THSD1_BOVIN
ID THSD1_BOVIN Reviewed; 849 AA.
AC Q5BIR3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 1;
DE Flags: Precursor;
GN Name=THSD1;
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 [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: Is a positive regulator of nascent focal adhesion assembly,
CC involved in the modulation of endothelial cell attachment to the
CC extracellular matrix. {ECO:0000250|UniProtKB:Q9NS62}.
CC -!- SUBUNIT: Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL.
CC Interacts with TLN1. {ECO:0000250|UniProtKB:Q9NS62}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9NS62};
CC Single-pass type I membrane protein {ECO:0000305}. Cell junction, focal
CC adhesion {ECO:0000250|UniProtKB:Q9NS62}. Note=Localizes to nascent
CC focal adhesions. {ECO:0000250|UniProtKB:Q9NS62}.
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DR EMBL; BT021161; AAX31343.1; -; mRNA.
DR RefSeq; NP_001014967.1; NM_001014967.1.
DR AlphaFoldDB; Q5BIR3; -.
DR SMR; Q5BIR3; -.
DR STRING; 9913.ENSBTAP00000027155; -.
DR iPTMnet; Q5BIR3; -.
DR PaxDb; Q5BIR3; -.
DR PRIDE; Q5BIR3; -.
DR GeneID; 541228; -.
DR KEGG; bta:541228; -.
DR CTD; 55901; -.
DR eggNOG; ENOG502QY3P; Eukaryota.
DR InParanoid; Q5BIR3; -.
DR OrthoDB; 130189at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR038877; THSD1.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR16311; PTHR16311; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Disulfide bond; Endosome; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..849
FT /note="Thrombospondin type-1 domain-containing protein 1"
FT /id="PRO_0000249583"
FT TOPO_DOM 25..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 340..393
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 472..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM61"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 352..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 356..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 367..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 849 AA; 92050 MW; FE8E2FCE4FC55476 CRC64;
MKQTLKDFSN LLLVVLCDYV LGEAEHLVLG EPGHVALSNS TVTVDFHGAN GTLRNVSVLL
VEASSNQTLT TKYLLTNQSQ GTLEFECFYF KEAGDYWFVM TREATNSSLP VPPRERSAFL
KVEWPVFHVD LSRTSMAAEG TFQVGLFTSQ PLCPFPGDKP DILLEVTFTN SLPEARAGQA
LPLEIRASKR VELAQGQWVE FDCPPVGPEA YVTVTVVLKL LGRDSVIMST GPIDLAQKFG
YKLVMEPELT CEAGVEVTVL PPPCIFVQGV IAVFKEAPRL PGERTNRLAE NSLALGERRT
GFNCTLFDMG RNKYCFDFGV SSQSQFSAKE KECMLIRRSI ETWGLWQPWS QCSASCGDGV
RERRRVCLTS SPSRPGCPGM SSETSPCSLE DCAAFQPSSP SPLQPQAPVK SNNVVTVTGI
SLCLFIIVAT VLITLWRKLG RAPKCSTPAR HNSLHGPGCR KNSDEENICE LSEPRGSFSD
AGDGPAGSPG DPGIPLTYRR SVPAPPDDEA SGSESFQANA QKIIPPLFSY RLAQQQLKEM
KKKGLTETTK VYHVSQSPLT DTAIDAAATA AAAAAASPGG SESPEEAAAG KFRIKSPFLE
HPPTVGAGDR PPSRLDHPFS AASCAVSPSQ TLLRKSQVRS HSRGSHFRRT ASFHEARQAR
PFRERSLSTL TPRPTPAHGP RARTWDQAGE RGRPPSRGTA LFPEKRDHGP GAAGASGPLS
PLPKPHSLGP PPRKPDLGDR QAGFVGAGER PEPPRARRGP SPSHRSVSRK QPSPPAPKDG
YQRVSPLSPS QGRKDKCQSF PAHPEFAFYD NTSFGLTEAE QRMLDLPGYF GSNEEDETTS
TLSVEKLVI
