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Protein

Collagen alpha-1(XV) chain

Gene

COL15A1

Organism
Homo sapiens (Human)
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.1 Publication
Restin potently inhibits angiogenesis.By similarity

GO - Molecular functioni

  • extracellular matrix structural constituent Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • collagen catabolic process Source: Reactome
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Cell adhesion, Differentiation

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XV) chain
Cleaved into the following 4 chains:
Alternative name(s):
Endostatin-XV
Related to endostatin
Restin-I
Alternative name(s):
Restin-II
Alternative name(s):
Restin-III
Alternative name(s):
Restin-IV
Gene namesi
Name:COL15A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2192. COL15A1.

Subcellular locationi

GO - Cellular componenti

  • collagen type XV trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi1306.
OpenTargetsiENSG00000204291.
PharmGKBiPA26708.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

DMDMi68839886.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000000578828 – 1388Collagen alpha-1(XV) chainAdd BLAST1361
ChainiPRO_00000057891198 – 1386RestinAdd BLAST189
ChainiPRO_00004230141207 – 1386Restin-2Add BLAST180
ChainiPRO_00004230151213 – 1386Restin-3Add BLAST174
ChainiPRO_00004230161221 – 1386Restin-4Add BLAST166

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi265O-linked (GalNAc...)1 Publication1
Glycosylationi306N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi687N-linked (GlcNAc...)Sequence analysis1
Glycosylationi807N-linked (GlcNAc...)Sequence analysis1
Glycosylationi814N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1046N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1237 ↔ 13771 Publication
Disulfide bondi1339 ↔ 13691 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.
O-glycosylated; with core 1 or possibly core 8 glycans. An N-terminal peptide contains chondroitin sulfate.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP39059.
PaxDbiP39059.
PeptideAtlasiP39059.
PRIDEiP39059.

PTM databases

iPTMnetiP39059.
PhosphoSitePlusiP39059.
UniCarbKBiP39059.

Expressioni

Tissue specificityi

Expressed predominantly in internal organs such as adrenal gland, pancreas and kidney.

Gene expression databases

BgeeiENSG00000204291.
CleanExiHS_COL15A1.
ExpressionAtlasiP39059. baseline and differential.
GenevisibleiP39059. HS.

Organism-specific databases

HPAiHPA017913.
HPA017915.

Interactioni

Subunit structurei

Trimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi107702. 1 interactor.
IntActiP39059. 4 interactors.
STRINGi9606.ENSP00000364140.

Structurei

Secondary structure

11388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1135 – 1140Combined sources6
Helixi1141 – 1145Combined sources5
Helixi1146 – 1150Combined sources5
Beta strandi1155 – 1159Combined sources5
Turni1160 – 1163Combined sources4
Beta strandi1164 – 1169Combined sources6
Beta strandi1172 – 1175Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N3FX-ray2.00A/B1133-1186[»]
ProteinModelPortaliP39059.
SMRiP39059.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 249Laminin G-likeAdd BLAST184
Repeati358 – 4081Add BLAST51
Repeati409 – 4592Add BLAST51
Repeati460 – 5093Add BLAST50
Repeati510 – 5554Add BLAST46
Domaini619 – 680Collagen-like 1Add BLAST62
Domaini681 – 731Collagen-like 2Add BLAST51
Domaini823 – 865Collagen-like 3Add BLAST43
Domaini879 – 927Collagen-like 4Add BLAST49

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 555Nonhelical region 1 (NC1)Add BLAST327
Regioni358 – 5554 X tandem repeatsAdd BLAST198
Regioni556 – 573Triple-helical region 1 (COL1)Add BLAST18
Regioni574 – 618Nonhelical region 2 (NC2)Add BLAST45
Regioni619 – 732Triple-helical region 2 (COL2)Add BLAST114
Regioni733 – 763Nonhelical region 3 (NC3)Add BLAST31
Regioni764 – 798Triple-helical region 3 (COL3)Add BLAST35
Regioni799 – 822Nonhelical region 4 (NC4)Add BLAST24
Regioni823 – 867Triple-helical region 4 (COL4)Add BLAST45
Regioni868 – 878Nonhelical region 5 (NC5)Add BLAST11
Regioni879 – 949Triple-helical region 5 (COL5)Add BLAST71
Regioni950 – 983Nonhelical region 6 (NC6)Add BLAST34
Regioni984 – 1013Triple-helical region 6 (COL6)Add BLAST30
Regioni1014 – 1027Nonhelical region 7 (NC7)Add BLAST14
Regioni1028 – 1045Triple-helical region 7 (COL7)Add BLAST18
Regioni1046 – 1052Nonhelical region 8 (NC8)7
Regioni1053 – 1107Triple-helical region 8 (COL8)Add BLAST55
Regioni1108 – 1117Nonhelical region 9 (NC9)10
Regioni1118 – 1132Triple-helical region 9 (COL9)Add BLAST15
Regioni1133 – 1388Nonhelical region 10 (NC10)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.
InParanoidiP39059.
KOiK08135.
OMAiGVEDGHQ.
OrthoDBiEOG091G01N2.
PhylomeDBiP39059.
TreeFamiTF315821.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di3.10.100.10. 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]
SMARTiSM00210. 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.

P39059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRRNNGQC WCLLMLLSVS TPLPAVTQTR GATETASQGH LDLTQLIGVP
60 70 80 90 100
LPSSVSFVTG YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVVVKPS
110 120 130 140 150
STRGGVLFAI TDAFQKVIYL GLRLSGVEDG HQRIILYYTE PGSHVSQEAA
160 170 180 190 200
AFSVPVMTHR WNRFAMIVQG EEVTLLVNCE EHSRIPFQRS SQALAFESSA
210 220 230 240 250
GIFMGNAGAT GLERFTGSLQ QLTVHPDPRT PEELCDPEES SASGETSGLQ
260 270 280 290 300
EADGVAEILE AVTYTQASPK EAKVEPINTP PTPSSPFEDM ELSGEPVPEG
310 320 330 340 350
TLETTNMSII QHSSPKQGSG EILNDTLEGV HSVDGDPITD SGSGAGAFLD
360 370 380 390 400
IAEEKNLAAT AAGLAEVPIS TAGEAEASSV PTGGPTLSMS TENPEEGVTP
410 420 430 440 450
GPDNEERLAA TAAGEAEALA SMPGEVEASG VAPGELDLSM SAQSLGEEAT
460 470 480 490 500
VGPSSEDSLT TAAAATEVSL STFEDEEASG VPTDGLAPLT ATMAPERAVT
510 520 530 540 550
SGPGDEEDLA AATTEEPLIT AGGEESGSPP PDGPPLPLPT VAPERWITPA
560 570 580 590 600
QREHVGMKGQ AGPKGEKGDA GEELPGPPEP SGPVGPTAGA EAEGSGLGWG
610 620 630 640 650
SDVGSGSGDL VGSEQLLRGP PGPPGPPGLP GIPGKPGTDV FMGPPGSPGE
660 670 680 690 700
DGPAGEPGPP GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG
710 720 730 740 750
LPGPPGKKGQ AGPPGVMGPP GPPGPPGPPG PGCTMGLGFE DTEGSGSTQL
760 770 780 790 800
LNEPKLSRPT AAIGLKGEKG DRGPKGERGM DGASIVGPPG PRGPPGHIKV
810 820 830 840 850
LSNSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR GPKGDTGLPG
860 870 880 890 900
FPGLKGEQGE KGEPGAILTE DIPLERLMGK KGEPGMHGAP GPMGPKGPPG
910 920 930 940 950
HKGEFGLPGR PGRPGLNGLK GTKGDPGVIM QGPPGLPGPP GPPGPPGAVI
960 970 980 990 1000
NIKGAIFPIP VRPHCKMPVD TAHPGSPELI TFHGVKGEKG SWGLPGSKGE
1010 1020 1030 1040 1050
KGDQGAQGPP GPPLDLAYLR HFLNNLKGEN GDKGFKGEKG EKGDINGSFL
1060 1070 1080 1090 1100
MSGPPGLPGN PGPAGQKGET VVGPQGPPGA PGLPGPPGFG RPGDPGPPGP
1110 1120 1130 1140 1150
PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN MDDMLQKAHL
1160 1170 1180 1190 1200
VIEGTFIYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ
1210 1220 1230 1240 1250
LLPPPNPISS ANYEKPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY
1260 1270 1280 1290 1300
RAFLSSHLQD LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNM
1310 1320 1330 1340 1350
HIPIYSFDGR DIMTDPSWPQ KVIWHGSSPH GVRLVDNYCE AWRTADTAVT
1360 1370 1380
GLASPLSTGK ILDQKAYSCA NRLIVLCIEN SFMTDARK
Length:1,388
Mass (Da):141,720
Last modified:July 5, 2005 - v2
Checksum:iAF54DDCC136C3745
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10C → S in BAA04762 (PubMed:8307960).Curated1
Sequence conflicti49V → D in AAA58429 (PubMed:8106446).Curated1
Sequence conflicti94 – 95SV → RA in AAA58429 (PubMed:8106446).Curated2
Sequence conflicti94 – 95SV → RA in BAA04762 (PubMed:8307960).Curated2
Sequence conflicti150A → P in AAA58429 (PubMed:8106446).Curated1
Sequence conflicti409A → R in AAA58429 (PubMed:8106446).Curated1
Sequence conflicti409A → R in AAC78500 (PubMed:9651385).Curated1
Sequence conflicti1134L → LLGELIPIPADSPPPPALSS N in AAC78500 (PubMed:9651385).Curated1
Sequence conflicti1178 – 1197Missing in AAC78500 (PubMed:9651385).CuratedAdd BLAST20
Sequence conflicti1227F → V in AAC78500 (PubMed:9651385).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033787163R → H.Corresponds to variant rs2075662dbSNPEnsembl.1
Natural variantiVAR_033788204M → V.1 PublicationCorresponds to variant rs2075663dbSNPEnsembl.1
Natural variantiVAR_033789391T → M.Corresponds to variant rs10988532dbSNPEnsembl.1
Natural variantiVAR_033790442A → T.Corresponds to variant rs16918128dbSNPEnsembl.1
Natural variantiVAR_033791446G → R.Corresponds to variant rs35934703dbSNPEnsembl.1
Natural variantiVAR_048776504G → V.Corresponds to variant rs2297603dbSNPEnsembl.1
Natural variantiVAR_033792506E → D.Corresponds to variant rs35250850dbSNPEnsembl.1
Natural variantiVAR_033793531P → R.Corresponds to variant rs35529307dbSNPEnsembl.1
Natural variantiVAR_061114705P → L.Corresponds to variant rs41308900dbSNPEnsembl.1
Natural variantiVAR_033794989K → R.Corresponds to variant rs35642150dbSNPEnsembl.1
Natural variantiVAR_0337951001K → R.Corresponds to variant rs35544077dbSNPEnsembl.1
Natural variantiVAR_0337961332V → I.Corresponds to variant rs10519dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25286 mRNA. Translation: AAA58429.1.
L25280
, L25281, L25282, L25283, L25284, L25285, AF052956, AF052957, AF052958, AF052959, AF052960, AF052961, AF052962, AF052963, AF052964, AF052965, AF052966, AF052967, AF052968, AF052969, AF052970, AF052971, AF052972, AF052973, AF052974, AF052975 Genomic DNA. Translation: AAC78500.1.
AL136084, AL354923 Genomic DNA. Translation: CAI17044.2.
AL354923, AL136084 Genomic DNA. Translation: CAI12548.2.
D21230 mRNA. Translation: BAA04762.1.
L01697 mRNA. No translation available.
CCDSiCCDS35081.1.
PIRiA53317.
RefSeqiNP_001846.3. NM_001855.4.
XP_011516516.1. XM_011518214.2.
UniGeneiHs.409034.

Genome annotation databases

EnsembliENST00000375001; ENSP00000364140; ENSG00000204291.
GeneIDi1306.
KEGGihsa:1306.
UCSCiuc004azb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25286 mRNA. Translation: AAA58429.1.
L25280
, L25281, L25282, L25283, L25284, L25285, AF052956, AF052957, AF052958, AF052959, AF052960, AF052961, AF052962, AF052963, AF052964, AF052965, AF052966, AF052967, AF052968, AF052969, AF052970, AF052971, AF052972, AF052973, AF052974, AF052975 Genomic DNA. Translation: AAC78500.1.
AL136084, AL354923 Genomic DNA. Translation: CAI17044.2.
AL354923, AL136084 Genomic DNA. Translation: CAI12548.2.
D21230 mRNA. Translation: BAA04762.1.
L01697 mRNA. No translation available.
CCDSiCCDS35081.1.
PIRiA53317.
RefSeqiNP_001846.3. NM_001855.4.
XP_011516516.1. XM_011518214.2.
UniGeneiHs.409034.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N3FX-ray2.00A/B1133-1186[»]
ProteinModelPortaliP39059.
SMRiP39059.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107702. 1 interactor.
IntActiP39059. 4 interactors.
STRINGi9606.ENSP00000364140.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP39059.
PhosphoSitePlusiP39059.
UniCarbKBiP39059.

Polymorphism and mutation databases

DMDMi68839886.

Proteomic databases

MaxQBiP39059.
PaxDbiP39059.
PeptideAtlasiP39059.
PRIDEiP39059.

Protocols and materials databases

DNASUi1306.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375001; ENSP00000364140; ENSG00000204291.
GeneIDi1306.
KEGGihsa:1306.
UCSCiuc004azb.3. human.

Organism-specific databases

CTDi1306.
DisGeNETi1306.
GeneCardsiCOL15A1.
H-InvDBHIX0008227.
HGNCiHGNC:2192. COL15A1.
HPAiHPA017913.
HPA017915.
MIMi120325. gene.
neXtProtiNX_P39059.
OpenTargetsiENSG00000204291.
PharmGKBiPA26708.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3546. Eukaryota.
ENOG410XQ04. LUCA.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiP39059.
KOiK08135.
OMAiGVEDGHQ.
OrthoDBiEOG091G01N2.
PhylomeDBiP39059.
TreeFamiTF315821.

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

ChiTaRSiCOL15A1. human.
GeneWikiiCollagen,_type_XV,_alpha_1.
GenomeRNAii1306.
PROiP39059.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204291.
CleanExiHS_COL15A1.
ExpressionAtlasiP39059. baseline and differential.
GenevisibleiP39059. HS.

Family and domain databases

CDDicd00247. Endostatin-like. 1 hit.
Gene3Di3.10.100.10. 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]
SMARTiSM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCOFA1_HUMAN
AccessioniPrimary (citable) accession number: P39059
Secondary accession number(s): Q5T6J4, Q9UDC5, Q9Y4W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.