SIAL_MOUSE
ID SIAL_MOUSE Reviewed; 324 AA.
AC Q61711; Q61363; Q80VR6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Bone sialoprotein 2;
DE AltName: Full=Bone sialoprotein II;
DE Short=BSP II;
DE AltName: Full=Cell-binding sialoprotein;
DE AltName: Full=Integrin-binding sialoprotein;
DE Flags: Precursor;
GN Name=Ibsp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8180469; DOI=10.1007/bf00292337;
RA Young M.F., Ibaraki K., Kerr J.M., Lyu M.S., Kozak C.A.;
RT "Murine bone sialoprotein (BSP): cDNA cloning, mRNA expression, and genetic
RT mapping.";
RL Mamm. Genome 5:108-111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RA Wuyts W., Tylzanowski P., Merregaert J.;
RT "Sequence of mouse bone sialoprotein II (BSP) cDNA.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated; glycans consist of sialylated and core-fucosylated
CC bi-, tri- and tetraantennary chains. {ECO:0000250}.
CC -!- PTM: Sulfated on either Tyr-320 or Tyr-321. {ECO:0000250}.
CC -!- MISCELLANEOUS: It is possible that the segments of clustered carboxyl
CC groups mediate the strong binding to hydroxyapatite.
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DR EMBL; L20232; AAA21726.1; -; mRNA.
DR EMBL; L23801; AAA37326.1; -; mRNA.
DR EMBL; AK132371; BAE21132.1; -; mRNA.
DR EMBL; BC045143; AAH45143.1; -; mRNA.
DR EMBL; CH466529; EDL20226.1; -; Genomic_DNA.
DR CCDS; CCDS19485.1; -.
DR PIR; I49768; I49768.
DR RefSeq; NP_032344.2; NM_008318.3.
DR AlphaFoldDB; Q61711; -.
DR IntAct; Q61711; 1.
DR MINT; Q61711; -.
DR STRING; 10090.ENSMUSP00000031246; -.
DR GlyGen; Q61711; 4 sites.
DR PhosphoSitePlus; Q61711; -.
DR PaxDb; Q61711; -.
DR PRIDE; Q61711; -.
DR ProteomicsDB; 261362; -.
DR Antibodypedia; 14494; 390 antibodies from 32 providers.
DR DNASU; 15891; -.
DR Ensembl; ENSMUST00000031246; ENSMUSP00000031246; ENSMUSG00000029306.
DR GeneID; 15891; -.
DR KEGG; mmu:15891; -.
DR UCSC; uc008ykg.2; mouse.
DR CTD; 3381; -.
DR MGI; MGI:96389; Ibsp.
DR VEuPathDB; HostDB:ENSMUSG00000029306; -.
DR eggNOG; KOG1181; Eukaryota.
DR GeneTree; ENSGT00390000002485; -.
DR HOGENOM; CLU_076119_0_0_1; -.
DR InParanoid; Q61711; -.
DR OMA; QDYYYHQ; -.
DR OrthoDB; 1565775at2759; -.
DR TreeFam; TF338678; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 15891; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q61711; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61711; protein.
DR Bgee; ENSMUSG00000029306; Expressed in secondary palatal shelf and 104 other tissues.
DR Genevisible; Q61711; MM.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR InterPro; IPR008412; BSP_II.
DR PANTHER; PTHR10345; PTHR10345; 1.
DR Pfam; PF05432; BSP_II; 1.
PE 2: Evidence at transcript level;
KW Biomineralization; Cell adhesion; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Sialic acid; Signal; Sulfation.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..324
FT /note="Bone sialoprotein 2"
FT /id="PRO_0000020331"
FT REGION 60..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..295
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 70..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q28862"
FT MOD_RES 320
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 321
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="G -> C (in Ref. 2; AAA37326)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="S -> A (in Ref. 1; AAA21726 and 2; AAA37326)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="I -> V (in Ref. 2; AAA37326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35734 MW; D0CD12EA82D27773 CRC64;
MKTALILLSI LGMACAFSMK NFHRRIKAED SEENGVFKYR PRYFLYKHAY FYPPLKRFPV
QGGSDSSEEN GDGDSSEEEG EEEETSNEEE NNEDSEGNED QEAEAENSTL STLSGVTASY
GAETTPQAQT FELAALQLPK KAGDAESRAP KVKESDEEEE EEEEEEENEN EEAEVDENEL
AVNGTSTNST EVDGGNGSSG GDNGEEAEAE EASVTEAGAE GTTGGRELTS VGTQTAVLLN
GFQQTTPPPE AYGTTSPPIR KSSTVEYGGE YEQTGNEYNN EYEVYDNENG EPRGDTYRAY
EDEYSYYKGH GYEGYEGQNY YYHQ
