (PubMed:10966814). Endostatin interacts with KDR/VEGFR2 (PubMed:12029087). Endostatin interacts with the ITGA5:ITGB1 complex (PubMed:11158588).4 Publications

Protein-protein interaction databases

BioGridi198812. 1 interactor.
STRINGi10090.ENSMUSP00000101049.

Structurei

Secondary structure

11774
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1600 – 1604Combined sources5
Beta strandi1611 – 1614Combined sources4
Helixi1615 – 1629Combined sources15
Beta strandi1636 – 1639Combined sources4
Helixi1647 – 1650Combined sources4
Helixi1653 – 1655Combined sources3
Turni1656 – 1658Combined sources3
Beta strandi1668 – 1671Combined sources4
Helixi1673 – 1676Combined sources4
Beta strandi1678 – 1680Combined sources3
Turni1698 – 1700Combined sources3
Beta strandi1704 – 1706Combined sources3
Beta strandi1708 – 1710Combined sources3
Helixi1725 – 1728Combined sources4
Beta strandi1736 – 1741Combined sources6
Helixi1742 – 1744Combined sources3
Beta strandi1751 – 1754Combined sources4
Beta strandi1762 – 1765Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DY0X-ray2.20A1587-1774[»]
1DY1X-ray2.20A1587-1774[»]
1KOEX-ray1.50A1597-1768[»]
ProteinModelPortaliP39061.
SMRiP39061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini365 – 482FZPROSITE-ProRule annotationAdd BLAST118
Domaini522 – 704Laminin G-likeAdd BLAST183
Domaini823 – 878Collagen-like 1Add BLAST56
Domaini953 – 1007Collagen-like 2Add BLAST55
Domaini1008 – 1041Collagen-like 3Add BLAST34
Domaini1066 – 1117Collagen-like 4Add BLAST52
Domaini1118 – 1147Collagen-like 5Add BLAST30
Domaini1162 – 1202Collagen-like 6Add BLAST41
Domaini1216 – 1264Collagen-like 7Add BLAST49

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 785Nonhelical region 1 (NC1)Add BLAST759
Regioni786 – 812Triple-helical region 1 (COL1)Add BLAST27
Regioni813 – 822Nonhelical region 2 (NC2)10
Regioni823 – 896Triple-helical region 2 (COL2)Add BLAST74
Regioni897 – 920Nonhelical region 3 (NC3)Add BLAST24
Regioni921 – 1042Triple-helical region 3 (COL3)Add BLAST122
Regioni1043 – 1065Nonhelical region 4 (NC4)Add BLAST23
Regioni1066 – 1148Triple-helical region 4 (COL4)Add BLAST83
Regioni1149 – 1162Nonhelical region 5 (NC5)Add BLAST14
Regioni1163 – 1204Triple-helical region 5 (COL5)Add BLAST42
Regioni1205 – 1217Nonhelical region 6 (NC6)Add BLAST13
Regioni1218 – 1290Triple-helical region 6 (COL6)Add BLAST73
Regioni1291 – 1300Nonhelical region 7 (NC7)10
Regioni1301 – 1333Triple-helical region 7 (COL7)Add BLAST33
Regioni1334 – 1345Nonhelical region 8 (NC8)Add BLAST12
Regioni1346 – 1369Triple-helical region 8 (COL8)Add BLAST24
Regioni1370 – 1376Nonhelical region 9 (NC9)7
Regioni1377 – 1428Triple-helical region 9 (COL9)Add BLAST52
Regioni1429 – 1441Nonhelical region 10 (NC10)Add BLAST13
Regioni1442 – 1459Triple-helical region 10 (COL10)Add BLAST18
Regioni1460 – 1774Nonhelical region 11 (NC11)Add BLAST315
Regioni1474 – 1519Non-collagenous domain 1 association domain1 PublicationAdd BLAST46
Regioni1520 – 1590Non-collagenous domain 1 hinge region1 PublicationAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1351 – 1353Cell attachment siteSequence analysis3

Sequence similaritiesi

Belongs to the multiplexin collagen family.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOVERGENiHBG053241.
InParanoidiP39061.
KOiK06823.
PhylomeDBiP39061.
TreeFamiTF315821.

Family and domain databases

CDDicd07455. CRD_Collagen_XVIII. 1 hit.
cd00247. Endostatin-like. 1 hit.
Gene3Di1.10.2000.10. 1 hit.
2.160.20.50. 1 hit.
3.10.100.10. 1 hit.
InterProiView protein in InterPro
IPR016186. C-type_lectin-like/link_sf.
IPR008160. Collagen.
IPR035523. Collagen_XVIII_Fz.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom_sf.
IPR016187. CTDL_fold.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR036790. Frizzled_dom_sf.
IPR016133. Insect_cyst_antifreeze_prot.
IPR001791. Laminin_G.
PfamiView protein in Pfam
PF01391. Collagen. 5 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
SMARTiView protein in SMART
SM00063. FRI. 1 hit.
SM00210. TSPN. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEiView protein in PROSITE
PS50038. FZ. 1 hit.

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: 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)DescriptionActionsGraphical viewLength
Sequence conflicti1046G → V in AAH66080 (PubMed:15489334).Curated1
Sequence conflicti1147P → L in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1194P → F in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1211A → R in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1347D → V in BAC27554 (PubMed:16141072).Curated1
Sequence conflicti1404P → R in AAA20657 (PubMed:8188673).Curated1
Sequence conflicti1404P → R in AAC52901 (PubMed:8838808).Curated1
Sequence conflicti1404P → R in AAC52902 (PubMed:8838808).Curated1
Sequence conflicti1404P → R in AAC52903 (PubMed:8838808).Curated1
Sequence conflicti1404P → R in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1513P → L in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1523L → F in AAA19787 (PubMed:8183893).Curated1
Sequence conflicti1684L → V in AAA19787 (PubMed:8183893).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0011571 – 459Missing in isoform 3. 5 PublicationsAdd BLAST459
Alternative sequenceiVSP_008303240 – 486Missing in isoform 2. CuratedAdd BLAST247
Alternative sequenceiVSP_001158460 – 486AGDRL…IGPAA → MAPRWHLLDVLTSLVLLLVA RVSWAEP in isoform 3. 5 PublicationsAdd BLAST27

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

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 1, 2007
Last modified: November 22, 2017
This is version 177 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Non-collagenous domain 1 seems to be the predominant tissue form from which endostatin is cleaved. However, the proteolytic cleavage site to generate non-collagenous domain 1 is not known. Soluble recombinant non-collagenous domain 1 amenable to biochemical studies has been used instead; its molecular wight corresponds to probable non-collagenous domain 1 immunoblot bands seen in tissue extracts.Curated

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