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Database: UniProt
Entry: P35440
LinkDB: P35440
Original site: P35440 
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   10-APR-2019, entry version 146.
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;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2022631;
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
CC       cell-to-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}.
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   UniGene; Gga.797; -.
DR   ProteinModelPortal; P35440; -.
DR   SMR; P35440; -.
DR   STRING; 9031.ENSGALP00000018239; -.
DR   PaxDb; P35440; -.
DR   PRIDE; P35440; -.
DR   GeneID; 414837; -.
DR   KEGG; gga:414837; -.
DR   CTD; 7058; -.
DR   eggNOG; ENOG410IFQQ; Eukaryota.
DR   eggNOG; ENOG410XQKE; LUCA.
DR   HOGENOM; HOG000007542; -.
DR   HOVERGEN; HBG018006; -.
DR   InParanoid; P35440; -.
DR   KO; K04659; -.
DR   OrthoDB; 120983at2759; -.
DR   PhylomeDB; P35440; -.
DR   PRO; PR:P35440; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000011200; Expressed in 7 organ(s), highest expression level in heart.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR037349; Thrombospondin.
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; PTHR10199; 2.
DR   PANTHER; PTHR10199:SF10; PTHR10199:SF10; 2.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Heparin-binding; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23   1178       Thrombospondin-2.
FT                                /FTId=PRO_0000035848.
FT   DOMAIN       25    221       Laminin G-like.
FT   DOMAIN      324    381       VWFC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN      387    437       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      443    498       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      500    555       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      555    595       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      654    698       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      699    734       TSP type-3 1.
FT   REPEAT      735    770       TSP type-3 2.
FT   REPEAT      771    793       TSP type-3 3.
FT   REPEAT      794    829       TSP type-3 4.
FT   REPEAT      830    852       TSP type-3 5.
FT   REPEAT      853    890       TSP type-3 6.
FT   REPEAT      891    926       TSP type-3 7.
FT   REPEAT      927    962       TSP type-3 8.
FT   DOMAIN      966   1178       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   REGION        ?    232       Heparin-binding. {ECO:0000255}.
FT   MOTIF       934    936       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    157    157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    244    244       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    317    317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    322    322       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    590    590       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    716    716       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1075   1075       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    272    272       Interchain. {ECO:0000250}.
FT   DISULFID    276    276       Interchain. {ECO:0000250}.
FT   DISULFID    399    431       {ECO:0000250}.
FT   DISULFID    403    436       {ECO:0000250}.
FT   DISULFID    414    421       {ECO:0000250}.
FT   DISULFID    455    492       {ECO:0000250}.
FT   DISULFID    459    497       {ECO:0000250}.
FT   DISULFID    470    482       {ECO:0000250}.
FT   DISULFID    512    549       {ECO:0000250}.
FT   DISULFID    516    554       {ECO:0000250}.
FT   DISULFID    527    539       {ECO:0000250}.
FT   DISULFID    559    570       {ECO:0000250}.
FT   DISULFID    564    580       {ECO:0000250}.
FT   DISULFID    583    594       {ECO:0000250}.
FT   DISULFID    600    616       {ECO:0000250}.
FT   DISULFID    607    625       {ECO:0000250}.
FT   DISULFID    628    652       {ECO:0000250}.
FT   DISULFID    658    671       {ECO:0000250}.
FT   DISULFID    665    684       {ECO:0000250}.
FT   DISULFID    686    697       {ECO:0000250}.
FT   DISULFID    713    721       {ECO:0000250}.
FT   DISULFID    726    746       {ECO:0000250}.
FT   DISULFID    762    782       {ECO:0000250}.
FT   DISULFID    785    805       {ECO:0000250}.
FT   DISULFID    821    841       {ECO:0000250}.
FT   DISULFID    844    864       {ECO:0000250}.
FT   DISULFID    882    902       {ECO:0000250}.
FT   DISULFID    918    938       {ECO:0000250}.
FT   DISULFID    954   1175       {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
//
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