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O35206

- COFA1_MOUSE

UniProt

O35206 - COFA1_MOUSE

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Protein
Collagen alpha-1(XV) chain
Gene
Col15a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.2 Publications
Restin potently inhibits angiogenesis.2 Publications

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XV) chain
Cleaved into the following chain:
Alternative name(s):
Endostatin-XV
Gene namesi
Name:Col15a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:88449. Col15a1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. collagen trimer Source: UniProtKB-KW
  3. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 13671336Collagen alpha-1(XV) chain
PRO_0000005790Add
BLAST
Chaini1177 – 1365189Restin
PRO_0000005791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi305 – 3051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi323 – 3231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi348 – 3481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi375 – 3751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi402 – 4021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi673 – 6731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi792 – 7921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi795 – 7951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi799 – 7991N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1216 ↔ 13561 Publication
Disulfide bondi1318 ↔ 13481 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiO35206.
PRIDEiO35206.

PTM databases

PhosphoSiteiO35206.

Expressioni

Tissue specificityi

Detected in testis, brain, heart, kidney, skeletal muscle and skin (at protein level). Detected in heart and skeletal muscle.1 Publication

Developmental stagei

Detected at low levels from day 7 to 11 of embryonic development. Levels are much increased and remain high from day 15 to 17.

Gene expression databases

ArrayExpressiO35206.
BgeeiO35206.
CleanExiMM_COL15A1.
GenevestigatoriO35206.

Interactioni

Subunit structurei

Trimer; disulfide-linked By similarity.1 Publication

Protein-protein interaction databases

IntActiO35206. 1 interaction.
MINTiMINT-4104642.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1197 – 12015
Helixi1212 – 122211
Beta strandi1229 – 12335
Helixi1240 – 12423
Helixi1246 – 12483
Beta strandi1249 – 12513
Beta strandi1261 – 12644
Helixi1267 – 12704
Beta strandi1271 – 12733
Turni1291 – 12933
Beta strandi1301 – 13033
Helixi1318 – 13214
Beta strandi1329 – 13346
Helixi1335 – 13373
Beta strandi1339 – 13413
Beta strandi1344 – 13474
Beta strandi1355 – 13584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY2X-ray2.00A1192-1367[»]
ProteinModelPortaliO35206.
SMRiO35206. Positions 1112-1165, 1194-1361.

Miscellaneous databases

EvolutionaryTraceiO35206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 249196Laminin G-like
Add
BLAST
Domaini605 – 66561Collagen-like 1
Add
BLAST
Domaini666 – 71752Collagen-like 2
Add
BLAST
Domaini808 – 85043Collagen-like 3
Add
BLAST
Domaini863 – 91250Collagen-like 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 604376Nonhelical region 1 (NC1)
Add
BLAST
Regioni605 – 718114Triple-helical region 1 (COL1)
Add
BLAST
Regioni719 – 74830Nonhelical region 2 (NC2)
Add
BLAST
Regioni749 – 78335Triple-helical region 2 (COL2)
Add
BLAST
Regioni784 – 80724Nonhelical region 3 (NC3)
Add
BLAST
Regioni808 – 85245Triple-helical region 3 (COL3)
Add
BLAST
Regioni853 – 86311Nonhelical region 4 (NC4)
Add
BLAST
Regioni864 – 93471Triple-helical region 4 (COL4)
Add
BLAST
Regioni935 – 96834Nonhelical region 5 (NC5)
Add
BLAST
Regioni969 – 99830Triple-helical region 5 (COL5)
Add
BLAST
Regioni999 – 103133Nonhelical region 6 (NC6)
Add
BLAST
Regioni1032 – 108655Triple-helical region 6 (COL6)
Add
BLAST
Regioni1087 – 109610Nonhelical region 7 (NC7)
Regioni1097 – 111115Triple-helical region 7 (COL7)
Add
BLAST
Regioni1112 – 1367256Nonhelical region 8 (NC8)
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiO35206.
KOiK08135.
OMAiPELITFH.
PhylomeDBiO35206.
TreeFamiTF315821.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. 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]
PfamiPF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view]
SMARTiSM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35206-1 [UniParc]FASTAAdd to Basket

« Hide

MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP     50
LPSSVSFTTG YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN 100
SAQGGVLFAI TDAFQKVIYL GLRLSSVEDG RQRVILYYTE PGSHVSREAA 150
VFSVPVMTNR WNRFAVTVQG EEVALFMDCE EQSQVRFQRS SWPLTFEPSA 200
GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES SASGEASGFQ 250
EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG 300
TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT 350
DGQGLSATAT GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP 400
ENLTTTASGD GEVPTSTDGD TEADSSPTGG PTLKPREEAT LGSHGEEWLT 450
PAVSKMPLKA FEEEEASGTA IDSLDVIFTP TVVLEQVSRR PTDIQATFTP 500
TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA STEEAEEEGS 550
GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE 600
DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG 650
QPGLDGASGQ QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP 700
GVMGPPGPPG PPGPPGPGCT TELGFEIEGS GDVRLLSKPT ISGPTSPSGP 750
KGEKGEQGAK GERGADGTST MGPPGPRGPP GHVEVLSSSL INITNGSMNF 800
SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG 850
AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG 900
LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC 950
KTPVGTAHPG DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD 1000
PAYLRHFLNS LKGENEDASF RGESSNNLFV SGPPGLPGYP GLVGQKGEAV 1050
VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP GPPGPPAILG AAVALPGPPG 1100
PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD SGEFFIRVRD 1150
GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV 1200
ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF 1250
GLPIVNLKGQ VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK 1300
VVWHGSNPHG VRLVDKYCEA WRTTDMAVTG FASPLSTGKI LDQKAYSCAN 1350
RLIVLCIENS FMTDTRK 1367
Length:1,367
Mass (Da):140,472
Last modified:April 3, 2007 - v2
Checksum:iBD92E26B5E99B607
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801T → L in AAC53387. 1 Publication
Sequence conflicti499 – 4991T → K in BAE21987. 1 Publication
Sequence conflicti569 – 5691R → K in AAG27545. 1 Publication
Sequence conflicti593 – 5931S → A in AAG27545. 1 Publication
Sequence conflicti699 – 6991T → P in AAC53387. 1 Publication
Sequence conflicti699 – 6991T → P in AAG27545. 1 Publication
Sequence conflicti736 – 7361L → M in AAG27545. 1 Publication
Sequence conflicti779 – 7791P → R in AAC53387. 1 Publication
Sequence conflicti1116 – 11161A → G in AAC53387. 1 Publication
Sequence conflicti1116 – 11161A → G in AAG27545. 1 Publication
Sequence conflicti1309 – 13091H → Y in AAG27545. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS18159.1.
RefSeqiNP_034058.2. NM_009928.3.
UniGeneiMm.233547.

Genome annotation databases

EnsembliENSMUST00000102917; ENSMUSP00000099981; ENSMUSG00000028339.
GeneIDi12819.
KEGGimmu:12819.
UCSCiuc008sum.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS18159.1.
RefSeqi NP_034058.2. NM_009928.3.
UniGenei Mm.233547.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DY2 X-ray 2.00 A 1192-1367 [» ]
ProteinModelPortali O35206.
SMRi O35206. Positions 1112-1165, 1194-1361.
ModBasei Search...

Protein-protein interaction databases

IntActi O35206. 1 interaction.
MINTi MINT-4104642.

PTM databases

PhosphoSitei O35206.

Proteomic databases

PaxDbi O35206.
PRIDEi O35206.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102917 ; ENSMUSP00000099981 ; ENSMUSG00000028339 .
GeneIDi 12819.
KEGGi mmu:12819.
UCSCi uc008sum.1. mouse.

Organism-specific databases

CTDi 1306.
MGIi MGI:88449. Col15a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00710000106713.
HOGENOMi HOG000231591.
HOVERGENi HBG080337.
InParanoidi O35206.
KOi K08135.
OMAi PELITFH.
PhylomeDBi O35206.
TreeFami TF315821.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.

Miscellaneous databases

EvolutionaryTracei O35206.
NextBioi 282290.
PROi O35206.
SOURCEi Search...

Gene expression databases

ArrayExpressi O35206.
Bgeei O35206.
CleanExi MM_COL15A1.
Genevestigatori O35206.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProi 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 ]
Pfami PF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view ]
SMARTi SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiCOFA1_MOUSE
AccessioniPrimary (citable) accession number: O35206
Secondary accession number(s): A2AJY3, Q3UZ71, Q9EQD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

Similar proteinsi