GRPA_RAT
ID GRPA_RAT Reviewed; 246 AA.
AC P08568;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Submandibular gland secretory Glx-rich protein CA;
DE Short=GRP-CA;
DE Flags: Precursor;
GN Name=Grpca;
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 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-246.
RX PubMed=2438276; DOI=10.1016/s0021-9258(18)48235-x;
RA Mirels L., Bedi G.S., Dickinson D.P., Gross K.W., Tabak L.A.;
RT "Molecular characterization of glutamic acid/glutamine-rich secretory
RT proteins from rat submandibular glands.";
RL J. Biol. Chem. 262:7289-7297(1987).
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; M58653; AAA41278.1; -; mRNA.
DR EMBL; J02730; AAA41276.1; -; mRNA.
DR PIR; A29573; A29573.
DR PIR; A38647; A38647.
DR AlphaFoldDB; P08568; -.
DR SMR; P08568; -.
DR RGD; 619775; Grpca.
DR PhylomeDB; P08568; -.
DR PRO; PR:P08568; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:RGD.
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..246
FT /note="Submandibular gland secretory Glx-rich protein CA"
FT /id="PRO_0000013038"
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..223
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"
FT CONFLICT 63
FT /note="A -> P (in Ref. 2; AAA41276)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Q -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="E -> D (in Ref. 2; AAA41276)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> P (in Ref. 2; AAA41276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26528 MW; 1C7144CFE67375AA CRC64;
MLVVLLTAAL LALSSAQGTD EEVNNAETSD VPADSEQQPV DSGSDPPSAD ADAENVQEGE
SAAPANEEPP ATSGSEEEQQ QQEPTQAENQ EPPATSGSEE EQQQQEPTQA ENQEPPATSG
SEEEQQQQEP TQAEDQQPPA TSGSEEEQQQ QESTQAENQE PSDSAGEGQE TQPEEGNVES
PPSSPENSQE QPQQTNPEEK PPAPKTQEEP QHDSGRPKKP LLPFIANLIR ERIRKLLARS
PLGRRF