ID G1LEN2_AILME Unreviewed; 1124 AA.
AC G1LEN2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Thrombospondin 2 {ECO:0000313|Ensembl:ENSAMEP00000005369.2};
GN Name=THBS2 {ECO:0000313|Ensembl:ENSAMEP00000005369.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000005369.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000005369.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000005369.2}
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 AlphaFoldDB; G1LEN2; -.
DR STRING; 9646.ENSAMEP00000005369; -.
DR Ensembl; ENSAMET00000005591.2; ENSAMEP00000005369.2; ENSAMEG00000004995.2.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 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:SF10; THROMBOSPONDIN-2; 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 3: Inferred from homology;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
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..1124
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030170767"
FT DOMAIN 318..375
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 549..589
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 648..692
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 729..764
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 788..823
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 885..920
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT REPEAT 921..956
FT /note="TSP type-3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT DOMAIN 960..1124
FT /note="TSP C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51236"
FT REGION 726..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 124135 MW; 58A5A1A5F7A05923 CRC64;
MFWALMLLAL WASSGARAGG QDEDTAFDLF SISNINRKTI GAKQFRGPDP SVPAYRFVRF
DYIPPVNADY LSKIAKTVRQ REGFFLTASL KQDPKSRGTL LALEGPGASQ RQFEIVSNGP
ADTLDLTYWI DGTQHVISLE DVGLADSQWK NVTVQVTGDT YSLYVGCDLI DSFTLDEPFY
EQLRTEKSRM YVAKGSARES HFRGLLQNVY LVFENSVEDV LSKKGCQQSQ GAEANAISET
TETLHLSPQV APEYAGPGAP RRPEVCERSC EELGTMITEL SGLHVMVNQL HENLRKVSND
NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTK CTCKKFKTVC HQITCPPATC
ANPSFVEGEC CPSCFHSLDG EEGWSPWAEW TQCSVTCGSG TQQRGRSCDV TSNTCLGPSI
QTRVCSLGKC DNRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCRGSG
RETKGCQGVP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQHGG KDCVGDVQEQ
QMCNKRSCPI DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECAVVTDV
CFTTSKAHRC VNTNPGFHCL PCPPRYKGTQ PFGVGLEAAR TEKQVCEPEN PCKDKTHACH
KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNKNLVCATN ATYHCIQDNC
PLLPNSGQED FDKDGTGDAC DDDDDNDGVD DEKDNCQLLF NPRQFDYDKD EVGDRCDNCP
YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL
VHNPDQTDVD NDLVGDQCDN NEDIDEDGHQ NNQDNCPYIS NANQADHDHD GQGDACDSDD
DNDGVPDDRD NCRLVSNPGQ EDSDGDGRGD ACKDDFDNDS IPDIDDVCPE NSAISETDFR
NFQMVHLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR
DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN
ALWHTGNTEG QVRTLWHDPK NIGWKDYTAY RWHLTHRPKS GYIS
//
