GenomeNet

Database: UniProt
Entry: G3VPY7_SARHA
LinkDB: G3VPY7_SARHA
Original site: G3VPY7_SARHA 
ID   G3VPY7_SARHA            Unreviewed;       302 AA.
AC   G3VPY7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Bone sialoprotein 2 {ECO:0000256|ARBA:ARBA00017177};
DE   AltName: Full=Bone sialoprotein II {ECO:0000256|ARBA:ARBA00033169};
DE   AltName: Full=Cell-binding sialoprotein {ECO:0000256|ARBA:ARBA00032072};
DE   AltName: Full=Integrin-binding sialoprotein {ECO:0000256|ARBA:ARBA00030309};
GN   Name=IBSP {ECO:0000313|Ensembl:ENSSHAP00000005242.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000005242.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000005242.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000005242.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral
CC       part of the mineralized matrix. Probably important to cell-matrix
CC       interaction. Promotes Arg-Gly-Asp-dependent cell attachment.
CC       {ECO:0000256|ARBA:ARBA00025685}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   RefSeq; XP_003773007.1; XM_003772959.1.
DR   AlphaFoldDB; G3VPY7; -.
DR   STRING; 9305.ENSSHAP00000005242; -.
DR   Ensembl; ENSSHAT00000005294.2; ENSSHAP00000005242.2; ENSSHAG00000004585.2.
DR   GeneID; 100924685; -.
DR   KEGG; shr:100924685; -.
DR   CTD; 3381; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   GeneTree; ENSGT00390000002485; -.
DR   HOGENOM; CLU_076119_0_0_1; -.
DR   InParanoid; G3VPY7; -.
DR   TreeFam; TF338678; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0036094; F:small molecule binding; IEA:Ensembl.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR   InterPro; IPR008412; BSP_II.
DR   PANTHER; PTHR10345; BONE SIALOPROTEIN 2; 1.
DR   PANTHER; PTHR10345:SF0; BONE SIALOPROTEIN 2; 1.
DR   Pfam; PF05432; BSP_II; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..302
FT                   /note="Bone sialoprotein 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029736591"
FT   REGION          58..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..95
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  34112 MW;  27E462740A917C8C CRC64;
     MKTALILLSL LGIACAFSVK NLYRRAKLGD SEENGVLNHR HRYYIYKYSY LYPPLKRIPV
     QRNGDSSEEG DGESSEEEEE EEENSNEEEE TESNGSEEST TLSATTLGYG EENTTASGDI
     GLAAIQNPKK EEKNNQVTKK EESDEEEEEE EENEESEAEV DENKEGGNST NHENAEGDHG
     NGNGGKEEGE EEEEVENGTE ATENEASNST EVTTSLNGYE FTTLLKGDFE VTSPPYEEST
     SNLYDSGYEE PVTNEYDNGY EVYENENREP RGDNYRAYED EYSYYKGHAY NGYGGQDYYY
     HQ
//
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