PRP_PIG
ID PRP_PIG Reviewed; 676 AA.
AC Q95JC9; P84505; P84506; Q95JD0; Q95JD1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Basic proline-rich protein;
DE Contains:
DE RecName: Full=Proline-rich peptide SP-B-like;
DE Short=PRP-SP-B-like;
DE Contains:
DE RecName: Full=Proline-rich peptide SP-A;
DE Short=PRP-SP-A;
DE Contains:
DE RecName: Full=Proline-rich peptide SP-B;
DE Short=PRP-SP-B;
DE Contains:
DE RecName: Full=Parotid hormone;
DE AltName: Full=PH-Ab;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK61383.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF
RP 647-676 (ISOFORMS 1/3), AND TISSUE SPECIFICITY.
RC STRAIN=Yorkshire {ECO:0000312|EMBL:AAK61383.1};
RC TISSUE=Parotid gland {ECO:0000312|EMBL:AAK61383.1};
RX PubMed=15805110; DOI=10.1074/jbc.m501366200;
RA Zhang Q., Szalay A.A., Tieche J.-M., Kyeyune-Nyombi E., Sands J.F.,
RA Oberg K.C., Leonora J.;
RT "Cloning and functional study of porcine parotid hormone, a novel proline-
RT rich protein.";
RL J. Biol. Chem. 280:22233-22244(2005).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE (ISOFORMS 1/2/3), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-28 AND SER-30.
RC STRAIN=Landrace {ECO:0000269|PubMed:16112392};
RC TISSUE=Saliva {ECO:0000269|PubMed:16112392};
RX PubMed=16112392; DOI=10.1016/j.peptides.2005.02.021;
RA Patamia M., Messana I., Petruzzelli R., Vitali A., Inzitari R., Cabras T.,
RA Fanali C., Scarano E., Contucci A., Galtieri A., Castagnola M.;
RT "Two proline-rich peptides from pig (Sus scrofa) salivary glands generated
RT by pre-secretory pathway underlying the action of a proteinase cleaving
RT Pro-Ala bonds.";
RL Peptides 26:1550-1559(2005).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 647-672 (ISOFORMS 1/3), AND FUNCTION.
RC TISSUE=Parotid gland {ECO:0000269|PubMed:7371600};
RX PubMed=7371600; DOI=10.1210/endo-106-6-1994;
RA Tieche J.-M., Leonora J., Steinman R.R.;
RT "Isolation and partial characterization of a porcine parotid hormone that
RT stimulates dentinal fluid transport.";
RL Endocrinology 106:1994-2005(1980).
CC -!- FUNCTION: The parotid hormone stimulates dentinal fluid transport in
CC teeth. {ECO:0000269|PubMed:7371600}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16112392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15805110};
CC IsoId=Q95JC9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15805110};
CC IsoId=Q95JC9-2; Sequence=VSP_052037, VSP_052038, VSP_052040,
CC VSP_052041;
CC Name=3 {ECO:0000269|PubMed:15805110};
CC IsoId=Q95JC9-3; Sequence=VSP_052037, VSP_052038, VSP_052039;
CC -!- TISSUE SPECIFICITY: Acinar cells and secretory granules of the parotid
CC gland. {ECO:0000269|PubMed:15805110, ECO:0000269|PubMed:16112392}.
CC -!- MASS SPECTROMETRY: [Proline-rich peptide SP-A]: Mass=6156.0;
CC Mass_error=0.8; Method=Electrospray; Note=Proline-rich peptide SP-A.;
CC Evidence={ECO:0000269|PubMed:16112392};
CC -!- MASS SPECTROMETRY: [Proline-rich peptide SP-B]: Mass=1904.0;
CC Mass_error=0.4; Method=Electrospray; Note=Proline-rich peptide SP-B.;
CC Evidence={ECO:0000269|PubMed:16112392};
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DR EMBL; AY035847; AAK61381.1; -; mRNA.
DR EMBL; AY035848; AAK61382.1; -; mRNA.
DR EMBL; AY035849; AAK61383.1; -; mRNA.
DR RefSeq; NP_001092050.1; NM_001098580.1.
DR RefSeq; NP_001094495.1; NM_001101025.1.
DR AlphaFoldDB; Q95JC9; -.
DR iPTMnet; Q95JC9; -.
DR PaxDb; Q95JC9; -.
DR PeptideAtlas; Q95JC9; -.
DR GeneID; 100049648; -.
DR GeneID; 100113399; -.
DR KEGG; ssc:100049648; -.
DR KEGG; ssc:100113399; -.
DR CTD; 100049648; -.
DR CTD; 100113399; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Hormone; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:16112392"
FT PEPTIDE 17..72
FT /note="Proline-rich peptide SP-A"
FT /id="PRO_0000235856"
FT PEPTIDE 73..93
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235857"
FT PEPTIDE 94..114
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235858"
FT PEPTIDE 115..135
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235859"
FT PEPTIDE 136..156
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235860"
FT PEPTIDE 157..177
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235861"
FT PEPTIDE 178..198
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235862"
FT PEPTIDE 199..219
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235863"
FT PEPTIDE 220..240
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235864"
FT PEPTIDE 241..261
FT /note="Proline-rich peptide SP-B-like"
FT /id="PRO_0000235865"
FT PEPTIDE 262..282
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235866"
FT PEPTIDE 283..303
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235867"
FT PEPTIDE 304..324
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235868"
FT PEPTIDE 325..345
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235869"
FT PEPTIDE 346..366
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235870"
FT PEPTIDE 367..387
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235871"
FT PEPTIDE 388..408
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235872"
FT PROPEP 409..457
FT /evidence="ECO:0000269|PubMed:16112392"
FT /id="PRO_0000235873"
FT PEPTIDE 458..478
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235874"
FT PEPTIDE 479..499
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235875"
FT PEPTIDE 500..520
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235876"
FT PEPTIDE 521..541
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235877"
FT PEPTIDE 542..562
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235878"
FT PEPTIDE 563..583
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235879"
FT PEPTIDE 584..604
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235880"
FT PEPTIDE 605..625
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235881"
FT PEPTIDE 626..646
FT /note="Proline-rich peptide SP-B"
FT /id="PRO_0000235882"
FT PEPTIDE 647..676
FT /note="Parotid hormone"
FT /evidence="ECO:0000269|PubMed:15805110,
FT ECO:0000269|PubMed:7371600"
FT /id="PRO_0000235883"
FT REGION 29..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16112392"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16112392"
FT VAR_SEQ 150..292
FT /note="GPPPPGPAPPGARPPPGPPPPGPPPPGPAPPGARPPPGPPPPGPPPPGPAPP
FT GARPPPGPPPPGPPPPGPAPPGARPPPGPPPPGPPPPGPAPPGARPPPGPPPLGPPPPG
FT PAPPGARPPPGPPPPGPPPPGPAPPGARPPPG -> AGGLQQGPAPSHVGPKKKPPPPG
FT AGHPPRPPPPANESQPGPRPPPGPPSPPANDSQEGSPPSADGPQQGPAPSGDKPKKKPP
FT PPAGPPPPP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15805110"
FT /id="VSP_052037"
FT VAR_SEQ 418..466
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15805110"
FT /id="VSP_052038"
FT VAR_SEQ 556..612
FT /note="GPPPPGPAPPGARPPPGPPPPGPPPPGPAPPGARPPPGPPPPGPPPPGPAPP
FT GARPP -> ADEPQQGPAPSGDKPKKKPPPPAGPPPPPPPPPGIQGQKMSAKTPVLRRA
FT VTLECDG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15805110"
FT /id="VSP_052040"
FT VAR_SEQ 556..593
FT /note="GPPPPGPAPPGARPPPGPPPPGPPPPGPAPPGARPPPG -> ADEPQQGPAP
FT SGDKPKKKPPPPAGPPPPP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15805110"
FT /id="VSP_052039"
FT VAR_SEQ 613..676
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15805110"
FT /id="VSP_052041"
FT CONFLICT 30
FT /note="S -> A (in Ref. 1; AAK61383)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="R -> E (in Ref. 1; AAK61383)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> D (in Ref. 1; AAK61383)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="P -> H (in Ref. 1; AAK61381/AAK61382)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="P -> L (in Ref. 1; AAK61381/AAK61382)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="G -> P (in Ref. 1; AAK61381/AAK61382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 62283 MW; B127F6AA83D0FBDE CRC64;
MLPILLSVAL LALSSARSPF FDLEDANSNS AEKFLRPPPG GGPPRPPPPE ESQGEGHQKR
PRPPGDGPEQ GPAPPGARPP PGPPPPGPPP PGPAPPGARP PPGPPPPGPP PPGPAPPGAR
PPPGPPPPGP PPPGPAPPGA RPPPGPPPPG PPPPGPAPPG ARPPPGPPPP GPPPPGPAPP
GARPPPGPPP PGPPPPGPAP PGARPPPGPP PPGPPPPGPA PPGARPPPGP PPPGPPPPGP
APPGARPPPG PPPLGPPPPG PAPPGARPPP GPPPPGPPPP GPAPPGARPP PGPPPPGPPP
PGPAPPGARP PPGPPPPGPP PPGPAPPGAR PPPGPPPPGP PPPGPAPPGA RPPPGPPPPG
PPPPGPAPPG ARPPPGPPPP GPPPPGPAPP GARPPPGPPP PGPPPPGPAP PGARPPPPPP
PPADEPQQGP APSGDKPKKK PPPPAGPPPP GPPSPGPAPP GARPPPGPPP PGPPPPGPAP
PGARPPPGPP PPGPPPPGPA PPGARPPPGP PPPGPPPPGP APPGARPPPG PPPPGPPPPG
PAPPGARPPP GPPPPGPPPP GPAPPGARPP PGPPPPGPPP PGPAPPGARP PPGPPPPGPP
PPGPAPPGAR PPPGPPPPGP PPPGPAPPGA RPPPGPPPPG PPPPGPAPPG ARPPPGPPPP
PPGPSPPRPP PGPPPQ
