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O35206 (COFA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XV) chain

Cleaved into the following chain:

  1. Restin
    Alternative name(s):
    Endostatin-XV
Gene names
Name:Col15a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Restin potently inhibits angiogenesis. Ref.5 Ref.6

Subunit structure

Trimer; disulfide-linked By similarity. Ref.7

Subcellular location

Secretedextracellular spaceextracellular 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.

Caution

The name Restin has also been used for CAP-Gly domain-containing linker protein 1 the product of the CLIP1 gene.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 13671336Collagen alpha-1(XV) chain
PRO_0000005790
Chain1177 – 1365189Restin
PRO_0000005791

Regions

Domain54 – 249196Laminin G-like
Domain605 – 66561Collagen-like 1
Domain666 – 71752Collagen-like 2
Domain808 – 85043Collagen-like 3
Domain863 – 91250Collagen-like 4
Region229 – 604376Nonhelical region 1 (NC1)
Region605 – 718114Triple-helical region 1 (COL1)
Region719 – 74830Nonhelical region 2 (NC2)
Region749 – 78335Triple-helical region 2 (COL2)
Region784 – 80724Nonhelical region 3 (NC3)
Region808 – 85245Triple-helical region 3 (COL3)
Region853 – 86311Nonhelical region 4 (NC4)
Region864 – 93471Triple-helical region 4 (COL4)
Region935 – 96834Nonhelical region 5 (NC5)
Region969 – 99830Triple-helical region 5 (COL5)
Region999 – 103133Nonhelical region 6 (NC6)
Region1032 – 108655Triple-helical region 6 (COL6)
Region1087 – 109610Nonhelical region 7 (NC7)
Region1097 – 111115Triple-helical region 7 (COL7)
Region1112 – 1367256Nonhelical region 8 (NC8)

Amino acid modifications

Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation6731N-linked (GlcNAc...) Potential
Glycosylation7921N-linked (GlcNAc...) Potential
Glycosylation7951N-linked (GlcNAc...) Potential
Glycosylation7991N-linked (GlcNAc...) Potential
Disulfide bond1216 ↔ 1356 Ref.7
Disulfide bond1318 ↔ 1348 Ref.7

Experimental info

Sequence conflict3801T → L in AAC53387. Ref.1
Sequence conflict4991T → K in BAE21987. Ref.3
Sequence conflict5691R → K in AAG27545. Ref.2
Sequence conflict5931S → A in AAG27545. Ref.2
Sequence conflict6991T → P in AAC53387. Ref.1
Sequence conflict6991T → P in AAG27545. Ref.2
Sequence conflict7361L → M in AAG27545. Ref.2
Sequence conflict7791P → R in AAC53387. Ref.1
Sequence conflict11161A → G in AAC53387. Ref.1
Sequence conflict11161A → G in AAG27545. Ref.2
Sequence conflict13091H → Y in AAG27545. Ref.2

Secondary structure

................................ 1367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35206 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: BD92E26B5E99B607

FASTA1,367140,472
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
RefSeqNP_034058.2. NM_009928.3.
UniGeneMm.233547.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY2X-ray2.00A1192-1367[»]
ProteinModelPortalO35206.
SMRO35206. Positions 1112-1165, 1194-1361.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35206. 1 interaction.
MINTMINT-4104642.

PTM databases

PhosphoSiteO35206.

Proteomic databases

PaxDbO35206.
PRIDEO35206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102917; ENSMUSP00000099981; ENSMUSG00000028339.
GeneID12819.
KEGGmmu:12819.
UCSCuc008sum.1. mouse.

Organism-specific databases

CTD1306.
MGIMGI:88449. Col15a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00710000106713.
HOGENOMHOG000231591.
HOVERGENHBG080337.
InParanoidO35206.
KOK08135.
OMAPELITFH.
PhylomeDBO35206.
TreeFamTF315821.

Gene expression databases

ArrayExpressO35206.
BgeeO35206.
CleanExMM_COL15A1.
GenevestigatorO35206.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProIPR016186. 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]
PfamPF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view]
SMARTSM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceO35206.
NextBio282290.
PROO35206.
SOURCESearch...

Entry information

Entry nameCOFA1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot