OSTK_BOVIN
ID OSTK_BOVIN Reviewed; 277 AA.
AC P31098;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Osteopontin-K;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1414488; DOI=10.1002/jbmr.5650070614;
RA Crivello J.F., Delvin E.;
RT "Isolation and characterization of a cDNA for osteopontin-k: a kidney cell
RT adhesion molecule with high homology to osteopontins.";
RL J. Bone Miner. Res. 7:693-699(1992).
CC -!- FUNCTION: Probably involved in cell adhesion.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Kidney, liver and heart. Weak in bone.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
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DR EMBL; S45840; AAB23593.2; -; mRNA.
DR AlphaFoldDB; P31098; -.
DR PeptideAtlas; P31098; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
DR InterPro; IPR002038; Osteopontin.
DR InterPro; IPR019841; Osteopontin_CS.
DR PANTHER; PTHR10607; PTHR10607; 2.
DR Pfam; PF00865; Osteopontin; 2.
DR PRINTS; PR00216; OSTEOPONTIN.
DR SMART; SM00017; OSTEO; 1.
DR PROSITE; PS00884; OSTEOPONTIN; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Glycoprotein; Phosphoprotein; Reference proteome; Secreted;
KW Sialic acid; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..277
FT /note="Osteopontin-K"
FT /id="PRO_0000020328"
FT REGION 38..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..154
FT /note="Cell attachment site"
FT COMPBIAS 46..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 277 AA; 30969 MW; 0943B831CDC18DF2 CRC64;
MRIAVICFCL LGIASALPVK PTSSGSSEEK QLNNKYPDAV ATWLKPDPSQ KQTFLAPQNS
VSSEETDDNK QNTLPSKSNE DPEQTDDLDD DDDNSQDVNS NDSDDAETTD DPDHSDESHH
SDESHQVHFP TDIPTIAVFT PFIPTESAND GRGDRCGLRT EVKIIEVPPI NVQSPDATEE
DFTSHIESER CMSTKKTSRL TDHSKETNRC ELSKELMPKA KDKNKHSNLI ESQENSKLSQ
EFHSLEDKLD LDHKSEEDKH LKIRISHELD SASSEVN
