O35206 (COFA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XV) chain

Cleaved into the following chain:

1. Endostatin
   Alternative name(s):
   Endostatin-XV

Gene names

Name:

Col15a1

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	1367 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	Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. Ref.5 Ref.6 Endostatin potently inhibits angiogenesis. Ref.5 Ref.6
Subunit structure	Trimer; disulfide-linked By similarity. Ref.7
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Detected in testis, brain, heart, kidney, skeletal muscle and skin (at protein level). Detected in heart and skeletal muscle. Ref.1
Developmental stage	Detected at low levels from day 7 to 11 of embryonic development. Levels are much increased and remain high from day 15 to 17.
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 By similarity. O-glycosylated; contains chondroitin sulfate By similarity.
Sequence similarities	Belongs to the multiplexin collagen family. Contains 4 collagen-like domains. Contains 1 laminin G-like domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from direct assay PubMed 18757743. Source: MGI collagen Inferred from electronic annotation. Source: UniProtKB-KW extracellular space Inferred from electronic annotation. Source: Compara
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Potential

Chain

32 – 1367

1336

Collagen alpha-1(XV) chain

PRO_0000005790

Chain

1191 – 1367

177

Endostatin

PRO_0000005791

Regions

Domain

54 – 249

196

Laminin G-like

Domain

605 – 665

61

Collagen-like 1

Domain

666 – 717

52

Collagen-like 2

Domain

808 – 850

43

Collagen-like 3

Domain

863 – 912

50

Collagen-like 4

Region

229 – 604

376

Nonhelical region 1 (NC1)

Region

605 – 718

114

Triple-helical region 1 (COL1)

Region

719 – 748

30

Nonhelical region 2 (NC2)

Region

749 – 783

35

Triple-helical region 2 (COL2)

Region

784 – 807

24

Nonhelical region 3 (NC3)

Region

808 – 852

45

Triple-helical region 3 (COL3)

Region

853 – 863

11

Nonhelical region 4 (NC4)

Region

864 – 934

71

Triple-helical region 4 (COL4)

Region

935 – 968

34

Nonhelical region 5 (NC5)

Region

969 – 998

30

Triple-helical region 5 (COL5)

Region

999 – 1031

33

Nonhelical region 6 (NC6)

Region

1032 – 1086

55

Triple-helical region 6 (COL6)

Region

1087 – 1096

10

Nonhelical region 7 (NC7)

Region

1097 – 1111

15

Triple-helical region 7 (COL7)

Region

1112 – 1367

256

Nonhelical region 8 (NC8)

Amino acid modifications

Glycosylation

305

1

N-linked (GlcNAc...) Potential

Glycosylation

323

1

N-linked (GlcNAc...) Potential

Glycosylation

348

1

N-linked (GlcNAc...) Potential

Glycosylation

375

1

N-linked (GlcNAc...) Potential

Glycosylation

402

1

N-linked (GlcNAc...) Potential

Glycosylation

673

1

N-linked (GlcNAc...) Potential

Glycosylation

792

1

N-linked (GlcNAc...) Potential

Glycosylation

795

1

N-linked (GlcNAc...) Potential

Glycosylation

799

1

N-linked (GlcNAc...) Potential

Disulfide bond

1216 ↔ 1356

Ref.7

Disulfide bond

1318 ↔ 1348

Ref.7

Experimental info

Sequence conflict

380

1

T → L in AAC53387. Ref.1

Sequence conflict

499

1

T → K in BAE21987. Ref.3

Sequence conflict

569

1

R → K in AAG27545. Ref.2

Sequence conflict

593

1

S → A in AAG27545. Ref.2

Sequence conflict

699

1

T → P in AAC53387. Ref.1

Sequence conflict

699

1

T → P in AAG27545. Ref.2

Sequence conflict

736

1

L → M in AAG27545. Ref.2

Sequence conflict

779

1

P → R in AAC53387. Ref.1

Sequence conflict

1116

1

A → G in AAC53387. Ref.1

Sequence conflict

1116

1

A → G in AAG27545. Ref.2

Sequence conflict

1309

1

H → Y in AAG27545. Ref.2

Secondary structure

1

.

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1367

Helix Strand Turn

Details...

Beta strand

1197 – 1201

5

Helix

1212 – 1222

11

Beta strand

1229 – 1233

5

Helix

1240 – 1242

3

Helix

1246 – 1248

3

Beta strand

1249 – 1251

3

Beta strand

1261 – 1264

4

Helix

1267 – 1270

4

Beta strand

1271 – 1273

3

Turn

1291 – 1293

3

Beta strand

1301 – 1303

3

Helix

1318 – 1321

4

Beta strand

1329 – 1334

6

Helix

1335 – 1337

3

Beta strand

1339 – 1341

3

Beta strand

1344 – 1347

4

Beta strand

1355 – 1358

4

Sequences

	Sequence		Length	Mass (Da)
	O35206 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: BD92E26B5E99B607	FASTA	1,367	140,472
	10 20 30 40 50 60 MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP LPSSVSFTTG 70 80 90 100 110 120 YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN SAQGGVLFAI TDAFQKVIYL 130 140 150 160 170 180 GLRLSSVEDG RQRVILYYTE PGSHVSREAA VFSVPVMTNR WNRFAVTVQG EEVALFMDCE 190 200 210 220 230 240 EQSQVRFQRS SWPLTFEPSA GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES 250 260 270 280 290 300 SASGEASGFQ EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG 310 320 330 340 350 360 TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT DGQGLSATAT 370 380 390 400 410 420 GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP ENLTTTASGD GEVPTSTDGD 430 440 450 460 470 480 TEADSSPTGG PTLKPREEAT LGSHGEEWLT PAVSKMPLKA FEEEEASGTA IDSLDVIFTP 490 500 510 520 530 540 TVVLEQVSRR PTDIQATFTP TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA 550 560 570 580 590 600 STEEAEEEGS GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE 610 620 630 640 650 660 DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG QPGLDGASGQ 670 680 690 700 710 720 QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP GVMGPPGPPG PPGPPGPGCT 730 740 750 760 770 780 TELGFEIEGS GDVRLLSKPT ISGPTSPSGP KGEKGEQGAK GERGADGTST MGPPGPRGPP 790 800 810 820 830 840 GHVEVLSSSL INITNGSMNF SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK 850 860 870 880 890 900 GEQGEKGEPG AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG 910 920 930 940 950 960 LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC KTPVGTAHPG 970 980 990 1000 1010 1020 DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD PAYLRHFLNS LKGENEDASF 1030 1040 1050 1060 1070 1080 RGESSNNLFV SGPPGLPGYP GLVGQKGEAV VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP 1090 1100 1110 1120 1130 1140 GPPGPPAILG AAVALPGPPG PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD 1150 1160 1170 1180 1190 1200 SGEFFIRVRD GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV 1210 1220 1230 1240 1250 1260 ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF GLPIVNLKGQ 1270 1280 1290 1300 1310 1320 VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK VVWHGSNPHG VRLVDKYCEA 1330 1340 1350 1360 WRTTDMAVTG FASPLSTGKI LDQKAYSCAN RLIVLCIENS FMTDTRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of mouse type XV collagen sequences and mapping of the corresponding gene to 4B1-3. Comparison of mouse and human alpha 1 (XV) collagen sequences indicates divergence in the number of small collagenous domains." Haegg P.M., Horelli-Kuitunen N., Eklund L., Palotie A., Pihlajaniemi T. Genomics 45:31-41(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: 129/Sv. Tissue: Kidney.
[2]	"Structure of the mouse type XV collagen gene, Col15a1, comparison with the human COL15A1 gene and functional analysis of the promoters of both genes." Eklund L., Muona A., Lietard J., Pihlajaniemi T. Matrix Biol. 19:489-500(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[3]	"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: Thymus.
[4]	"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.
[5]	"Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity." Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., Timpl R. J. Mol. Biol. 301:1179-1190(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Lack of type XV collagen causes a skeletal myopathy and cardiovascular defects in mice." Eklund L., Piuhola J., Komulainen J., Sormunen R., Ongvarrasopone C., Faessler R., Muona A., Ilves M., Ruskoaho H., Takala T.E.S., Pihlajaniemi T. Proc. Natl. Acad. Sci. U.S.A. 98:1194-1199(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"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 (2.0 ANGSTROMS) OF 1192-1367, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF011450 mRNA. Translation: AAC53387.1.
AF261131 , AF261109, AF261110, AF261111, AF261112, AF261113, AF261114, AF261115, AF261116, AF261117, AF261118, AF261119, AF261120, AF261121, AF261122, AF261123, AF261124, AF261125, AF261126, AF261127, AF261128, AF261129, AF261130 Genomic DNA. Translation: AAG27545.1.
AK134030 mRNA. Translation: BAE21987.1.
AL772232, AL928652 Genomic DNA. Translation: CAM13891.1.
AL928652, AL772232 Genomic DNA. Translation: CAM20188.1.

IPI

IPI00409035.

RefSeq

NP_034058.2. NM_009928.3.

UniGene

Mm.233547.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DY2	X-ray	2.00	A	1192-1367	[»]

ProteinModelPortal

O35206.

SMR

O35206. Positions 1112-1165, 1194-1361.

ModBase

Search...

PTM databases

PhosphoSite

O35206.

Proteomic databases

PaxDb

O35206.

PRIDE

O35206.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000102917; ENSMUSP00000099981; ENSMUSG00000028339.

GeneID

12819.

KEGG

mmu:12819.

UCSC

uc008sum.1. mouse.

Organism-specific databases

CTD

1306.

MGI

MGI:88449. Col15a1.

Phylogenomic databases

eggNOG

NOG12793.

GeneTree

ENSGT00700000104250.

HOGENOM

HOG000231591.

HOVERGEN

HBG080337.

InParanoid

O35206.

KO

K08135.

OMA

GTDVFMG.

OrthoDB

EOG4KSPJP.

Gene expression databases

ArrayExpress

O35206.

Bgee

O35206.

CleanEx

MM_COL15A1.

Genevestigator

O35206.

GermOnline

ENSMUSG00000028339. Mus musculus.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.
3.10.100.10. 1 hit.

InterPro

IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view]

Pfam

PF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view]

SMART

SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 2 hits.
SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50025. LAM_G_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O35206.

NextBio

282290.

SOURCE

Search...

Entry information

Entry name

COFA1_MOUSE

Accession

Primary (citable) accession number: O35206
Secondary accession number(s): A2AJY3, Q3UZ71, Q9EQD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program