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Protein

Angiopoietin-related protein 7

Gene

ANGPTL7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

  • response to oxidative stress Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Angiopoietin-related protein 7
Alternative name(s):
Angiopoietin-like factor
Angiopoietin-like protein 7
Cornea-derived transcript 6 protein
Gene namesi
Name:ANGPTL7
Synonyms:CDT6
ORF Names:UNQ313/PRO356
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24078. ANGPTL7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959516.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 346320Angiopoietin-related protein 7PRO_0000009131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence analysis
Disulfide bondi131 ↔ 162PROSITE-ProRule annotation
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence analysis
Disulfide bondi285 ↔ 298PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO43827.
PaxDbiO43827.
PeptideAtlasiO43827.
PRIDEiO43827.

PTM databases

iPTMnetiO43827.

Expressioni

Tissue specificityi

Highly and specifically expressed in the cornea where is confined to the stromal layer.1 Publication

Gene expression databases

BgeeiO43827.
CleanExiHS_ANGPTL7.
GenevisibleiO43827. HS.

Interactioni

Protein-protein interaction databases

BioGridi115513. 14 interactions.
STRINGi9606.ENSP00000366015.

Structurei

3D structure databases

ProteinModelPortaliO43827.
SMRiO43827. Positions 53-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 343222Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili39 – 11981Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO43827.
OMAiFVSHPVW.
OrthoDBiEOG7X9G60.
PhylomeDBiO43827.
TreeFamiTF329953.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
[Graphical view]
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O43827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKPLSAVT WLCIFIVAFV SHPAWLQKLS KHKTPAQPQL KAANCCEEVK
60 70 80 90 100
ELKAQVANLS SLLSELNKKQ ERDWVSVVMQ VMELESNSKR MESRLTDAES
110 120 130 140 150
KYSEMNNQID IMQLQAAQTV TQTSADAIYD CSSLYQKNYR ISGVYKLPPD
160 170 180 190 200
DFLGSPELEV FCDMETSGGG WTIIQRRKSG LVSFYRDWKQ YKQGFGSIRG
210 220 230 240 250
DFWLGNEHIH RLSRQPTRLR VEMEDWEGNL RYAEYSHFVL GNELNSYRLF
260 270 280 290 300
LGNYTGNVGN DALQYHNNTA FSTKDKDNDN CLDKCAQLRK GGYWYNCCTD
310 320 330 340
SNLNGVYYRL GEHNKHLDGI TWYGWHGSTY SLKRVEMKIR PEDFKP
Length:346
Mass (Da):40,018
Last modified:June 1, 1998 - v1
Checksum:iAEC0A601CC498B43
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511E → D.1 Publication
Corresponds to variant rs28990992 [ dbSNP | Ensembl ].
VAR_025075
Natural varianti140 – 1401R → H.1 Publication
Corresponds to variant rs28991002 [ dbSNP | Ensembl ].
VAR_025076
Natural varianti175 – 1751Q → H.1 Publication
Corresponds to variant rs28991009 [ dbSNP | Ensembl ].
VAR_025077

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16132 mRNA. Translation: CAA76078.1.
AJ300188 Genomic DNA. Translation: CAC15571.1.
AY358301 mRNA. Translation: AAQ88668.1.
BT009802 mRNA. Translation: AAP88804.1.
AK313716 mRNA. Translation: BAG36459.1.
DQ012507 Genomic DNA. Translation: AAY22173.1.
AB593026 mRNA. Translation: BAJ83980.1.
AB593027 mRNA. Translation: BAJ83981.1.
AL049653, AL391561 Genomic DNA. Translation: CAB44734.1.
AL391561, AL049653 Genomic DNA. Translation: CAI17229.1.
CH471130 Genomic DNA. Translation: EAW71685.1.
BC001881 mRNA. Translation: AAH01881.1.
CCDSiCCDS128.1.
RefSeqiNP_066969.1. NM_021146.3.
UniGeneiHs.146559.

Genome annotation databases

EnsembliENST00000376819; ENSP00000366015; ENSG00000171819.
GeneIDi10218.
KEGGihsa:10218.
UCSCiuc001ase.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16132 mRNA. Translation: CAA76078.1.
AJ300188 Genomic DNA. Translation: CAC15571.1.
AY358301 mRNA. Translation: AAQ88668.1.
BT009802 mRNA. Translation: AAP88804.1.
AK313716 mRNA. Translation: BAG36459.1.
DQ012507 Genomic DNA. Translation: AAY22173.1.
AB593026 mRNA. Translation: BAJ83980.1.
AB593027 mRNA. Translation: BAJ83981.1.
AL049653, AL391561 Genomic DNA. Translation: CAB44734.1.
AL391561, AL049653 Genomic DNA. Translation: CAI17229.1.
CH471130 Genomic DNA. Translation: EAW71685.1.
BC001881 mRNA. Translation: AAH01881.1.
CCDSiCCDS128.1.
RefSeqiNP_066969.1. NM_021146.3.
UniGeneiHs.146559.

3D structure databases

ProteinModelPortaliO43827.
SMRiO43827. Positions 53-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115513. 14 interactions.
STRINGi9606.ENSP00000366015.

PTM databases

iPTMnetiO43827.

Proteomic databases

MaxQBiO43827.
PaxDbiO43827.
PeptideAtlasiO43827.
PRIDEiO43827.

Protocols and materials databases

DNASUi10218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376819; ENSP00000366015; ENSG00000171819.
GeneIDi10218.
KEGGihsa:10218.
UCSCiuc001ase.5. human.

Organism-specific databases

CTDi10218.
GeneCardsiANGPTL7.
HGNCiHGNC:24078. ANGPTL7.
neXtProtiNX_O43827.
PharmGKBiPA134959516.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiO43827.
OMAiFVSHPVW.
OrthoDBiEOG7X9G60.
PhylomeDBiO43827.
TreeFamiTF329953.

Miscellaneous databases

GeneWikiiANGPTL7.
GenomeRNAii10218.
PROiO43827.

Gene expression databases

BgeeiO43827.
CleanExiHS_ANGPTL7.
GenevisibleiO43827. HS.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
[Graphical view]
PfamiPF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a new angiopoietin-like factor from the human cornea."
    Peek R., van Gelderen B.E., Bruinenberg M., Kijlstra A.
    Invest. Ophthalmol. Vis. Sci. 39:1782-1788(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Cornea.
  2. "The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
    Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
    Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-51; HIS-140 AND HIS-175.
  7. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
    Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
    Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retinoblastoma.
  8. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  11. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.

Entry informationi

Entry nameiANGL7_HUMAN
AccessioniPrimary (citable) accession number: O43827
Secondary accession number(s): B2R9B2, F1T0A6, Q4ZGK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 116 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.