ID A0A087R3X5_APTFO Unreviewed; 286 AA.
AC A0A087R3X5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=AS27_05723 {ECO:0000313|EMBL:KFM08179.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM08179.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM08179.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM08179.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL226085; KFM08179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R3X5; -.
DR STRING; 9233.A0A087R3X5; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
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; 2.
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:UP000053286};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..286
FT /note="Bone sialoprotein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001828418"
FT REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 31339 MW; 48F73B8DBE2C520C CRC64;
MRTALVFACL VGMACAFSVK SWLQRAKSDD SEENGVFKNR HRYYLYRYAY VHPPQRQYQG
SDSSEEEGDG SEEEGGVSTA NQQPAKQIWE LGNFLWFSGH PAGAAPGDSQ DGLEGDVASP
QQVWEREGEE EEEEEEVVEN ENGVNGTSTN TTEGADGPHG NGTAVVEEGT GAAEEEEEEE
EEEEEEEEEE ETEATTVAST TGEEGLSQAT TTGDGGPTDA TTAGEQWEYE VTAGGRSRGD
EGTTDGSYGE QDEYARGDSY QAYEDEYGYY KGHGYDVYGQ DYYYSQ
//
