SMR1_RAT
ID SMR1_RAT Reviewed; 146 AA.
AC P13432;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=SMR1 protein;
DE AltName: Full=VCS-alpha 1;
DE Contains:
DE RecName: Full=SMR1-related undecapeptide;
DE Contains:
DE RecName: Full=SMR1-related hexapeptide;
DE Contains:
DE RecName: Full=Sialorphin;
DE AltName: Full=SMR1-related pentapeptide;
DE Contains:
DE RecName: Full=Submandibular gland peptide T;
DE Short=SGP-T;
DE Flags: Precursor;
GN Name=Vcsa1; Synonyms=Smr1;
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=Submandibular gland;
RX PubMed=3186744; DOI=10.1073/pnas.85.22.8553;
RA Rosinski-Chupin I., Tronik D., Rougeon F.;
RT "High level of accumulation of a mRNA coding for a precursor-like protein
RT in the submaxillary gland of male rats.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8553-8557(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-114.
RC STRAIN=Wistar;
RX PubMed=2125424; DOI=10.1089/dna.1990.9.553;
RA Rosinski-Chupin I., Rougeon F.;
RT "The gene encoding SMR1, a precursor-like polypeptide of the male rat
RT submaxillary gland, has the same organization as the preprothyrotropin-
RT releasing hormone gene.";
RL DNA Cell Biol. 9:553-559(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-114.
RC STRAIN=Wistar;
RX PubMed=7557446; DOI=10.1016/0378-1119(95)00318-z;
RA Courty Y., Rosinski-Chupin I., Rougeon F.;
RT "Various transcripts are generated from the VCSA1 gene by alternative
RT splicing and poly(A) processing in the rat submandibular gland.";
RL Gene 162:291-296(1995).
RN [4]
RP PROTEIN SEQUENCE OF 23-33, AND SUBCELLULAR LOCATION.
RC TISSUE=Submandibular gland;
RX PubMed=8112327; DOI=10.1111/j.1432-1033.1994.tb18556.x;
RA Rougeot C., Rosinski-Chupin I., Njamkepo E., Rougeon F.;
RT "Selective processing of submandibular rat 1 protein at dibasic cleavage
RT sites. Salivary and bloodstream secretion products.";
RL Eur. J. Biochem. 219:765-773(1994).
RN [5]
RP PROTEIN SEQUENCE OF 138-144, AND FUNCTION.
RC TISSUE=Submandibular gland;
RX PubMed=9321881; DOI=10.1152/ajpregu.1997.273.3.r1017;
RA Mathison R.D., Befus A.D., Davison J.S.;
RT "A novel submandibular gland peptide protects against endotoxic and
RT anaphylactic shock.";
RL Am. J. Physiol. 273:R1017-R1023(1997).
RN [6]
RP FUNCTION.
RX PubMed=9362294; DOI=10.1152/ajpregu.1997.273.4.r1309;
RA Rougeot C., Vienet R., Cardona A., Le Doledec L., Grognet J.M., Rougeon F.;
RT "Targets for SMR1-pentapeptide suggest a link between the circulating
RT peptide and mineral transport.";
RL Am. J. Physiol. 273:R1309-R1320(1997).
RN [7]
RP FUNCTION OF SIALORPHIN.
RX PubMed=12835417; DOI=10.1073/pnas.1431850100;
RA Rougeot C., Messaoudi M., Hermitte V., Rigault A.G., Blisnick T.,
RA Dugave C., Desor D., Rougeon F.;
RT "Sialorphin, a natural inhibitor of rat membrane-bound neutral
RT endopeptidase that displays analgesic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8549-8554(2003).
CC -!- FUNCTION: Sialorphin may be involved in the modulation of mineral
CC balance between at least four systems: kidney, bone, tooth and
CC circulation.
CC -!- FUNCTION: Submandibular gland peptide T is able to directly or
CC indirectly down-regulate cardiovascular depression induced by septic
CC shock (endotoxin stimuli), or anaphylactic challenge (nematode antigen
CC sensitization).
CC -!- FUNCTION: Sialorphin is an endogenous inhibitor of neprilysin. Inhibits
CC the breakdown of Met-enkephalin and substance P in isolated tissue from
CC the dorsal zone of the rat spinal cord. Has an analgesic effect when
CC administered to rats by intravenous injection.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8112327}. Note=Found
CC in blood. Secreted from the salivary compartment into the blood
CC circulation, rather than through absorption by the gastro-intestinal
CC tract.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the acinar cells of the
CC submandibular gland and to lesser extent in the prostate.
CC -!- INDUCTION: By androgens; strongly.
CC -!- PTM: Several O-linked glycosylation sites might be present in the C-
CC terminal part.
CC -!- MISCELLANEOUS: SMR1 mRNA is about 1000 times more abundant in the
CC submandibular gland of male than female.
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DR EMBL; M63112; AAA42153.1; -; mRNA.
DR EMBL; M59467; AAA42154.1; -; Genomic_DNA.
DR EMBL; X84997; CAA59355.1; -; Genomic_DNA.
DR EMBL; X52467; CAA36705.1; -; Genomic_DNA.
DR PIR; A36302; A36302.
DR RefSeq; NP_036816.4; NM_012684.4.
DR AlphaFoldDB; P13432; -.
DR STRING; 10116.ENSRNOP00000035658; -.
DR GlyGen; P13432; 2 sites.
DR PaxDb; P13432; -.
DR GeneID; 24867; -.
DR KEGG; rno:24867; -.
DR UCSC; RGD:3953; rat.
DR CTD; 10879; -.
DR RGD; 3953; Vcsa1.
DR InParanoid; P13432; -.
DR OrthoDB; 1650758at2759; -.
DR PhylomeDB; P13432; -.
DR PRO; PR:P13432; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR InterPro; IPR026288; SMR-like.
DR PANTHER; PTHR14179; PTHR14179; 1.
DR Pfam; PF15621; PROL5-SMR; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8112327"
FT CHAIN 23..146
FT /note="SMR1 protein"
FT /id="PRO_0000022369"
FT PEPTIDE 23..33
FT /note="SMR1-related undecapeptide"
FT /id="PRO_0000022370"
FT PEPTIDE 28..33
FT /note="SMR1-related hexapeptide"
FT /id="PRO_0000022371"
FT PEPTIDE 29..33
FT /note="Sialorphin"
FT /id="PRO_0000022372"
FT PEPTIDE 138..144
FT /note="Submandibular gland peptide T"
FT /id="PRO_0000022373"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 114
FT /note="H -> L"
FT /evidence="ECO:0000269|PubMed:2125424,
FT ECO:0000269|PubMed:7557446"
SQ SEQUENCE 146 AA; 15970 MW; F31B619A3BD85B5C CRC64;
MKSLYLIFGL WILLACFQSG EGVRGPRRQH NPRRQQDPST LPHYLGLQPD PNGGQIGVTI
TIPLNLQPPR VLVNLPGFIT GPPLVVQGTT EYQYQWQLTA PDPTPLSNPP TQLHSTEQAN
TKTDAKISNT TATTQNSTDI FEGGGK
