SRGN_RAT
ID SRGN_RAT Reviewed; 179 AA.
AC P04917;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Serglycin;
DE AltName: Full=Chondroitin sulfate proteoglycan core protein;
DE AltName: Full=Cytolytic granule proteoglycan core protein;
DE AltName: Full=PG19 core protein;
DE AltName: Full=Proteoglycan 10K core protein;
DE AltName: Full=Secretory granule proteoglycan core protein;
DE Flags: Precursor;
GN Name=Srgn; Synonyms=Pgsg, Prg, Prg1;
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=Yolk sac carcinoma;
RX PubMed=2427521; DOI=10.1016/s0021-9258(18)67120-0;
RA Bourdon M.A., Shiga M., Ruoslahti E.;
RT "Identification from cDNA of the precursor form of a chondroitin sulfate
RT proteoglycan core protein.";
RL J. Biol. Chem. 261:12534-12537(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3366780; DOI=10.1016/s0021-9258(18)68640-5;
RA Avraham S., Stevens R.L., Gartner M.C., Austen K.F., Lalley P.A.,
RA Weis J.H.;
RT "Isolation of a cDNA that encodes the peptide core of the secretory granule
RT proteoglycan of rat basophilic leukemia-1 cells and assessment of its
RT homology to the human analogue.";
RL J. Biol. Chem. 263:7292-7296(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2352541;
RA Giorda R., Chambers W.H., Dahl C.A., Trucco M.;
RT "Isolation and characterization of a cDNA that encodes the core protein of
RT the cytolytic granule proteoglycan in rat natural killer cells.";
RL Nat. Immun. Cell Growth Regul. 9:91-102(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-179, AND PROTEIN SEQUENCE OF 76-94.
RC TISSUE=Yolk sac;
RX PubMed=3919394; DOI=10.1073/pnas.82.5.1321;
RA Bourdon M.A., Oldberg A., Pierschbacher M.D., Ruoslahti E.;
RT "Molecular cloning and sequence analysis of a chondroitin sulfate
RT proteoglycan cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1321-1325(1985).
CC -!- FUNCTION: Plays a role in formation of mast cell secretory granules and
CC mediates storage of various compounds in secretory vesicles. Required
CC for storage of some proteases in both connective tissue and mucosal
CC mast cells and for storage of granzyme B in T-lymphocytes. Plays a role
CC in localizing neutrophil elastase in azurophil granules of neutrophils.
CC Mediates processing of MMP2. Plays a role in cytotoxic cell granule-
CC mediated apoptosis by forming a complex with granzyme B which is
CC delivered to cells by perforin to induce apoptosis. Regulates the
CC secretion of TNF-alpha and may also regulate protease secretion.
CC Inhibits bone mineralization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to activated CD44 and to GZMB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P10124}. Cytolytic granule
CC {ECO:0000250|UniProtKB:P10124}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P10124}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in
CC cytoplasmic granules of cytolytic T-lymphocytes from where it is
CC secreted upon cell activation. Secreted constitutively by endothelial
CC cells and macrophages. Located to Golgi apparatus during neutrophil
CC differentiation (By similarity). {ECO:0000250|UniProtKB:P10124,
CC ECO:0000250|UniProtKB:P13609}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serglycin family. {ECO:0000305}.
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DR EMBL; K02934; AAA42171.1; -; mRNA.
DR EMBL; J03224; AAA41837.1; -; mRNA.
DR EMBL; BC088144; AAH88144.1; -; mRNA.
DR PIR; A25644; GZRT0.
DR RefSeq; NP_064459.1; NM_020074.2.
DR RefSeq; XP_006256545.1; XM_006256483.3.
DR RefSeq; XP_006256546.1; XM_006256484.3.
DR AlphaFoldDB; P04917; -.
DR STRING; 10116.ENSRNOP00000000443; -.
DR GlyGen; P04917; 8 sites.
DR SwissPalm; P04917; -.
DR PaxDb; P04917; -.
DR Ensembl; ENSRNOT00000000443; ENSRNOP00000000443; ENSRNOG00000000394.
DR GeneID; 56782; -.
DR KEGG; rno:56782; -.
DR UCSC; RGD:619969; rat.
DR CTD; 5552; -.
DR RGD; 619969; Srgn.
DR eggNOG; ENOG502S72N; Eukaryota.
DR GeneTree; ENSGT00390000000885; -.
DR HOGENOM; CLU_142594_0_0_1; -.
DR InParanoid; P04917; -.
DR OMA; NAFYYNF; -.
DR OrthoDB; 1340705at2759; -.
DR PhylomeDB; P04917; -.
DR TreeFam; TF336310; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P04917; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000394; Expressed in thymus and 20 other tissues.
DR Genevisible; P04917; RN.
DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0042629; C:mast cell granule; ISS:UniProtKB.
DR GO; GO:0099091; C:postsynaptic specialization, intracellular component; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0005518; F:collagen binding; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISS:UniProtKB.
DR GO; GO:0033382; P:maintenance of granzyme B location in T cell secretory granule; ISS:UniProtKB.
DR GO; GO:0033373; P:maintenance of protease location in mast cell secretory granule; ISS:UniProtKB.
DR GO; GO:0033364; P:mast cell secretory granule organization; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:0033363; P:secretory granule organization; IBA:GO_Central.
DR GO; GO:0033371; P:T cell secretory granule organization; ISS:UniProtKB.
DR InterPro; IPR007455; Serglycin.
DR Pfam; PF04360; Serglycin; 2.
PE 1: Evidence at protein level;
KW Apoptosis; Biomineralization; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Lysosome; Proteoglycan; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..75
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3919394"
FT /id="PRO_0000026681"
FT CHAIN 76..179
FT /note="Serglycin"
FT /id="PRO_0000026682"
FT REPEAT 90..91
FT /note="1"
FT REPEAT 92..93
FT /note="2"
FT REPEAT 94..95
FT /note="3"
FT REPEAT 96..97
FT /note="4"
FT REPEAT 98..99
FT /note="5"
FT REPEAT 100..101
FT /note="6"
FT REPEAT 102..103
FT /note="7"
FT REPEAT 104..105
FT /note="8"
FT REPEAT 106..107
FT /note="9"
FT REPEAT 108..109
FT /note="10"
FT REPEAT 110..111
FT /note="11"
FT REPEAT 112..113
FT /note="12"
FT REPEAT 114..115
FT /note="13"
FT REPEAT 116..117
FT /note="14"
FT REPEAT 118..119
FT /note="15"
FT REPEAT 120..121
FT /note="16"
FT REPEAT 122..123
FT /note="17"
FT REPEAT 124..125
FT /note="18"
FT REPEAT 126..127
FT /note="19"
FT REPEAT 128..129
FT /note="20"
FT REPEAT 130..131
FT /note="21"
FT REPEAT 132..133
FT /note="22"
FT REPEAT 134..135
FT /note="23"
FT REPEAT 136..137
FT /note="24"
FT REGION 86..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..137
FT /note="24 X 2 AA tandem repeats of S-G"
FT COMPBIAS 87..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 39..48
FT /evidence="ECO:0000255"
SQ SEQUENCE 179 AA; 18577 MW; D2E2A8E7D3AAA0D6 CRC64;
MRQVPVGTRL VLALAFVLVW GSSVQGYPAR RARYQWVRCK PDGIFANCIE EKGPRFDLIA
EESNVGPPMT DPVLMRGFPN DFFPISDDYS GSGSGSGSGS GSGSGSGSGS GSGSGSGSGS
GSGSGSGSGS GSGSGSGSLA DMEWEYQPTD ENNIVYFNYG PFDRMLTEQN QEQPGDFII
