ID H2Q953_PANTR Unreviewed; 1170 AA.
AC H2Q953; A0A2J8QDB9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Thrombospondin 1 {ECO:0000313|EMBL:JAA43410.1, ECO:0000313|Ensembl:ENSPTRP00000011794.2};
GN Name=THBS1 {ECO:0000313|EMBL:JAA43410.1,
GN ECO:0000313|Ensembl:ENSPTRP00000011794.2, ECO:0000313|VGNC:VGNC:1597};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000011794.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000011794.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA43410.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA43410.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000011794.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC {ECO:0000256|ARBA:ARBA00009456}.
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; AACZ04038091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABE01001329; JAA43410.1; -; mRNA.
DR RefSeq; XP_016783411.1; XM_016927922.1.
DR RefSeq; XP_510294.3; XM_510294.6.
DR STRING; 9598.ENSPTRP00000066460; -.
DR PaxDb; 9598-ENSPTRP00000011794; -.
DR Ensembl; ENSPTRT00000012736.3; ENSPTRP00000011794.2; ENSPTRG00000006907.5.
DR GeneID; 453319; -.
DR KEGG; ptr:453319; -.
DR CTD; 7057; -.
DR VGNC; VGNC:1597; THBS1.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000155832; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR OMA; AVPDDKF; -.
DR OrthoDB; 5345349at2759; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000002277; Chromosome 15.
DR Bgee; ENSPTRG00000006907; Expressed in fibroblast and 21 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 6.20.200.20; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR PANTHER; PTHR10199:SF78; THROMBOSPONDIN-1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 7.
DR Pfam; PF05735; TSP_C; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00209; TSP1; 3.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF103647; TSP type-3 repeat; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 4.
DR PROSITE; PS51236; TSP_CTER; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00634}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1170
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015092541"
FT DOMAIN 316..373
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 547..587
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 646..690
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 727..762
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 786..821
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 883..918
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 919..954
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 958..1170
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 839..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 129421 MW; E3245BEE8E6156B1 CRC64;
MGLAWGLGVL FLMHVCGTNR IPESGGDNSV FDIFELTGAA RKGSGRRLVK GPDPSSPAFR
IEDANLIPPV PDDKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLALERK DHSGQVFSVV
SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD
VPIQSVFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVLL
TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK
VTEENKELAN ELRRPPLCYH NGVQYRNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSTSCGNGIQ QRGRSCDSLN NRCEGSSVQT
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE
TKACKKDACP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPTPQFGGKD CVGDVTENQI
CNKQDCPIDG CLSNPCFAGV KCTSYPDGSW KCGACPPGYS GNGIQCTDVD ECKEVPDACF
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GQGVEYATAN KQVCKPRNPC TDGTHDCNKN
AKCNYLGHYS DPMFRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
HNPDQADTDN NGEGDACAAD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH
NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDSVP DIDDICPENV DISETDFRRF
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGF IRVVMYEGKK IMADSGPIYD
KTYAGGRLGL FVFSQEMVFF SDLKYECRDP
//
