ID G3HB88_CRIGR Unreviewed; 353 AA.
AC G3HB88;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=SCO-spondin {ECO:0000313|EMBL:EGV91806.1};
GN ORFNames=I79_007709 {ECO:0000313|EMBL:EGV91806.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV91806.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; JH000263; EGV91806.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HB88; -.
DR STRING; 10029.G3HB88; -.
DR InParanoid; G3HB88; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd19941; TIL; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR22906:SF21; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22906; PROPERDIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT DOMAIN 1..43
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 53..65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 60..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 72..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 142..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 353 AA; 38219 MW; 636F60D905CC3C99 CRC64;
MAPEVWTFNQ MVQARYVRVW PHSGRHSDNI QHNIFLWVEL LGCKPVSPRT PACPENRHHC
ASGECVPKGG PCDGAVDCRD GSDDEACRPL RAGTTSRAKS SGIPEAETPL SSDYPKRAVE
SRDTGHQLSC GSGECLPREQ RCDLQLNCQD GSDEDNCVDC VLAPWSVWSD CSHSCGLGLI
FQRRELLRPP LPGGSCLLDQ LRSQPCFMQA CPVAGAWAEW GPWEPCSVSC GGGHQSRQRS
CVDPPPKNGG APCPGPSHER APCSLQLCPG DTGLVHVNSE LCQKGLVPPC PPSCLDPEAN
RSCNGQCMEG CRCPPGLFLQ DSRCMPLSEC PCLVGQDLRQ PGLAFLLDNC SEW
//
