ID   ANGL7_BOVIN             Reviewed;         344 AA.
AC   Q5EA66; B2Z4B5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Angiopoietin-related protein 7;
DE   AltName: Full=Angiopoietin-like protein 7;
DE   Flags: Precursor;
GN   Name=ANGPTL7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Shui Y.;
RT   "Genomic structure of Bos taurus angiopoietin-like proteins.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Has a role in the formation and organization of the
CC       extracellular matrix. In the eye, it functions as a mediator of
CC       dexamethasone-induced matrix deposition in the trabecular meshwork, the
CC       tissue responsible for the outflow of the ocular aqueous humor and for
CC       the maintenance of intraocular pressure. Is a negative regulator of
CC       angiogenesis in the cornea, and plays a major role in maintaining
CC       corneal avascularity and transparency. {ECO:0000250|UniProtKB:O43827}.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked.
CC       {ECO:0000250|UniProtKB:O43827}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43827}.
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DR   EMBL; EU599230; ACD50906.1; -; mRNA.
DR   EMBL; EU599236; ACD50912.1; -; Genomic_DNA.
DR   EMBL; BT020703; AAX08720.1; -; mRNA.
DR   RefSeq; NP_001014909.1; NM_001014909.1.
DR   AlphaFoldDB; Q5EA66; -.
DR   SMR; Q5EA66; -.
DR   STRING; 9913.ENSBTAP00000020392; -.
DR   PaxDb; Q5EA66; -.
DR   Ensembl; ENSBTAT00000020392; ENSBTAP00000020392; ENSBTAG00000015340.
DR   GeneID; 512698; -.
DR   KEGG; bta:512698; -.
DR   CTD; 10218; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015340; -.
DR   VGNC; VGNC:25895; ANGPTL7.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000157064; -.
DR   HOGENOM; CLU_038628_1_3_1; -.
DR   InParanoid; Q5EA66; -.
DR   OMA; DCASLYS; -.
DR   OrthoDB; 357340at2759; -.
DR   TreeFam; TF329953; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000015340; Expressed in anterior segment of eyeball and 60 other tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:1901346; P:negative regulation of vasculature development involved in avascular cornea development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:1903053; P:regulation of extracellular matrix organization; ISS:UniProtKB.
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   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..344
FT                   /note="Angiopoietin-related protein 7"
FT                   /id="PRO_0000009130"
FT   DOMAIN          120..341
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   COILED          37..116
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        129..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        283..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   344 AA;  39457 MW;  099534D822A595DD CRC64;
     MLKKTLSAVA WLCIFLVAFV SHPVWPQKPP KRKTPAELTA ATCCEEAKAL QAQIANLSSL
     LSDLGKKQER DWVSVVMQVM ELESSAKSME TRLTEAESKY SEMNNQIGIM QLQAAQTVTQ
     TSADAIYDCS SLYQKNYRIS GVYKLPPDDF LGSPELEVFC DMETSGGGWT IIQRRKSGLV
     SFYRDWKQYK QGFGSIRGDF WLGNDHIHRL SRRPTRLRVE MQDWEGNMRY AEYSHFVLGN
     ELNSYRLFLG NYSGDVGNDA LIYHNNTAFS TKDKDNDNCL DKCAQLRKGG YWYNCCTDSN
     LNGVYYRLGE HNKHLDGITW YGWHGSSYSL KRVEMKIRPE DFQP