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Protein

Serglycin

Gene

Srgn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization.7 Publications

GO - Biological processi

  • biomineral tissue development Source: UniProtKB-KW
  • granzyme-mediated apoptotic signaling pathway Source: UniProtKB
  • maintenance of granzyme B location in T cell secretory granule Source: UniProtKB
  • maintenance of protease location in mast cell secretory granule Source: UniProtKB
  • mast cell secretory granule organization Source: UniProtKB
  • negative regulation of bone mineralization Source: UniProtKB
  • negative regulation of cytokine secretion Source: UniProtKB
  • protein processing Source: UniProtKB
  • T cell secretory granule organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Biomineralization

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serglycin
Alternative name(s):
Mastocytoma proteoglycan core protein
Secretory granule proteoglycan core protein
gp600
Gene namesi
Name:Srgn
Synonyms:Prg, Prg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97756. Srgn.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: Ensembl
  • mast cell granule Source: UniProtKB
  • zymogen granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice develop normally and are fertile but display mast cell granule and T-lymphocyte secretory granule defects. Granules are more amorphous than in the wild-type and show a less defined dense core formation. There is a lack of mast cell-specific protease activity although mRNAs for a variety of proteases are detected and storage of granzyme B is affected in T-lymphocytes. Neutrophil granules display a lack of neutrophil elastase and processing of MMP2 is abrogated. Macrophages show no major morphological defects.5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Propeptidei26 – 7449Activation peptideBy similarityPRO_0000290036Add
BLAST
Chaini75 – 15278SerglycinPRO_0000026680Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi38 ↔ 47Sequence analysis
Glycosylationi92 – 921O-linked (Xyl...) (glycosaminoglycan)By similarity
Glycosylationi94 – 941O-linked (Xyl...) (glycosaminoglycan)By similarity
Glycosylationi98 – 981O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi100 – 1001O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi102 – 1021O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi104 – 1041O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi106 – 1061O-linked (Xyl...) (glycosaminoglycan)Sequence analysis
Glycosylationi108 – 1081O-linked (Xyl...) (glycosaminoglycan)Sequence analysis

Post-translational modificationi

O-glycosylated; contains chondroitin sulfate and heparan sulfate.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

EPDiP13609.
MaxQBiP13609.
PaxDbiP13609.
PRIDEiP13609.

Expressioni

Inductioni

By phorbol myristate acetate in T-lymphocytes. This induction is not inhibited by cyclosporine.1 Publication

Gene expression databases

BgeeiP13609.
CleanExiMM_SRGN.
ExpressionAtlasiP13609. baseline and differential.
GenevisibleiP13609. MM.

Interactioni

Subunit structurei

Binds to activated CD44 and to GZMB.

Protein-protein interaction databases

BioGridi202359. 1 interaction.
IntActiP13609. 1 interaction.
STRINGi10090.ENSMUSP00000020271.

Structurei

3D structure databases

ProteinModelPortaliP13609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati89 – 9021
Repeati91 – 9222
Repeati93 – 9423
Repeati95 – 9624
Repeati97 – 9825
Repeati99 – 10026
Repeati101 – 10227
Repeati103 – 10428
Repeati105 – 10629
Repeati107 – 108210

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni89 – 1082010 X 2 AA tandem repeats of G-SAdd
BLAST

Sequence similaritiesi

Belongs to the serglycin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410J42T. Eukaryota.
ENOG4111DTK. LUCA.
GeneTreeiENSGT00390000000885.
HOGENOMiHOG000154415.
HOVERGENiHBG008180.
InParanoidiP13609.
KOiK06849.
OMAiSNSANCI.
OrthoDBiEOG7J9VS0.
PhylomeDBiP13609.
TreeFamiTF336310.

Family and domain databases

InterProiIPR007455. Serglycin.
[Graphical view]
PfamiPF04360. Serglycin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVPVGSRLV LALAFVLVWG SSVQGYPARR ARYQWVRCKP NGFFANCIEE
60 70 80 90 100
KGPQFDLIDE SNNIGPPMNN PVLMEGPSKD FISNYDDYGS GSGSGSGSGS
110 120 130 140 150
GSGSGSGSGF LGDMEWEYQP TDESNIVYFN YKPFDRILTE QNQDQPEDDF

II
Length:152
Mass (Da):16,711
Last modified:January 1, 1990 - v1
Checksum:iDCEC9829BA31036F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16133 mRNA. Translation: CAA34259.1.
M27393, M27391, M27392 Genomic DNA. Translation: AAA39965.1.
J04549 mRNA. Translation: AAA40111.1.
M33499 Genomic DNA. Translation: AAA39900.1.
M34603 mRNA. Translation: AAA39991.1.
AK087960 mRNA. Translation: BAC40059.1.
AK151357 mRNA. Translation: BAE30332.1.
AK157945 mRNA. Translation: BAE34275.1.
BC037076 mRNA. Translation: AAH37076.1.
CCDSiCCDS23889.1.
PIRiJQ0791.
RefSeqiNP_035287.1. NM_011157.2.
XP_006513438.1. XM_006513375.1.
XP_006513439.1. XM_006513376.2.
XP_006513440.1. XM_006513377.2.
UniGeneiMm.338790.

Genome annotation databases

EnsembliENSMUST00000020271; ENSMUSP00000020271; ENSMUSG00000020077.
ENSMUST00000160987; ENSMUSP00000125622; ENSMUSG00000020077.
ENSMUST00000162161; ENSMUSP00000125533; ENSMUSG00000020077.
GeneIDi19073.
KEGGimmu:19073.
UCSCiuc007fhi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16133 mRNA. Translation: CAA34259.1.
M27393, M27391, M27392 Genomic DNA. Translation: AAA39965.1.
J04549 mRNA. Translation: AAA40111.1.
M33499 Genomic DNA. Translation: AAA39900.1.
M34603 mRNA. Translation: AAA39991.1.
AK087960 mRNA. Translation: BAC40059.1.
AK151357 mRNA. Translation: BAE30332.1.
AK157945 mRNA. Translation: BAE34275.1.
BC037076 mRNA. Translation: AAH37076.1.
CCDSiCCDS23889.1.
PIRiJQ0791.
RefSeqiNP_035287.1. NM_011157.2.
XP_006513438.1. XM_006513375.1.
XP_006513439.1. XM_006513376.2.
XP_006513440.1. XM_006513377.2.
UniGeneiMm.338790.

3D structure databases

ProteinModelPortaliP13609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202359. 1 interaction.
IntActiP13609. 1 interaction.
STRINGi10090.ENSMUSP00000020271.

Proteomic databases

EPDiP13609.
MaxQBiP13609.
PaxDbiP13609.
PRIDEiP13609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020271; ENSMUSP00000020271; ENSMUSG00000020077.
ENSMUST00000160987; ENSMUSP00000125622; ENSMUSG00000020077.
ENSMUST00000162161; ENSMUSP00000125533; ENSMUSG00000020077.
GeneIDi19073.
KEGGimmu:19073.
UCSCiuc007fhi.1. mouse.

Organism-specific databases

CTDi5552.
MGIiMGI:97756. Srgn.

Phylogenomic databases

eggNOGiENOG410J42T. Eukaryota.
ENOG4111DTK. LUCA.
GeneTreeiENSGT00390000000885.
HOGENOMiHOG000154415.
HOVERGENiHBG008180.
InParanoidiP13609.
KOiK06849.
OMAiSNSANCI.
OrthoDBiEOG7J9VS0.
PhylomeDBiP13609.
TreeFamiTF336310.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.

Miscellaneous databases

NextBioi295598.
PROiP13609.
SOURCEiSearch...

Gene expression databases

BgeeiP13609.
CleanExiMM_SRGN.
ExpressionAtlasiP13609. baseline and differential.
GenevisibleiP13609. MM.

Family and domain databases

InterProiIPR007455. Serglycin.
[Graphical view]
PfamiPF04360. Serglycin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a mouse mastocytoma proteoglycan core protein."
    Kjellen L., Pettersson L., Lillhager P., Steen M.L., Pettersson U., Lehtonen P., Karlsson T., Ruoslahti E., Hellman L.
    Biochem. J. 263:105-113(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and characterization of the mouse gene that encodes the peptide core of secretory granule proteoglycans and expression of this gene in transfected rat-1 fibroblasts."
    Avraham S., Austen K.F., Nicodemus C.F., Gartner M.C., Stevens R.L.
    J. Biol. Chem. 264:16719-16726(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular cloning of a cDNA that encodes the peptide core of a mouse mast cell secretory granule proteoglycan and comparison with the analogous rat and human cDNA."
    Avraham S., Stevens R.L., Nicodemus C.F., Gartner M.C., Austen K.F., Weis J.H.
    Proc. Natl. Acad. Sci. U.S.A. 86:3763-3767(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Cloning and structural analysis of a gene encoding a mouse mastocytoma proteoglycan core protein; analysis of its evolutionary relation to three cross hybridizing regions in the mouse genome."
    Angerth T., Huang R., Aveskogh M., Pettersson I., Kjellen L., Hellman L.
    Gene 93:235-240(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Induction of a proteoglycan core protein mRNA in mouse T lymphocytes."
    Elliott J.F., Miller C.L., Pohajdak B., Talbot D., Helgason C.D., Bleackley R.C., Paetkau V.
    Mol. Immunol. 30:749-754(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Inner ear and Thymus.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  8. "A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation."
    Toyama-Sorimachi N., Sorimachi H., Tobita Y., Kitamura F., Yagita H., Suzuki K., Miyasaka M.
    J. Biol. Chem. 270:7437-7444(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 86-101, INTERACTION WITH CD44, GLYCOSYLATION.
  9. "Serglycin is essential for maturation of mast cell secretory granule."
    Abrink M., Grujic M., Pejler G.
    J. Biol. Chem. 279:40897-40905(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Serglycin-deficient cytotoxic T lymphocytes display defective secretory granule maturation and granzyme B storage."
    Grujic M., Braga T., Lukinius A., Eloranta M.-L., Knight S.D., Pejler G., Abrink M.
    J. Biol. Chem. 280:33411-33418(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases."
    Lundequist A., Abrink M., Pejler G.
    Biol. Chem. 387:1513-1519(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "A role for serglycin proteoglycan in granular retention and processing of mast cell secretory granule components."
    Henningsson F., Hergeth S., Cortelius R., Abrink M., Pejler G.
    FEBS J. 273:4901-4912(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION, DISRUPTION PHENOTYPE.
  13. "Serglycin is the major secreted proteoglycan in macrophages and has a role in the regulation of macrophage tumor necrosis factor-alpha secretion in response to lipopolysaccharide."
    Zernichow L., Abrink M., Hallgren J., Grujic M., Pejler G., Kolset S.O.
    J. Biol. Chem. 281:26792-26801(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Serglycin proteoglycan is required for secretory granule integrity in mucosal mast cells."
    Braga T., Grujic M., Lukinius A., Hellman L., Abrink M., Pejler G.
    Biochem. J. 403:49-57(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. "Neutrophil elastase depends on serglycin proteoglycan for localization in granules."
    Niemann C.U., Abrink M., Pejler G., Fischer R.L., Christensen E.I., Knight S.D., Borregaard N.
    Blood 109:4478-4486(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiSRGN_MOUSE
AccessioniPrimary (citable) accession number: P13609
Secondary accession number(s): Q3TZD4, Q8C2U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 16, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.