ANGL6_MOUSE
ID ANGL6_MOUSE Reviewed; 457 AA.
AC Q8R0Z6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Angiopoietin-related protein 6;
DE AltName: Full=Angiopoietin-like protein 6;
DE AltName: Full=Angiopoietin-related growth factor;
DE Flags: Precursor;
GN Name=Angptl6; Synonyms=Agf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP FUNCTION.
RX PubMed=14764539; DOI=10.1182/blood-2003-04-1272;
RA Oike Y., Ito Y., Maekawa H., Morisada T., Kubota Y., Akao M., Urano T.,
RA Yasunaga K., Suda T.;
RT "Angiopoietin-related growth factor (AGF) promotes angiogenesis.";
RL Blood 103:3760-3765(2004).
RN [4]
RP FUNCTION.
RX PubMed=15778720; DOI=10.1038/nm1214;
RA Oike Y., Akao M., Yasunaga K., Yamauchi T., Morisada T., Ito Y., Urano T.,
RA Kimura Y., Kubota Y., Maekawa H., Miyamoto T., Miyata K., Matsumoto S.,
RA Sakai J., Nakagata N., Takeya M., Koseki H., Ogawa Y., Kadowaki T.,
RA Suda T.;
RT "Angiopoietin-related growth factor antagonizes obesity and insulin
RT resistance.";
RL Nat. Med. 11:400-408(2005).
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 {ECO:0000269|PubMed:12871997, ECO:0000269|PubMed:14764539,
CC ECO:0000269|PubMed:15778720}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, specifically in
CC hepatocytes, and weakly in the heart. Expressed in hematopoietic cells,
CC platelets and mast cells, and detected at wounded skin.
CC {ECO:0000269|PubMed:12871997}.
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DR EMBL; AB054065; BAB91249.1; -; mRNA.
DR EMBL; BC025904; AAH25904.1; -; mRNA.
DR CCDS; CCDS22886.1; -.
DR RefSeq; NP_660136.1; NM_145154.2.
DR AlphaFoldDB; Q8R0Z6; -.
DR SMR; Q8R0Z6; -.
DR BioGRID; 214222; 1.
DR STRING; 10090.ENSMUSP00000035784; -.
DR GlyGen; Q8R0Z6; 1 site.
DR iPTMnet; Q8R0Z6; -.
DR PhosphoSitePlus; Q8R0Z6; -.
DR MaxQB; Q8R0Z6; -.
DR PaxDb; Q8R0Z6; -.
DR PeptideAtlas; Q8R0Z6; -.
DR PRIDE; Q8R0Z6; -.
DR ProteomicsDB; 296357; -.
DR Antibodypedia; 25178; 181 antibodies from 26 providers.
DR Ensembl; ENSMUST00000043726; ENSMUSP00000035784; ENSMUSG00000038742.
DR GeneID; 70726; -.
DR KEGG; mmu:70726; -.
DR UCSC; uc009ojj.1; mouse.
DR CTD; 83854; -.
DR MGI; MGI:1917976; Angptl6.
DR VEuPathDB; HostDB:ENSMUSG00000038742; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000160969; -.
DR HOGENOM; CLU_038628_0_1_1; -.
DR InParanoid; Q8R0Z6; -.
DR OMA; AAPRCTY; -.
DR OrthoDB; 525245at2759; -.
DR PhylomeDB; Q8R0Z6; -.
DR TreeFam; TF336658; -.
DR BioGRID-ORCS; 70726; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8R0Z6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R0Z6; protein.
DR Bgee; ENSMUSG00000038742; Expressed in yolk sac and 116 other tissues.
DR Genevisible; Q8R0Z6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
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 2: Evidence at transcript level;
KW Angiogenesis; Coiled coil; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..457
FT /note="Angiopoietin-related protein 6"
FT /id="PRO_0000009129"
FT DOMAIN 238..456
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 201..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..77
FT /evidence="ECO:0000255"
FT COILED 126..164
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 247..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 397..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 457 AA; 51095 MW; B7C4289E3FEC6C3E CRC64;
MGTARLRKLQ LLLLLGAWRA LGGAARCRVT LVLSPQKATS AVCRSSEATQ DSELATLRMR
LGRHEELLRA LQRRAAEGGA LADEVRALRE HSLTLNTRLG QLRAQLQQEA RAEPDLGAEP
AAALGLLAER ALDAEAEARR TTARLQQLDA QLREHAQLMS QHSSLLGRLQ RACAGPERGQ
QQVLPLPLAP LVPLSLVGSA SNTSRRLDQT PEHQREQSLR QQGPPSSLLP TGHLAVPTRP
VGPWRDCAEA HGAGHWQSGV YDLRLGRRVV AVWCEQQQEG GGWTVIQRRQ DGSVNFFTNW
QHYKAGFGRP EGEYWLGLEP VHQVTSRGDH ELLILLEDWG GRAARAHYDS FSLEPESDHY
RLRLGQYHGD AGDSLSWHND KPFSTVDRDR DSYSGNCALY HRGGWWYHAC AHSNLNGVWY
HGGHYRSRYQ DGVYWAEFRG GAYSLKKAVM LTRLVRL
