Q00780 (CO8A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(VIII) chain

Cleaved into the following chain:

1. Vastatin

Gene names

Name:

Col8a1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	744 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the maintenance of vessel wall integrity and structure, in particular in atherogenesis. Ref.5 Ref.6 Ref.7 Vastatin, the C-terminal fragment comprising the NC1 domain, inhibits aortic endothelial cell proliferation and causes cell apoptosis By similarity. Ref.5 Ref.6 Ref.7
Subunit structure	Homotrimers, or heterotrimers in association with alpha 2(VIII) type collagens. Four homotrimers can form a tetrhedron stabilized by central interacting C-terminal NC1 trimers By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
Tissue specificity	High levels in calvarium, eye and skin of newborn mice; also in various epithelial, endothelial and mesenchymal cells. Ref.5 Ref.7
Induction	Up-regulated in astrocytes during the repair process and in mesangial cells in diabetic animals. Ref.5 Ref.7
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Proteolytically cleaved by neutrophil elastase, in vitro. Proteolytic processing produces the C-terminal NC1 domain fragment, vastatin By similarity.
Disruption phenotype	COL8A1-/COL8A2- mice exhibit decreased proliferation of measngial cells, reduced phosphorylation of ERK1/2 and increased p27(KIP1) expression. Diabetic COL8A1-/COL8A2- mice reveal reduced mesangial expansion and cellularity and extracellular matrix expansion. Ref.7
Sequence similarities	Contains 1 C1q domain.

Ontologies

Keywords
Biological process	Angiogenesis Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Collagen Repeat Signal
PTM	Hydroxylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW camera-type eye morphogenesis Inferred from genetic interaction PubMed 16051690. Source: MGI cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW epithelial cell proliferation Inferred from genetic interaction PubMed 16051690. Source: MGI positive regulation of cell-substrate adhesion Inferred from direct assay PubMed 18757743. Source: MGI
Cellular_component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell collagen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 744

720

Collagen alpha-1(VIII) chain

PRO_0000005763

Chain

573 – 744

172

Vastatin

PRO_0000390485

Regions

Domain

611 – 744

134

C1q

Region

29 – 118

90

Nonhelical region (NC2)

Region

119 – 572

454

Triple-helical region (COL1)

Region

573 – 744

172

Nonhelical region (NC1)

Experimental info

Sequence conflict

3

1

V → L in AAH11061. Ref.4

Sequence conflict

6

1

R → G in CAA47387. Ref.1

Sequence conflict

85

1

H → Y in CAA47387. Ref.1

Sequence conflict

110

1

Missing in CAA47387. Ref.1

Sequence conflict

249

1

P → L in CAA47387. Ref.1

Sequence conflict

314

1

P → A in BAB31383. Ref.2

Sequence conflict

324 – 325

2

IP → SR in CAA47387. Ref.1

Sequence conflict

362

1

D → H in CAA47387. Ref.1

Sequence conflict

597

1

P → T in CAA47387. Ref.1

Sequence conflict

635

1

F → L in BAE35169. Ref.2

Sequence conflict

718 – 720

3

MPS → NPF in CAA47387. Ref.1

Secondary structure

1

.

.

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.

.

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.

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744

Helix Strand Turn

Details...

Beta strand

617 – 622

6

Beta strand

637 – 642

6

Turn

648 – 650

3

Beta strand

659 – 680

22

Beta strand

683 – 690

8

Beta strand

698 – 708

11

Beta strand

713 – 717

5

Helix

721 – 723

3

Beta strand

724 – 727

4

Beta strand

734 – 743

10

Sequences

	Sequence		Length	Mass (Da)
	Q00780 [UniParc]. Last modified February 6, 2007. Version 3. Checksum: 88F31CD20BDC8372	FASTA	744	73,607
	10 20 30 40 50 60 MAVPPRPLQL LGILFIISLN SVRLIQAGAY YGIKPLPPQI PPQIPPQIPQ YQPLGQQVPH 70 80 90 100 110 120 MPLGKDGLSM GKEMPHMQYG KEYPHLPQYM KEIPPVPRMG KEVVPKKGKG EVPLASLRGE 130 140 150 160 170 180 QGPRGEPGPR GPPGPPGLPG HGMPGIKGKP GPQGYPGIGK PGMPGMPGKP GAMGMPGAKG 190 200 210 220 230 240 EIGPKGEIGP MGIPGPQGPP GPHGLPGIGK PGGPGLPGQP GAKGERGPKG PPGPPGLQGP 250 260 270 280 290 300 KGEKGFGMPG LPGLKGPPGM HGPPGPVGLP GVGKPGVTGF PGPQGPLGKP GPPGEPGPQG 310 320 330 340 350 360 LIGVPGVQGP PGMPGVGKPG QDGIPGQPGF PGGKGEQGLP GLPGPPGLPG VGKPGFPGPK 370 380 390 400 410 420 GDRGIGGVPG VLGPRGEKGP IGAPGMGGPP GEPGLPGIPG PMGPPGAIGF PGPKGEGGVV 430 440 450 460 470 480 GPQGPPGPKG EPGLQGFPGK PGFLGEVGPP GMRGLPGPIG PKGEGGHKGL PGLPGVPGLL 490 500 510 520 530 540 GPKGEPGIPG DQGLQGPPGI PGIVGPSGPI GPPGIPGPKG EPGLPGPPGF PGVGKPGVAG 550 560 570 580 590 600 LHGPPGKPGA LGPQGQPGLP GPPGPPGPPG PPAVMPTPSP QGEYLPDMGL GIDGVKPPHA 610 620 630 640 650 660 YAGKKGKHGG PAYEMPAFTA ELTVPFPPVG APVKFDKLLY NGRQNYNPQT GIFTCEVPGV 670 680 690 700 710 720 YYFAYHVHCK GGNVWVALFK NNEPMMYTYD EYKKGFLDQA SGSAVLLLRP GDQVFLQMPS 730 740 EQAAGLYAGQ YVHSSFSGYL LYPM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alpha 1(VIII)-collagen gene transcripts encode a short-chain collagen polypeptide and are expressed by various epithelial, endothelial and mesenchymal cells in newborn mouse tissues." Muragaki Y., Shiota C., Inoue M., Ooshima A., Olsen B.R., Ninomiya Y. Eur. J. Biochem. 207:895-902(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c.
[2]	"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]. Strain: C57BL/6J. Tissue: Corpora quadrigemina, Kidney and Medulla oblongata.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]. Strain: FVB/N. Tissue: Mammary gland.
[5]	"Astrocytes express type VIII collagen during the repair process of brain cold injury." Hirano S., Yonezawa T., Hasegawa H., Hattori S., Greenhill N.S., Davis P.F., Sage E.H., Ninomiya Y. Biochem. Biophys. Res. Commun. 317:437-443(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, FUNCTION, INDUCTION.
[6]	"Migration and growth are attenuated in vascular smooth muscle cells with type VIII collagen-null alleles." Adiguzel E., Hou G., Mulholland D., Hopfer U., Fukai N., Olsen B., Bendeck M. Arterioscler. Thromb. Vasc. Biol. 26:56-61(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Lack of type VIII collagen in mice ameliorates diabetic nephropathy." Hopfer U., Hopfer H., Meyer-Schwesinger C., Loeffler I., Fukai N., Olsen B.R., Stahl R.A., Wolf G. Diabetes 58:1672-1681(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION.
[8]	"Crystal structure of the collagen alpha1(VIII) NC1 trimer." Kvansakul M., Bogin O., Hohenester E., Yayon A. Matrix Biol. 22:145-152(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 573-744.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66976, X66977 Genomic DNA. Translation: CAA47387.1.
AK018742 mRNA. Translation: BAB31383.1.
AK032048 mRNA. Translation: BAC27670.1.
AK046370 mRNA. Translation: BAC32693.1.
AK159542 mRNA. Translation: BAE35169.1.
CT025753 Genomic DNA. Translation: CAX16095.1.
BC011061 mRNA. Translation: AAH11061.1.

IPI

IPI00399464.

PIR

S23779.

RefSeq

NP_031765.2. NM_007739.2.

UniGene

Mm.130388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O91	X-ray	1.90	A/B/C	573-744	[»]

ProteinModelPortal

Q00780.

SMR

Q00780. Positions 614-744.

ModBase

Search...

PTM databases

PhosphoSite

Q00780.

Proteomic databases

PaxDb

Q00780.

PRIDE

Q00780.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000089332; ENSMUSP00000086745; ENSMUSG00000068196.

GeneID

12837.

KEGG

mmu:12837.

UCSC

uc007znl.1. mouse.

Organism-specific databases

CTD

1295.

MGI

MGI:88463. Col8a1.

Phylogenomic databases

eggNOG

NOG114228.

GeneTree

ENSGT00700000104270.

HOGENOM

HOG000085653.

HOVERGEN

HBG108220.

InParanoid

Q00780.

OMA

TCEVPGV.

OrthoDB

EOG4DJJXP.

Gene expression databases

Bgee

Q00780.

CleanEx

MM_COL8A1.

Genevestigator

Q00780.

GermOnline

ENSMUSG00000068196. Mus musculus.

Family and domain databases

Gene3D

2.60.120.40. 1 hit.

InterPro

IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00386. C1q. 1 hit.
PF01391. Collagen. 3 hits.
[Graphical view]

PRINTS

PR00007. COMPLEMNTC1Q.

SMART

SM00110. C1Q. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS50871. C1Q. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q00780.

NextBio

282360.

SOURCE

Search...

Entry information

Entry name

CO8A1_MOUSE

Accession

Primary (citable) accession number: Q00780
Secondary accession number(s): B8JJL9 , Q3TWU7, Q8BGL6, Q921S8, Q9D2V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program