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Protein

Collagen alpha-1(XV) chain

Gene

Col15a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.
Restin potently inhibits angiogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88449. Col15a1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: MGI
  • collagen trimer Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000000579032 – 1367Collagen alpha-1(XV) chainAdd BLAST1336
ChainiPRO_00000057911177 – 1365RestinAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi305N-linked (GlcNAc...)Sequence analysis1
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi348N-linked (GlcNAc...)Sequence analysis1
Glycosylationi375N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi673N-linked (GlcNAc...)Sequence analysis1
Glycosylationi792N-linked (GlcNAc...)Sequence analysis1
Glycosylationi795N-linked (GlcNAc...)Sequence analysis1
Glycosylationi799N-linked (GlcNAc...)Sequence analysis1
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

MaxQBiO35206.
PaxDbiO35206.
PRIDEiO35206.

PTM databases

PhosphoSitePlusiO35206.

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

BgeeiENSMUSG00000028339.
CleanExiMM_COL15A1.
ExpressionAtlasiO35206. baseline and differential.
GenevisibleiO35206. MM.

Interactioni

Subunit structurei

Trimer; disulfide-linked.By similarity

Protein-protein interaction databases

IntActiO35206. 1 interactor.
MINTiMINT-4104642.
STRINGi10090.ENSMUSP00000099981.

Structurei

Secondary structure

11367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1197 – 1201Combined sources5
Helixi1212 – 1222Combined sources11
Beta strandi1229 – 1233Combined sources5
Helixi1240 – 1242Combined sources3
Helixi1246 – 1248Combined sources3
Beta strandi1249 – 1251Combined sources3
Beta strandi1261 – 1264Combined sources4
Helixi1267 – 1270Combined sources4
Beta strandi1271 – 1273Combined sources3
Turni1291 – 1293Combined sources3
Beta strandi1301 – 1303Combined sources3
Helixi1318 – 1321Combined sources4
Beta strandi1329 – 1334Combined sources6
Helixi1335 – 1337Combined sources3
Beta strandi1339 – 1341Combined sources3
Beta strandi1344 – 1347Combined sources4
Beta strandi1355 – 1358Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DY2X-ray2.00A1192-1367[»]
ProteinModelPortaliO35206.
SMRiO35206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 249Laminin G-likeAdd BLAST196
Domaini605 – 665Collagen-like 1Add BLAST61
Domaini666 – 717Collagen-like 2Add BLAST52
Domaini808 – 850Collagen-like 3Add BLAST43
Domaini863 – 912Collagen-like 4Add BLAST50

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 604Nonhelical region 1 (NC1)Add BLAST376
Regioni605 – 718Triple-helical region 1 (COL1)Add BLAST114
Regioni719 – 748Nonhelical region 2 (NC2)Add BLAST30
Regioni749 – 783Triple-helical region 2 (COL2)Add BLAST35
Regioni784 – 807Nonhelical region 3 (NC3)Add BLAST24
Regioni808 – 852Triple-helical region 3 (COL3)Add BLAST45
Regioni853 – 863Nonhelical region 4 (NC4)Add BLAST11
Regioni864 – 934Triple-helical region 4 (COL4)Add BLAST71
Regioni935 – 968Nonhelical region 5 (NC5)Add BLAST34
Regioni969 – 998Triple-helical region 5 (COL5)Add BLAST30
Regioni999 – 1031Nonhelical region 6 (NC6)Add BLAST33
Regioni1032 – 1086Triple-helical region 6 (COL6)Add BLAST55
Regioni1087 – 1096Nonhelical region 7 (NC7)10
Regioni1097 – 1111Triple-helical region 7 (COL7)Add BLAST15
Regioni1112 – 1367Nonhelical region 8 (NC8)Add BLAST256

Sequence similaritiesi

Belongs to the multiplexin collagen family.Curated
Contains 4 collagen-like domains.Curated
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiO35206.
KOiK08135.
OMAiGVEDGHQ.
OrthoDBiEOG091G01N2.
PhylomeDBiO35206.
TreeFamiTF315821.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR016187. CTDL_fold.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF06482. Endostatin. 1 hit.
[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

        10         20         30         40         50
MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP
60 70 80 90 100
LPSSVSFTTG YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN
110 120 130 140 150
SAQGGVLFAI TDAFQKVIYL GLRLSSVEDG RQRVILYYTE PGSHVSREAA
160 170 180 190 200
VFSVPVMTNR WNRFAVTVQG EEVALFMDCE EQSQVRFQRS SWPLTFEPSA
210 220 230 240 250
GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES SASGEASGFQ
260 270 280 290 300
EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG
310 320 330 340 350
TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT
360 370 380 390 400
DGQGLSATAT GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP
410 420 430 440 450
ENLTTTASGD GEVPTSTDGD TEADSSPTGG PTLKPREEAT LGSHGEEWLT
460 470 480 490 500
PAVSKMPLKA FEEEEASGTA IDSLDVIFTP TVVLEQVSRR PTDIQATFTP
510 520 530 540 550
TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA STEEAEEEGS
560 570 580 590 600
GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE
610 620 630 640 650
DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG
660 670 680 690 700
QPGLDGASGQ QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP
710 720 730 740 750
GVMGPPGPPG PPGPPGPGCT TELGFEIEGS GDVRLLSKPT ISGPTSPSGP
760 770 780 790 800
KGEKGEQGAK GERGADGTST MGPPGPRGPP GHVEVLSSSL INITNGSMNF
810 820 830 840 850
SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG
860 870 880 890 900
AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG
910 920 930 940 950
LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC
960 970 980 990 1000
KTPVGTAHPG DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD
1010 1020 1030 1040 1050
PAYLRHFLNS LKGENEDASF RGESSNNLFV SGPPGLPGYP GLVGQKGEAV
1060 1070 1080 1090 1100
VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP GPPGPPAILG AAVALPGPPG
1110 1120 1130 1140 1150
PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD SGEFFIRVRD
1160 1170 1180 1190 1200
GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV
1210 1220 1230 1240 1250
ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF
1260 1270 1280 1290 1300
GLPIVNLKGQ VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK
1310 1320 1330 1340 1350
VVWHGSNPHG VRLVDKYCEA WRTTDMAVTG FASPLSTGKI LDQKAYSCAN
1360
RLIVLCIENS FMTDTRK
Length:1,367
Mass (Da):140,472
Last modified:April 3, 2007 - v2
Checksum:iBD92E26B5E99B607
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti380T → L in AAC53387 (PubMed:9339358).Curated1
Sequence conflicti499T → K in BAE21987 (PubMed:16141072).Curated1
Sequence conflicti569R → K in AAG27545 (PubMed:11068203).Curated1
Sequence conflicti593S → A in AAG27545 (PubMed:11068203).Curated1
Sequence conflicti699T → P in AAC53387 (PubMed:9339358).Curated1
Sequence conflicti699T → P in AAG27545 (PubMed:11068203).Curated1
Sequence conflicti736L → M in AAG27545 (PubMed:11068203).Curated1
Sequence conflicti779P → R in AAC53387 (PubMed:9339358).Curated1
Sequence conflicti1116A → G in AAC53387 (PubMed:9339358).Curated1
Sequence conflicti1116A → G in AAG27545 (PubMed:11068203).Curated1
Sequence conflicti1309H → Y in AAG27545 (PubMed:11068203).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DY2X-ray2.00A1192-1367[»]
ProteinModelPortaliO35206.
SMRiO35206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35206. 1 interactor.
MINTiMINT-4104642.
STRINGi10090.ENSMUSP00000099981.

PTM databases

PhosphoSitePlusiO35206.

Proteomic databases

MaxQBiO35206.
PaxDbiO35206.
PRIDEiO35206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1306.
MGIiMGI:88449. Col15a1.

Phylogenomic databases

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiO35206.
KOiK08135.
OMAiGVEDGHQ.
OrthoDBiEOG091G01N2.
PhylomeDBiO35206.
TreeFamiTF315821.

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSiCol15a1. mouse.
EvolutionaryTraceiO35206.
PROiO35206.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028339.
CleanExiMM_COL15A1.
ExpressionAtlasiO35206. baseline and differential.
GenevisibleiO35206. MM.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR016187. CTDL_fold.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF06482. Endostatin. 1 hit.
[Graphical view]
SMARTiSM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNetiSearch...

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: November 30, 2016
This is version 126 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.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.