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P39059

- COFA1_HUMAN

UniProt

P39059 - COFA1_HUMAN

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Protein

Collagen alpha-1(XV) chain

Gene

COL15A1

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

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. collagen catabolic process Source: Reactome
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Cell adhesion, Differentiation

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2192. COL15A1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type XV trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26708.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 13881361Collagen alpha-1(XV) chainPRO_0000005788Add
BLAST
Chaini1198 – 1386189RestinPRO_0000005789Add
BLAST
Chaini1207 – 1386180Restin-2PRO_0000423014Add
BLAST
Chaini1213 – 1386174Restin-3PRO_0000423015Add
BLAST
Chaini1221 – 1386166Restin-4PRO_0000423016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi265 – 2651O-linked (GalNAc...)1 Publication
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1046 – 10461N-linked (GlcNAc...)Sequence Analysis
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.
PRIDEiP39059.

PTM databases

PhosphoSiteiP39059.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP39059.
CleanExiHS_COL15A1.
GenevestigatoriP39059.

Organism-specific databases

HPAiHPA017913.
HPA017915.

Interactioni

Subunit structurei

Trimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi107702. 2 interactions.
IntActiP39059. 4 interactions.
STRINGi9606.ENSP00000364140.

Structurei

Secondary structure

1
1388
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1135 – 11406Combined sources
Helixi1141 – 11455Combined sources
Helixi1146 – 11505Combined sources
Beta strandi1155 – 11595Combined sources
Turni1160 – 11634Combined sources
Beta strandi1164 – 11696Combined sources
Beta strandi1172 – 11754Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N3FX-ray2.00A/B1133-1186[»]
ProteinModelPortaliP39059.
SMRiP39059. Positions 1133-1186, 1215-1382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 249184Laminin G-likeAdd
BLAST
Repeati358 – 408511Add
BLAST
Repeati409 – 459512Add
BLAST
Repeati460 – 509503Add
BLAST
Repeati510 – 555464Add
BLAST
Domaini619 – 68062Collagen-like 1Add
BLAST
Domaini681 – 73151Collagen-like 2Add
BLAST
Domaini823 – 86543Collagen-like 3Add
BLAST
Domaini879 – 92749Collagen-like 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 555327Nonhelical region 1 (NC1)Add
BLAST
Regioni358 – 5551984 X tandem repeatsAdd
BLAST
Regioni556 – 57318Triple-helical region 1 (COL1)Add
BLAST
Regioni574 – 61845Nonhelical region 2 (NC2)Add
BLAST
Regioni619 – 732114Triple-helical region 2 (COL2)Add
BLAST
Regioni733 – 76331Nonhelical region 3 (NC3)Add
BLAST
Regioni764 – 79835Triple-helical region 3 (COL3)Add
BLAST
Regioni799 – 82224Nonhelical region 4 (NC4)Add
BLAST
Regioni823 – 86745Triple-helical region 4 (COL4)Add
BLAST
Regioni868 – 87811Nonhelical region 5 (NC5)Add
BLAST
Regioni879 – 94971Triple-helical region 5 (COL5)Add
BLAST
Regioni950 – 98334Nonhelical region 6 (NC6)Add
BLAST
Regioni984 – 101330Triple-helical region 6 (COL6)Add
BLAST
Regioni1014 – 102714Nonhelical region 7 (NC7)Add
BLAST
Regioni1028 – 104518Triple-helical region 7 (COL7)Add
BLAST
Regioni1046 – 10527Nonhelical region 8 (NC8)
Regioni1053 – 110755Triple-helical region 8 (COL8)Add
BLAST
Regioni1108 – 111710Nonhelical region 9 (NC9)
Regioni1118 – 113215Triple-helical region 9 (COL9)Add
BLAST
Regioni1133 – 1388256Nonhelical region 10 (NC10)Add
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiP39059.
KOiK08135.
OMAiPELITFH.
OrthoDBiEOG7NSB2B.
PhylomeDBiP39059.
TreeFamiTF315821.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101C → S in BAA04762. (PubMed:8307960)Curated
Sequence conflicti49 – 491V → D in AAA58429. (PubMed:8106446)Curated
Sequence conflicti94 – 952SV → RA in AAA58429. (PubMed:8106446)Curated
Sequence conflicti94 – 952SV → RA in BAA04762. (PubMed:8307960)Curated
Sequence conflicti150 – 1501A → P in AAA58429. (PubMed:8106446)Curated
Sequence conflicti409 – 4091A → R in AAA58429. (PubMed:8106446)Curated
Sequence conflicti409 – 4091A → R in AAC78500. (PubMed:9651385)Curated
Sequence conflicti1134 – 11341L → LLGELIPIPADSPPPPALSS N in AAC78500. (PubMed:9651385)Curated
Sequence conflicti1178 – 119720Missing in AAC78500. (PubMed:9651385)CuratedAdd
BLAST
Sequence conflicti1227 – 12271F → V in AAC78500. (PubMed:9651385)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631R → H.
Corresponds to variant rs2075662 [ dbSNP | Ensembl ].
VAR_033787
Natural varianti204 – 2041M → V.1 Publication
Corresponds to variant rs2075663 [ dbSNP | Ensembl ].
VAR_033788
Natural varianti391 – 3911T → M.
Corresponds to variant rs10988532 [ dbSNP | Ensembl ].
VAR_033789
Natural varianti442 – 4421A → T.
Corresponds to variant rs16918128 [ dbSNP | Ensembl ].
VAR_033790
Natural varianti446 – 4461G → R.
Corresponds to variant rs35934703 [ dbSNP | Ensembl ].
VAR_033791
Natural varianti504 – 5041G → V.
Corresponds to variant rs2297603 [ dbSNP | Ensembl ].
VAR_048776
Natural varianti506 – 5061E → D.
Corresponds to variant rs35250850 [ dbSNP | Ensembl ].
VAR_033792
Natural varianti531 – 5311P → R.
Corresponds to variant rs35529307 [ dbSNP | Ensembl ].
VAR_033793
Natural varianti705 – 7051P → L.
Corresponds to variant rs41308900 [ dbSNP | Ensembl ].
VAR_061114
Natural varianti989 – 9891K → R.
Corresponds to variant rs35642150 [ dbSNP | Ensembl ].
VAR_033794
Natural varianti1001 – 10011K → R.
Corresponds to variant rs35544077 [ dbSNP | Ensembl ].
VAR_033795
Natural varianti1332 – 13321V → I.
Corresponds to variant rs10519 [ dbSNP | Ensembl ].
VAR_033796

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.
UniGeneiHs.409034.

Genome annotation databases

EnsembliENST00000375001; ENSP00000364140; ENSG00000204291.
GeneIDi1306.
KEGGihsa:1306.
UCSCiuc004azb.2. human.

Polymorphism databases

DMDMi68839886.

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.
CCDSi CCDS35081.1.
PIRi A53317.
RefSeqi NP_001846.3. NM_001855.4.
UniGenei Hs.409034.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3N3F X-ray 2.00 A/B 1133-1186 [» ]
ProteinModelPortali P39059.
SMRi P39059. Positions 1133-1186, 1215-1382.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107702. 2 interactions.
IntActi P39059. 4 interactions.
STRINGi 9606.ENSP00000364140.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P39059.

Polymorphism databases

DMDMi 68839886.

Proteomic databases

MaxQBi P39059.
PaxDbi P39059.
PRIDEi P39059.

Protocols and materials databases

DNASUi 1306.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375001 ; ENSP00000364140 ; ENSG00000204291 .
GeneIDi 1306.
KEGGi hsa:1306.
UCSCi uc004azb.2. human.

Organism-specific databases

CTDi 1306.
GeneCardsi GC09P101705.
H-InvDB HIX0008227.
HGNCi HGNC:2192. COL15A1.
HPAi HPA017913.
HPA017915.
MIMi 120325. gene.
neXtProti NX_P39059.
PharmGKBi PA26708.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00710000106713.
HOGENOMi HOG000231591.
HOVERGENi HBG080337.
InParanoidi P39059.
KOi K08135.
OMAi PELITFH.
OrthoDBi EOG7NSB2B.
PhylomeDBi P39059.
TreeFami TF315821.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi COL15A1. human.
GeneWikii Collagen,_type_XV,_alpha_1.
GenomeRNAii 1306.
NextBioi 5345.
PROi P39059.
SOURCEi Search...

Gene expression databases

Bgeei P39059.
CleanExi HS_COL15A1.
Genevestigatori P39059.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
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. "Primary structure of the alpha 1 chain of human type XV collagen and exon-intron organization in the 3' region of the corresponding gene."
    Kivirikko S., Heinamaki P., Rehn M.V., Honkanen N., Myers J.C., Pihlajaniemi T.
    J. Biol. Chem. 269:4773-4779(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Umbilical cord.
  2. "Complete exon-intron organization of the human gene for the alpha1 chain of type XV collagen (COL15A1) and comparison with the homologous COL18A1 gene."
    Haegg P.M., Muona A., Lietard J., Kivirikko S., Pihlajaniemi T.
    J. Biol. Chem. 273:17824-17831(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The human alpha 1(XV) collagen chain contains a large amino-terminal non-triple helical domain with a tandem repeat structure and homology to alpha 1(XVIII) collagen."
    Muragaki Y., Abe N., Ninomiya Y., Olsen B.R., Ooshima A.
    J. Biol. Chem. 269:4042-4046(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-569, VARIANT VAL-204.
    Tissue: Placenta.
  5. "Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region."
    Myers J.C., Kivirikko S., Gordon M.K., Dion A.S., Pihlajaniemi T.
    Proc. Natl. Acad. Sci. U.S.A. 89:10144-10148(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 544-1252.
  6. "Chromosomal assignment of a gene encoding a new collagen type (COL15A1) to 9q21 --> q22."
    Huebner K., Cannizzaro L.A., Jabs E.W., Kivirikko S., Manzone H., Pihlajaniemi T., Myers J.C.
    Genomics 14:220-224(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1105-1145, CHROMOSOMAL LOCATION.
    Tissue: Placenta.
  7. "Identification and characterization of novel endogenous proteolytic forms of the human angiogenesis inhibitors restin and endostatin."
    John H., Radtke K., Staendker L., Forssmann W.G.
    Biochim. Biophys. Acta 1747:161-170(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1198-1210; 1207-1219; 1213-1225 AND 1221-1233, IDENTIFICATION OF RESTIN-RELATED PEPTIDES, DISULFIDE BOND.
  8. "Antiangiogenic activity of restin, NC10 domain of human collagen XV: comparison to endostatin."
    Ramchandran R., Dhanabal M., Volk R., Waterman M.J.F., Segal M., Lu H., Knebelmann B., Sukhatme V.P.
    Biochem. Biophys. Res. Commun. 255:735-739(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells."
    Li D., Clark C.C., Myers J.C.
    J. Biol. Chem. 275:22339-22347(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, INTERCHAIN DISULFIDE BONDS.
  10. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-265, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

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 26, 2014
This is version 136 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

External Data

Dasty 3