TSP2_CHICK
ID TSP2_CHICK Reviewed; 1178 AA.
AC P35440;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Thrombospondin-2;
DE Flags: Precursor;
GN Name=THBS2; Synonyms=TSP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2022631; DOI=10.1016/s0021-9258(18)92936-4;
RA Lawler J., Duquette M., Ferro P.;
RT "Cloning and sequencing of chicken thrombospondin.";
RL J. Biol. Chem. 266:8039-8043(1991).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Can bind to fibrinogen,
CC fibronectin, laminin and type V collagen (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60853; AAA51437.1; -; mRNA.
DR PIR; A39804; A39804.
DR RefSeq; NP_001001755.1; NM_001001755.1.
DR RefSeq; XP_015139539.1; XM_015284053.1.
DR AlphaFoldDB; P35440; -.
DR SMR; P35440; -.
DR STRING; 9031.ENSGALP00000018239; -.
DR PaxDb; P35440; -.
DR GeneID; 414837; -.
DR KEGG; gga:414837; -.
DR CTD; 7058; -.
DR VEuPathDB; HostDB:geneid_414837; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; P35440; -.
DR PhylomeDB; P35440; -.
DR PRO; PR:P35440; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 4.10.1080.10; -; 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; IPR001791; Laminin_G.
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; IPR015455; TSP2.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199:SF10; PTHR10199:SF10; 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 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; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF82895; SSF82895; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 8.
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; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW Heparin-binding; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1178
FT /note="Thrombospondin-2"
FT /id="PRO_0000035848"
FT DOMAIN 25..221
FT /note="Laminin G-like"
FT DOMAIN 324..381
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 387..437
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 443..498
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 500..555
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 555..595
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 654..698
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 699..734
FT /note="TSP type-3 1"
FT REPEAT 735..770
FT /note="TSP type-3 2"
FT REPEAT 771..793
FT /note="TSP type-3 3"
FT REPEAT 794..829
FT /note="TSP type-3 4"
FT REPEAT 830..852
FT /note="TSP type-3 5"
FT REPEAT 853..890
FT /note="TSP type-3 6"
FT REPEAT 891..926
FT /note="TSP type-3 7"
FT REPEAT 927..962
FT /note="TSP type-3 8"
FT DOMAIN 966..1178
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 737..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 934..936
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 742..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING ?..232
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 276
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 399..431
FT /evidence="ECO:0000250"
FT DISULFID 403..436
FT /evidence="ECO:0000250"
FT DISULFID 414..421
FT /evidence="ECO:0000250"
FT DISULFID 455..492
FT /evidence="ECO:0000250"
FT DISULFID 459..497
FT /evidence="ECO:0000250"
FT DISULFID 470..482
FT /evidence="ECO:0000250"
FT DISULFID 512..549
FT /evidence="ECO:0000250"
FT DISULFID 516..554
FT /evidence="ECO:0000250"
FT DISULFID 527..539
FT /evidence="ECO:0000250"
FT DISULFID 559..570
FT /evidence="ECO:0000250"
FT DISULFID 564..580
FT /evidence="ECO:0000250"
FT DISULFID 583..594
FT /evidence="ECO:0000250"
FT DISULFID 600..616
FT /evidence="ECO:0000250"
FT DISULFID 607..625
FT /evidence="ECO:0000250"
FT DISULFID 628..652
FT /evidence="ECO:0000250"
FT DISULFID 658..671
FT /evidence="ECO:0000250"
FT DISULFID 665..684
FT /evidence="ECO:0000250"
FT DISULFID 686..697
FT /evidence="ECO:0000250"
FT DISULFID 713..721
FT /evidence="ECO:0000250"
FT DISULFID 726..746
FT /evidence="ECO:0000250"
FT DISULFID 762..782
FT /evidence="ECO:0000250"
FT DISULFID 785..805
FT /evidence="ECO:0000250"
FT DISULFID 821..841
FT /evidence="ECO:0000250"
FT DISULFID 844..864
FT /evidence="ECO:0000250"
FT DISULFID 882..902
FT /evidence="ECO:0000250"
FT DISULFID 918..938
FT /evidence="ECO:0000250"
FT DISULFID 954..1175
FT /evidence="ECO:0000250"
SQ SEQUENCE 1178 AA; 131817 MW; F37E02F42C8717A2 CRC64;
MLQRSRLLWL AVFITLWVSS DAQDDAKEEE NTFDLLQISN INRKTIGAKL FRGPDPAIPA
YRFIRFDHIP PFKPEKLKKI VKLIRQNEGF ILSATLRQDR QSRGTILALE GPGISERQFE
IISNGRANTL DLIYWVDGFQ NVISLEDVDL ADSQWKNLTV QVTGENYNLY VGCDLIDSFI
LEEPFYEQLK AENSRMYVAK GSIRENHFRG LLQNIHLIFD TSIEDVLRKK GCQRSQSTEV
NTINESTEIL HLSPAVTTEY VGEKTEKKAE FCDRSCEELG TMFTELTGLR IVVNNLADNL
QKVSEENQIM WELIGPNKTL KNQSVCWQDG RVFADSESWI VDSCTKCTCQ DSKIVCHQIT
CPPVSCADPS FIEGECCPVC SHSDDSEEGW SPWSDWTKCS VTCGSGTQMR GRSCDVTRSA
CTGPHIQTRM CSFKKCDHRI RQDGGWSHWS PWSSCSVTCG VGNITRIRLC NSPIPQMGGK
NCVGNGRETE KCEKAPCPVN GQWGPWSPWS ACTVTCGGGI RERSRLCNSP EPQYGGKPCV
GDTKQHDMCN KRDCPIDGCL SNPCFPGAEC NSYPDGSWSC GPCPAGFLGN GTVCEDLDEC
IAVSDVCFKV NQVHRCVNTN PGFHCLPCPP RYKGSQPYGV GLEVAKTEKQ VCEPENPCKD
KTHSCHKSAE CIYLGHFSDP MYKCECRTGY AGDGRICGED SDLDGWPNNN LVCAANATYH
CVKDNCPLLP NSGQEDFDKD GKGDACDEDD DNDGVEDDKD NCPLLFNPRQ FDYDKDEVGD
RCDNCPYVHN PAQIDTDNNG EGDSCAVDID GDDIFNERDN CPYVYNTDQS DTDGDGVGDQ
CDNCPLMHNP DQTDADNDLV GDQCDNNEDI DEDGHQNNQD NCPYIPNANQ ADHDKDGKGD
ACDPDDDNDG IPDDRDNCRL RYNPEQEDSD GDGRGDICKD DFDDDNVPDI FDVCPENNAI
SETDFRKFQM VPLDPKGTAQ IDPNWVIRHQ GKELVQTANS DPGIAVGYDE FSSVDFSGTF
YVNTDRDDDY AGFVFGYQSS SRFYVLMWKQ VTQTYWEDKP TRAYGYSGVS LKVVNSTTGT
GEHLRNALWH TGNTPGQVRT LWHDPKNIGW KDYTAYRWHL IHRPKTGLIK VLVYEGKQVM
VDSGPIYDTT FAGGRLGLFV FSQEMVYFSD LKYECRDA
