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Database: UniProt
Entry: A0A226ND19_CALSU
LinkDB: A0A226ND19_CALSU
Original site: A0A226ND19_CALSU 
ID   A0A226ND19_CALSU        Unreviewed;      1222 AA.
AC   A0A226ND19;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Thrombospondin-2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASZ78_017117 {ECO:0000313|EMBL:OXB65387.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB65387.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB65387.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB65387.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB65387.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXB65387.1}.
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DR   EMBL; MCFN01000095; OXB65387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226ND19; -.
DR   STRING; 9009.A0A226ND19; -.
DR   Proteomes; UP000198323; 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; 1.
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}; Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          369..426
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          699..743
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REPEAT          780..815
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          839..874
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          936..971
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   REPEAT          972..1007
FT                   /note="TSP type-3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00634"
FT   DOMAIN          1011..1222
FT                   /note="TSP C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51236"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..802
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1222 AA;  136353 MW;  18C1DD13E033B2E9 CRC64;
     MCDGGRVPRS APHCRQRSGS RQSPLAPSAL PMPGVMLQRS RLLWLAVLIT LWVSSDAQDD
     VKEEENTFDL LQISNINRKT IGAKLFRGPD PAIPAYRFIR FDHIPPFKPE KLKKIVKLIR
     QNEGFILSAT LRQDRQSRGT ILALEGPGIS ERQFEIISNG RANTLDLIYW MDGFQNVISL
     EDVDLADSQW KNLTVQITGE NYNLYVGCDL IDSFILEEPF YEQLKAENSR MYVAKGSIRE
     NHFRYQDTVS TIERARCGMW ETGKGWKCIG LGTSEVGFDF MATEVNTINE STEILHLSPA
     VTTEYVGEKT EKKAEFCDRS CEELGTMFTE LTGLRIVVNN LADNLQKVSE ENQIMWELIG
     PNKTLKNQSV CWQDGRIFAD SESWIVDSCT KCTCQDSKIV CHQITCPPVS CADPSFIEGE
     CCPVCSHSDD SEEGWSPWSD WTKCSVTCGS GTQMRGRSCD VTRSACTGPH IQTRMCSFKK
     CDHRIRQDGG WSHWSPWSSC SVTCGVGNIT RIRLCNSPIP QMGGKNCVGN GRETEKCEKA
     PCPVNGQWGP WSPWSACTVT CGGGIRERSR LCNSPEPQYG GKSCVGDTKQ HDMCNKKDCP
     IDGCLSNPCF PGAECNSYPD GSWSCGPCPA GFLGNGTVCE DLDECIAVSD VCFKVNQVHR
     CVNTNPGFHC LPCPPRYKGS QPYGVGLEVA KTEKQVCEPE NPCKDKTHSC HKSAECIYLG
     HFSDPMYKCE CRTGYAGDGR ICGEDSDLDG WPNNNLVCAA NATYHCVKDN CPLLPNSGQE
     DFDKDGKGDA CDEDDDNDGV EDDKDNCPLL FNPRQFDYDK DEVGDRCDNC PYVHNPAQID
     TDNNGEGDSC AVDIDGDDIF NERDNCPYVY NTDQSDTDGD GVGDQCDNCP LMHNPDQTDA
     DNDLVGDQCD NNEDIDEDGH QNNQDNCPYI PNANQADHDK DGKGDACDPD DDNDGVPDDR
     DNCRLRYNPE QEDSDGDGRG DICKDDFDDD SVPDIYDVCP ENNAISETDF RKFQMVPLDP
     KGTAQIDPNW VIRHQGKELV QTANSDPGIA VGYDEFSSVD FSGTFYVNTD RDDDYAGFVF
     GYQSSSRFYV LMWKQVTQTY WEDKPTRAYG YSGVSLKVVN STTGTGEHLR NALWHTGNTP
     GQVRTLWHDP KNIGWKDYTA YRWHLIHRPK TGLIKVLVYE GKQVMVDSGP IYDTTFAGGR
     LGLFVFSQEM VYFSDLKYEC RG
//
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