VASN_XENTR
ID VASN_XENTR Reviewed; 661 AA.
AC Q6DF55;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Vasorin;
DE Flags: Precursor;
GN Name=vasn;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as an inhibitor of TGF-beta signaling. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; BC076888; AAH76888.1; -; mRNA.
DR RefSeq; NP_001005036.1; NM_001005036.1.
DR AlphaFoldDB; Q6DF55; -.
DR SMR; Q6DF55; -.
DR PaxDb; Q6DF55; -.
DR Ensembl; ENSXETT00000037686; ENSXETP00000037686; ENSXETG00000017309.
DR GeneID; 448556; -.
DR KEGG; xtr:448556; -.
DR CTD; 114990; -.
DR Xenbase; XB-GENE-941552; vasn.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_432517_0_0_1; -.
DR InParanoid; Q6DF55; -.
DR OMA; NEETRCH; -.
DR OrthoDB; 397237at2759; -.
DR PhylomeDB; Q6DF55; -.
DR TreeFam; TF351825; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017309; Expressed in liver and 15 other tissues.
DR ExpressionAtlas; Q6DF55; baseline.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050431; F:transforming growth factor beta binding; IBA:GO_Central.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51450; LRR; 9.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..661
FT /note="Vasorin"
FT /id="PRO_0000232632"
FT TOPO_DOM 20..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..50
FT /note="LRRNT"
FT REPEAT 52..72
FT /note="LRR 1"
FT REPEAT 75..96
FT /note="LRR 2"
FT REPEAT 99..120
FT /note="LRR 3"
FT REPEAT 123..144
FT /note="LRR 4"
FT REPEAT 147..168
FT /note="LRR 5"
FT REPEAT 169..189
FT /note="LRR 6"
FT REPEAT 191..212
FT /note="LRR 7"
FT REPEAT 215..237
FT /note="LRR 8"
FT REPEAT 238..258
FT /note="LRR 9"
FT REPEAT 259..281
FT /note="LRR 10"
FT DOMAIN 293..346
FT /note="LRRCT"
FT DOMAIN 403..440
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 455..543
FT /note="Fibronectin type-III"
FT REGION 348..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 407..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 430..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 661 AA; 71958 MW; A0AC47946BE8DBEA CRC64;
MWHLLVWIIL LATAQQMITE GCPAGCQCNT PQTVFCLARK NSNFPRSVPP DTLNLYVFEN
GISSIEESSF IGLNGLHLLD LSHNQLSSLP GGVFRNLANL SNLDLTSNQL TEISADTFQG
LSRLERLYLN GNRIRSIHPE AFKGIESLLE LKLSNNQLVT PPAFSLPHLL LLDLSYNAIP
VIQQGVFNAG NIESLRLAGL GLKEVPEELL SGLKNLHELD LSDNQLDKVP PGLHGLTKLN
IAGNVGFSQI QVDDLSNLPA LQELDLSGLS LQTLPKGLFR SSKRLRAVSL AQNPFNCVCS
LGWLSEWMRV SGVVLLRPDE TRCHFPPKNA GKTLRQLRDS EYGCPAPTTI QMPSTMPPST
TTGPPTTTKH LQTEAPTTAS TTTTTIPHQE QEEDTQPFQF DFEDTLCPPQ TCLNGGSCHL
DPTGQLECEC PPGFQGTYCE TGPVTPAVVT EMYIEQVKII EVTVSSIRVD LQSYSQNKEK
LRAIRLTVRN LYGADRRPMI YKLPPTLPEY TVRALSSNSS YWVCLGSQGE GGPEEDLCTE
THTLGEPPKH SPQVTQSQEG NLTLVLVPAV AAGILLSAAV AAAACYARRR KGKGHSVEDG
GPLEMDGVKK GLDGKGEVKK LSEDPTGPEK TGAESEEPLM DSTRIGNNND APTGRLPHSY
F
