ID H0Y199_OTOGA Unreviewed; 676 AA.
AC H0Y199;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Vasorin {ECO:0000313|Ensembl:ENSOGAP00000022142.1};
GN Name=VASN {ECO:0000313|Ensembl:ENSOGAP00000022142.1};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000022142.1, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000022142.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAQR03078351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003790884.1; XM_003790836.2.
DR AlphaFoldDB; H0Y199; -.
DR STRING; 30611.ENSOGAP00000022142; -.
DR Ensembl; ENSOGAT00000025345.1; ENSOGAP00000022142.1; ENSOGAG00000028524.1.
DR GeneID; 100944725; -.
DR KEGG; oga:100944725; -.
DR CTD; 114990; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159318; -.
DR HOGENOM; CLU_432517_0_0_1; -.
DR InParanoid; H0Y199; -.
DR OMA; GPWVRES; -.
DR OrthoDB; 5353685at2759; -.
DR TreeFam; TF351825; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071461; P:cellular response to redox state; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24373; SLIT RELATED LEUCINE-RICH REPEAT NEURONAL PROTEIN; 1.
DR PANTHER; PTHR24373:SF275; VASORIN; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..676
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003545687"
FT TRANSMEM 580..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..445
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 463..561
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 356..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 435..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 676 AA; 72540 MW; 9374EDC1E3589DAE CRC64;
MPSRIPWPPV PLLLFLLLAF GPRVQGCPSG CQCSQPQTVF CTARQGTTVP QDVPLDTVGL
YVFENGITTL DADSFAGLPN LQLLDLSQNQ ITSLPGGVFQ PLANLSNLDL TANRLREITN
ETFRGLRRLE RLYLGKNCIR HIQPGAFDAL DRLLELKLQD NELQLLPPLR LPRLLLLDLS
HNSLLALEPG VLDTPNVEAL RLAGLGLQQL DEELFSHLRN LHDLDVADNH LEQVPPVIRG
LRGLTRLRLA GNTHIAQLRP EDLAGLAALQ ELDLSNLNLQ ALPSDLSGLF PRLRLLAAAR
NPFNCVCPLS WFGPWVRESH VTLASPEETR CHFPPKNAGR LLLELDYADF GCPATTTTAT
APTTRPAARE PTLLPSSLAP TWLSPTEPVT EALSPPTTAL PTVGPAPKPQ DCPPSMCLNG
GTCHLGVQYH LECLCPKGFT GLYCESQVEP GLWPSPTPAT PRPPQPPPLG IEPVSPTSLR
VGLQRYLQGS TVQLRSLRLT YRNLSGPDKR LVTLRLPASL SEYTVTQLRP NATYSICVMP
LGPGRVPEGE EACGEARTPP AIRSNHAPVT QAREGNLPLL IAPALAAVLL AALAAAGAAY
CVRRGRAVAA AAQDKGKVGP GAGPLELEGV KAPLESDPKA PEGGGEALPS GPECEVPLMG
YPGPSLQGPM HSKPYV
//
