ROB1_RAT
ID ROB1_RAT Reviewed; 240 AA.
AC O55006;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein RoBo-1;
DE AltName: Full=Rodent bone protein;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC STRAIN=CD Charles River; TISSUE=Tibial bone;
RX PubMed=9461570; DOI=10.1074/jbc.273.7.3878;
RA Noel L.S., Champion B.R., Holley C.L., Simmons C.J., Morris D.C.,
RA Payne J.A., Lean J.M., Chambers T.J., Zaman G., Lanyon L.E., Suva L.J.,
RA Miller L.R.;
RT "RoBo-1, a novel member of the urokinase plasminogen activator
RT receptor/CD59/Ly-6/snake toxin family selectively expressed in rat bone and
RT growth plate cartilage.";
RL J. Biol. Chem. 273:3878-3883(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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.
CC -!- FUNCTION: May play a novel role in the growth or remodeling of bone.
CC {ECO:0000269|PubMed:9461570}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in bone, including the
CC lengthening growth plate where cartilage is remodeled into bone.
CC {ECO:0000269|PubMed:9461570}.
CC -!- INDUCTION: Up-regulated by estradiol. {ECO:0000269|PubMed:9461570}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9461570}.
CC -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR EMBL; AF041083; AAC40033.1; -; mRNA.
DR EMBL; CH473948; EDM04544.1; -; Genomic_DNA.
DR RefSeq; NP_113725.1; NM_031537.1.
DR RefSeq; XP_006246439.1; XM_006246377.3.
DR AlphaFoldDB; O55006; -.
DR SMR; O55006; -.
DR GlyGen; O55006; 2 sites.
DR PaxDb; O55006; -.
DR PRIDE; O55006; -.
DR Ensembl; ENSRNOT00000003797; ENSRNOP00000003797; ENSRNOG00000002820.
DR GeneID; 24906; -.
DR KEGG; rno:24906; -.
DR RGD; 3683; LOC24906.
DR eggNOG; ENOG502SDSC; Eukaryota.
DR GeneTree; ENSGT00730000111648; -.
DR InParanoid; O55006; -.
DR OMA; PNGVECP; -.
DR OrthoDB; 1485195at2759; -.
DR PhylomeDB; O55006; -.
DR TreeFam; TF339495; -.
DR PRO; PR:O55006; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000002820; Expressed in spleen and 16 other tissues.
DR ExpressionAtlas; O55006; baseline and differential.
DR Genevisible; O55006; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046849; P:bone remodeling; IEP:UniProtKB.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..240
FT /note="Protein RoBo-1"
FT /id="PRO_0000402834"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..76
FT /evidence="ECO:0000250"
FT DISULFID 81..102
FT /evidence="ECO:0000250"
FT DISULFID 103..108
FT /evidence="ECO:0000250"
FT DISULFID 127..151
FT /evidence="ECO:0000250"
FT DISULFID 144..171
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 26187 MW; 72D746C0284ACAFB CRC64;
MSWFLVLKCL LTVCIISHLS VSSTESYGCI RKTCFGGRCL HNTTRSCEFS KGCFSQLQEF
AVPLLLLNRR VEQRGCSEDN CTELAFSATL GIDWMFSYNH QCCYSEQCNN KPINVSPLSL
QPNGVECPTC YSELGTCRPV SLKCTGAQTT CVNVTGQGIR EDFIKIHAMG CATQTACNLK
NVIILNNIKI DTSCVSGSPP LRYSPSLSTD QKTSSATAPT LCLLAAVLPA IMVMESFSEL