ANGL6_HUMAN
ID ANGL6_HUMAN Reviewed; 470 AA.
AC Q8NI99; A5PKV7; Q9BZZ0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Angiopoietin-related protein 6;
DE AltName: Full=Angiopoietin-like protein 6;
DE AltName: Full=Angiopoietin-related growth factor;
DE AltName: Full=Angiopoietin-related protein 5;
DE Flags: Precursor;
GN Name=ANGPTL6; Synonyms=AGF, ARP5; ORFNames=UNQ152/PRO178;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12871997; DOI=10.1073/pnas.1531901100;
RA Oike Y., Yasunaga K., Ito Y., Matsumoto S., Maekawa H., Morisada T.,
RA Arai F., Nakagata N., Takeya M., Masuho Y., Suda T.;
RT "Angiopoietin-related growth factor (AGF) promotes epidermal proliferation,
RT remodeling, and regeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9494-9499(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Samal B., Wu C., Dias P., Singh S.;
RT "Molecular cloning of a novel angiopoietin-related protein.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58 AND ASN-145.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP GLYCOSYLATION AT ASN-145.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: May play a role in the wound healing process. May promote
CC epidermal proliferation, remodeling and regeneration. May promote the
CC chemotactic activity of endothelial cells and induce
CC neovascularization. May counteract high-fat diet-induced obesity and
CC related insulin resistance through increased energy expenditure.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; AB054064; BAB91248.1; -; mRNA.
DR EMBL; AF230330; AAK06404.1; -; mRNA.
DR EMBL; AY358276; AAQ88643.1; -; mRNA.
DR EMBL; CH471106; EAW84071.1; -; Genomic_DNA.
DR EMBL; BC142632; AAI42633.1; -; mRNA.
DR CCDS; CCDS12224.1; -.
DR RefSeq; NP_001308340.1; NM_001321411.1.
DR RefSeq; NP_114123.2; NM_031917.2.
DR RefSeq; XP_011526649.1; XM_011528347.2.
DR RefSeq; XP_011526652.1; XM_011528350.2.
DR RefSeq; XP_016882836.1; XM_017027347.1.
DR PDB; 6Y43; X-ray; 1.60 A; A=251-470.
DR PDBsum; 6Y43; -.
DR AlphaFoldDB; Q8NI99; -.
DR SMR; Q8NI99; -.
DR BioGRID; 123770; 3.
DR IntAct; Q8NI99; 1.
DR STRING; 9606.ENSP00000253109; -.
DR GlyConnect; 1919; 5 N-Linked glycans (2 sites).
DR GlyGen; Q8NI99; 3 sites, 5 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q8NI99; -.
DR PhosphoSitePlus; Q8NI99; -.
DR BioMuta; ANGPTL6; -.
DR DMDM; 66774050; -.
DR jPOST; Q8NI99; -.
DR MassIVE; Q8NI99; -.
DR PaxDb; Q8NI99; -.
DR PeptideAtlas; Q8NI99; -.
DR PRIDE; Q8NI99; -.
DR ProteomicsDB; 73838; -.
DR Antibodypedia; 25178; 181 antibodies from 26 providers.
DR DNASU; 83854; -.
DR Ensembl; ENST00000253109.5; ENSP00000253109.3; ENSG00000130812.11.
DR Ensembl; ENST00000592641.5; ENSP00000467930.1; ENSG00000130812.11.
DR GeneID; 83854; -.
DR KEGG; hsa:83854; -.
DR MANE-Select; ENST00000253109.5; ENSP00000253109.3; NM_031917.3; NP_114123.2.
DR UCSC; uc002mmx.3; human.
DR CTD; 83854; -.
DR DisGeNET; 83854; -.
DR GeneCards; ANGPTL6; -.
DR HGNC; HGNC:23140; ANGPTL6.
DR HPA; ENSG00000130812; Tissue enriched (liver).
DR MalaCards; ANGPTL6; -.
DR MIM; 609336; gene.
DR neXtProt; NX_Q8NI99; -.
DR OpenTargets; ENSG00000130812; -.
DR Orphanet; 231160; Familial cerebral saccular aneurysm.
DR PharmGKB; PA134950669; -.
DR VEuPathDB; HostDB:ENSG00000130812; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000160969; -.
DR HOGENOM; CLU_038628_0_1_1; -.
DR InParanoid; Q8NI99; -.
DR OMA; AAPRCTY; -.
DR OrthoDB; 525245at2759; -.
DR PhylomeDB; Q8NI99; -.
DR PathwayCommons; Q8NI99; -.
DR BioGRID-ORCS; 83854; 18 hits in 1069 CRISPR screens.
DR ChiTaRS; ANGPTL6; human.
DR GenomeRNAi; 83854; -.
DR Pharos; Q8NI99; Tbio.
DR PRO; PR:Q8NI99; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NI99; protein.
DR Bgee; ENSG00000130812; Expressed in right lobe of liver and 102 other tissues.
DR ExpressionAtlas; Q8NI99; baseline and differential.
DR Genevisible; Q8NI99; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Coiled coil; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..470
FT /note="Angiopoietin-related protein 6"
FT /id="PRO_0000009128"
FT DOMAIN 251..469
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 214..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..116
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT DISULFID 260..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 410..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 92
FT /note="E -> K (in Ref. 2; AAK06404)"
FT /evidence="ECO:0000305"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 356..366
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:6Y43"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6Y43"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:6Y43"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:6Y43"
SQ SEQUENCE 470 AA; 51694 MW; FAD20B1B00965239 CRC64;
MGKPWLRALQ LLLLLGASWA RAGAPRCTYT FVLPPQKFTG AVCWSGPAST RATPEAANAS
ELAALRMRVG RHEELLRELQ RLAAADGAVA GEVRALRKES RGLSARLGQL RAQLQHEAGP
GAGPGADLGA EPAAALALLG ERVLNASAEA QRAAARFHQL DVKFRELAQL VTQQSSLIAR
LERLCPGGAG GQQQVLPPPP LVPVVPVRLV GSTSDTSRML DPAPEPQRDQ TQRQQEPMAS
PMPAGHPAVP TKPVGPWQDC AEARQAGHEQ SGVYELRVGR HVVSVWCEQQ LEGGGWTVIQ
RRQDGSVNFF TTWQHYKAGF GRPDGEYWLG LEPVYQLTSR GDHELLVLLE DWGGRGARAH
YDGFSLEPES DHYRLRLGQY HGDAGDSLSW HNDKPFSTVD RDRDSYSGNC ALYQRGGWWY
HACAHSNLNG VWHHGGHYRS RYQDGVYWAE FRGGAYSLRK AAMLIRPLKL
