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Database: UniProt
Entry: I3LS87_PIG
LinkDB: I3LS87_PIG
Original site: I3LS87_PIG 
ID   I3LS87_PIG              Unreviewed;       677 AA.
AC   I3LS87;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Vasorin {ECO:0000313|EMBL:HDA40051.1, ECO:0000313|EMBL:HDB53188.1, ECO:0000313|Ensembl:ENSSSCP00000026980.1};
GN   Name=VASN {ECO:0000313|Ensembl:ENSSSCP00000026980.1,
GN   ECO:0000313|VGNC:VGNC:94803};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000026980.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000026980.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000026980.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA40051.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000026980.1}
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; DQIR01084575; HDA40051.1; -; Transcribed_RNA.
DR   EMBL; DQIR01084576; HDA40052.1; -; Transcribed_RNA.
DR   EMBL; DQIR01087844; HDA43320.1; -; Transcribed_RNA.
DR   EMBL; DQIR01197711; HDB53188.1; -; Transcribed_RNA.
DR   EMBL; DQIR01312718; HDC68196.1; -; Transcribed_RNA.
DR   RefSeq; XP_005662230.1; XM_005662173.2.
DR   RefSeq; XP_005662231.1; XM_005662174.2.
DR   RefSeq; XP_013851147.1; XM_013995693.1.
DR   STRING; 9823.ENSSSCP00000051056; -.
DR   PaxDb; 9823-ENSSSCP00000026980; -.
DR   Ensembl; ENSSSCT00000027262.4; ENSSSCP00000026980.1; ENSSSCG00000025561.4.
DR   Ensembl; ENSSSCT00000047975.3; ENSSSCP00000051056.1; ENSSSCG00000025561.4.
DR   GeneID; 102158247; -.
DR   KEGG; ssc:102158247; -.
DR   CTD; 114990; -.
DR   VGNC; VGNC:94803; VASN.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000159318; -.
DR   HOGENOM; CLU_432517_0_0_1; -.
DR   OMA; GPWVRES; -.
DR   OrthoDB; 5353685at2759; -.
DR   TreeFam; TF351825; -.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Bgee; ENSSSCG00000025561; Expressed in forelimb bud and 35 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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: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; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00063; FN3; 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; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR24369:SF160; VASORIN; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SMART; SM00369; LRR_TYP; 8.
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   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:I3LS87};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..677
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014579593"
FT   TRANSMEM        581..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          409..446
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          466..562
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          359..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        436..445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   677 AA;  72187 MW;  D6085B931D98DB3C CRC64;
     MPPTISPPLL LPLLLLLLLA LEPRVQGCPS GCQCNQPQTV FCTARQGTTV PLDVPPDTVG
     LYIFENGITT IDTGSFAGLP GLQLLDLSQN QITSLPGGVF QPLANLSNLD LTANRLREIT
     NETFRGLRRL ERLYLGKNRI RHIQPGAFDA LEHLLELKLQ DNELRALPPL RLPRLLLLDL
     SHNSLPALEP GVLDTANVEA LRLAGLGLQQ LDEGLLGRLR NLHDLDVADN QLERVPPAIR
     GLRGLTRLRL AGNTRIAQLR PEDLAGLAAL QELDLSNLSL QVLPHELSIL FPRLRLLAAA
     RNPFNCVCPL SWFGPWVRES RVALTSPEET RCHFPPKNAG RLLLDLDYAD FGCPATTTTA
     TVPATRPTVG EPTFPPSSPA PTWLSPTEPA TVAPSLPPPA PPTEGPAPQP QDCPASICLN
     GGTCHLEARG HLECLCPEGF TGLYCESRVR QGPRPSSAPA TLQPPRPLPL SIEPVSPTSL
     RVGLQRYLQG SPLQLRSLRL TYRNLSGPDK RPVTLRLPAS LAEYTVTQLR PNATYSICVR
     PLGAGRMPEG EEACGEARTP PAVRSNHAPV TQAREGNLPL LIAPTLAAVL LAVLAAVGAA
     FCVRRGRAAA AVAQGKGQVG PGAGPLELEG VKAPLEPGPK GTEGGGEAPP GGPECEVPLM
     GYSGPGPQGP LPTKPYI
//
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