ID   THSD1_PONAB             Reviewed;         853 AA.
AC   Q5R7R7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Thrombospondin type-1 domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=THSD1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860043; CAH92193.1; -; mRNA.
DR   RefSeq; NP_001126283.1; NM_001132811.1.
DR   AlphaFoldDB; Q5R7R7; -.
DR   STRING; 9601.ENSPPYP00000006140; -.
DR   GeneID; 100173258; -.
DR   KEGG; pon:100173258; -.
DR   CTD; 55901; -.
DR   eggNOG; ENOG502QY3P; Eukaryota.
DR   InParanoid; Q5R7R7; -.
DR   Proteomes; UP000001595; 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..853
FT                   /note="Thrombospondin type-1 domain-containing protein 1"
FT                   /id="PRO_0000249586"
FT   TOPO_DOM        25..414
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..853
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          341..394
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   REGION          445..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JM61"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        353..388
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        357..393
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        368..378
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ   SEQUENCE   853 AA;  94511 MW;  614AD4433D1E34B9 CRC64;
     MKPMLKDFSN LLLVVLCDYV LGEAEYLLLR EPGHVALSND TVYVDFQYFD GANGTLRNVS
     VLLLEANTNQ TVTTKYLLTN QSQGTLKFEC FYFKEAGDYW FTMTPEATDN STPFPWWEKS
     AFLKVEWPVF HVDLNRSAKA AEGTFQVGLF TSQPLCPFPV DKPNIVVDVI FTNSLPEARR
     NSRQPLEIRT SKRTELAQGQ WVEFGCAPVG PEAYVTVVLK LLGRDSVITS TGPIGLAQKF
     GYKLVMVPEL TCESGVEVMV LPPPCTFVQG VVTVFKEAPR SPGKRTIHLA ENSLPLGERR
     TIFNCTLFDM GKNKYCFDFG ISSRSHFSAK EKECMLIQRN IETWGLWQPW SQCSATCGDG
     VRERRRVCLT SFPSRPGCPG MSLEASLCSL EECAAFQPSS PSPLQPQGPV KSNNIVTVTG
     ISLCLFIIIA TVLITLWRRF GRPAKCSTPA RHNSIHSPSF RKNSDEENIC ELSEQRGSFS
     DGGDGPTGSP GDTGIPLTYR RSGPVPPEDD ASGSESFQSN AQKIIPPLFS YRLAQQQLKE
     MKKKGLTETT KVYHVSQSPL TDTAIDAAPS APLDLESPEE AAANKFRIKS PFPEQPAVSA
     GERPPSRLDL SVTQASCAIS PSQTLIRKSQ ARHVGSRGGP SERSHARNAH FRRTASFHEA
     RQARPFRERS MSTLTPRQAP AYSTRTRTCE QAEDRFRPQS RGAHLFPEKL EHFQEASGTG
     GPLNPLPKSY TLGQPLRKPD LGDRQAGLVA GIERTEPHRA RRGPSPSHKS VSRKQSSPTS
     PKDSYQRVSP LSPSQCRKDK CQSFPTHPEF AFYDNTSFGL TEAEQRMLDL PGYFGSNEED
     ETTSTLSVEK LVI