GRPB_RAT
ID GRPB_RAT Reviewed; 247 AA.
AC P08462;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Submandibular gland secretory Glx-rich protein CB;
DE Short=GRP-CB;
DE AltName: Full=Contiguous repeat polypeptide;
DE Short=CRP;
DE Flags: Precursor;
GN Name=Grpcb;
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].
RC TISSUE=Liver;
RX PubMed=3558393; DOI=10.1016/s0021-9258(18)61183-4;
RA Heinrich G., Habener J.F.;
RT "Genes encoding proteins with homologous contiguous repeat sequences are
RT highly expressed in the serous cells of the rat submandibular gland.";
RL J. Biol. Chem. 262:5262-5270(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=1995617; DOI=10.1016/s0021-9258(19)67828-2;
RA Cooper L.F., Elia D.M., Tabak L.A.;
RT "Secretagogue-coupled changes in the expression of glutamine/glutamic acid-
RT rich proteins (GRPs). Isoproterenol induces changes in GRP transcript
RT expression and changes in isoforms secreted.";
RL J. Biol. Chem. 266:3532-3539(1991).
CC -!- FUNCTION: GRP proteins have a marked affinity for hydroxyapatite. They
CC may play a role in the formation of the protective acquired pellicle at
CC the saliva-tooth interface.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Submandibular gland acinar cells.
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DR EMBL; M31032; AAA40969.1; -; mRNA.
DR EMBL; M58654; AAA41279.1; ALT_SEQ; mRNA.
DR PIR; A29545; A29545.
DR PIR; B38647; B38647.
DR RefSeq; NP_852105.1; NM_181440.1.
DR RefSeq; NP_976077.1; NM_203332.1.
DR AlphaFoldDB; P08462; -.
DR STRING; 10116.ENSRNOP00000007659; -.
DR PRIDE; P08462; -.
DR GeneID; 192266; -.
DR GeneID; 360395; -.
DR KEGG; rno:360395; -.
DR UCSC; RGD:735181; rat.
DR CTD; 11272; -.
DR CTD; 5554; -.
DR RGD; 735181; Grpcb.
DR OrthoDB; 327524at32523; -.
DR PRO; PR:P08462; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR InterPro; IPR026086; Pro-rich.
DR PANTHER; PTHR23203; PTHR23203; 4.
DR Pfam; PF15240; Pro-rich; 1.
DR SMART; SM01412; Pro-rich; 1.
PE 2: Evidence at transcript level;
KW Biomineralization; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..247
FT /note="Submandibular gland secretory Glx-rich protein CB"
FT /id="PRO_0000013037"
FT REPEAT 67..89
FT /note="1"
FT REPEAT 90..112
FT /note="2"
FT REPEAT 113..135
FT /note="3"
FT REPEAT 136..158
FT /note="4"
FT REPEAT 159..181
FT /note="5"
FT REGION 14..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..181
FT /note="5 X 23 AA tandem repeats"
FT COMPBIAS 14..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 247 AA; 26948 MW; 72A5075BCCC314E4 CRC64;
MLVVLLTAAL LALSSAQGTD EEVNNAETSD VPADSEQQPV DSGSDPPSAD ADAENVQEGE
SAPPANEEPP ATSGSEEEQQ QQEPTQAENQ EPPATSGSEE EQQQQEPTQA ENQEPPATSG
SEEEQQQQQP TQAENQEPPA TSGSEEEQQQ QESTQAENQE PSDSAGEGQE TQPEEGNVES
PPSSPENSQE QPQQTNPEEK PPAPKTQEEP QHYRGRPPKK IFPFFIYRGR PVVVFRLEPR
NPFARRF