ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O43827


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ANGL7_HUMAN
Primary accession number O43827
Secondary accession number Q4ZGK4
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 57)
Name and origin of the protein
Protein name Angiopoietin-related protein 7 [Precursor]
Synonyms Angiopoietin-like 7
Angiopoietin-like factor
Cornea-derived transcript 6 protein
Gene name
Name: ANGPTL7
Synonyms: CDT6
ORFNames: UNQ313/PRO356
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Cornea;
PubMed=9727400 [NCBI, ExPASy, EBI, Israel, Japan]
Peek R., van Gelderen B.E., Bruinenberg M., Kijlstra A.;
"Molecular cloning of a new angiopoietin-like factor from the human cornea.";
Invest. Ophthalmol. Vis. Sci. 39:1782-1788(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/sj.gene.6363745; PubMed=11426320 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Genes Immun. 2:119-127(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-51; HIS-140 AND HIS-175.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 27-41.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y16132; CAA76078.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ300188; CAC15571.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358301; AAQ88668.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT009802; AAP88804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ012507; AAY22173.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049653; CAB44734.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391561; CAB44734.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391561; CAI17229.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049653; CAI17229.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001881; AAH01881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_066969.1; -.
UniGene Hs.146559
3D structure databases
HSSP Q9U8W8; 1JC9. [HSSP ENTRY / PDB]
ModBase O43827.
Polymorphism databases
NIEHS-SNPs ANGPTL7.
Organism-specific databases
H-InvDB HIX0000122; -.
HGNC HGNC:24078; ANGPTL7.
GenAtlas ANGPTL7.
PharmGKB PA134959516; -.
GeneCards O43827.
Gene expression databases
ArrayExpress O43827; -.
CleanEx HS_ANGPTL7; -.
GermOnline ENSG00000171819; Homo sapiens.
Ontologies
GO
GO:0006979; Biological process: response to oxidative stress (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002181; Fibrinogen_a/b/g_C.
IPR014716; Fibrinogen_a/b/g_C_1.
Graphical view of domain structure.
Gene3D G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
Pfam PF00147; Fibrinogen_C; 1.
Pfam graphical view of domain structure.
SMART SM00186; FBG; 1.
SMART graphical view of domain structure.
PROSITE PS00514; FIBRIN_AG_C_DOMAIN; FALSE_NEG.
BLOCKS O43827.
Genome annotation databases
Ensembl ENSG00000171819; Homo sapiens. [Contig view]
GeneID 10218; -.
KEGG hsa:10218; -.
Phylogenomic databases
HOGENOM O43827; -.
HOVERGEN O43827; -.
Other
ProtoNet O43827.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Coiled coil; Direct protein sequencing; Glycoprotein; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26      
CHAIN   27   346  320     Angiopoietin-related protein 7. PRO_0000009131
DOMAIN   128   342  215     Fibrinogen C-terminal. 
COILED   39   119  81     Potential. 
CARBOHYD   58    58        N-linked (GlcNAc...) (Potential). 
CARBOHYD   253   253        N-linked (GlcNAc...) (Potential). 
CARBOHYD   267   267        N-linked (GlcNAc...) (Potential). 
DISULFID   131   162        By similarity. 
DISULFID   285   298        By similarity. 
VARIANT   51    51  1     E -> D. VAR_025075 
VARIANT   140   140  1     R -> H. VAR_025076 
VARIANT   175   175  1     Q -> H. VAR_025077 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 40018 Da [This is the MW of the unprocessed precursor] CRC64: AEC0A601CC498B43 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLKKPLSAVT WLCIFIVAFV SHPAWLQKLS KHKTPAQPQL KAANCCEEVK ELKAQVANLS 

        70         80         90        100        110        120 
SLLSELNKKQ ERDWVSVVMQ VMELESNSKR MESRLTDAES KYSEMNNQID IMQLQAAQTV 

       130        140        150        160        170        180 
TQTSADAIYD CSSLYQKNYR ISGVYKLPPD DFLGSPELEV FCDMETSGGG WTIIQRRKSG 

       190        200        210        220        230        240 
LVSFYRDWKQ YKQGFGSIRG DFWLGNEHIH RLSRQPTRLR VEMEDWEGNL RYAEYSHFVL 

       250        260        270        280        290        300 
GNELNSYRLF LGNYTGNVGN DALQYHNNTA FSTKDKDNDN CLDKCAQLRK GGYWYNCCTD 

       310        320        330        340 
SNLNGVYYRL GEHNKHLDGI TWYGWHGSTY SLKRVEMKIR PEDFKP 

O43827 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!