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P10124 (SRGN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serglycin
Alternative name(s):
Hematopoietic proteoglycan core protein
Platelet proteoglycan core protein
Short name=P.PG
Secretory granule proteoglycan core protein
Gene names
Name:SRGN
Synonyms:PRG, PRG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.15 Ref.16

Subunit structure

Binds to activated CD44 and to GZMB. Ref.12 Ref.13

Subcellular location

Cytoplasmic granule By similarity. Secretedextracellular space. Golgi apparatus. Note: Found in mast cell granules and in cytoplasmic granules of cytolytic T lymphocytes from where it is secreted upon cell activation. Secreted constitutively by endothelial cells and macrophages. Located to Golgi apparatus during neutrophil differentiation. Ref.11 Ref.14 Ref.16

Induction

By Epstein-Barr virus (EBV).

Post-translational modification

O-glycosylated; contains chondroitin sulfate and heparan sulfate By similarity. Ref.9

Sequence similarities

Belongs to the serglycin family.

Ontologies

Keywords
   Biological processApoptosis
Biomineralization
   Cellular componentGolgi apparatus
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell secretory granule organization

Inferred from sequence or structural similarity. Source: UniProtKB

biomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

granzyme-mediated apoptotic signaling pathway

Inferred from direct assay Ref.12. Source: UniProtKB

maintenance of granzyme B location in T cell secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of protease location in mast cell secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

mast cell secretory granule organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of bone mineralization

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of cytokine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

protein processing

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.14. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.11. Source: UniProtKB

mast cell granule

Inferred from sequence or structural similarity. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

zymogen granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GZMBP101442EBI-744915,EBI-2505785

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.9 Ref.10
Chain28 – 158131Serglycin
PRO_0000026679

Regions

Repeat94 – 9521
Repeat96 – 9722
Repeat98 – 9923
Repeat100 – 10124
Repeat102 – 10325
Repeat104 – 10526
Repeat106 – 10727
Repeat108 – 10928
Repeat110 – 11129
Region94 – 111189 X 2 AA tandem repeats of [SF]-G

Amino acid modifications

Glycosylation941O-linked (Xyl...) (glycosaminoglycan) Ref.9
Glycosylation961O-linked (Xyl...) (glycosaminoglycan) Ref.9
Glycosylation1001O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1021O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1041O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1061O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1081O-linked (Xyl...) (glycosaminoglycan) Potential
Glycosylation1101O-linked (Xyl...) (glycosaminoglycan) Potential
Disulfide bond40 ↔ 49 Potential

Natural variations

Natural variant311R → Q. Ref.1 Ref.2 Ref.3 Ref.5 Ref.7 Ref.8
Corresponds to variant rs2805910 [ dbSNP | Ensembl ].
VAR_032761

Experimental info

Sequence conflict1391N → S in CAA31255. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P10124 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: BD7767F39FFBC477

FASTA15817,652
        10         20         30         40         50         60 
MMQKLLKCSR LVLALALILV LESSVQGYPT RRARYQWVRC NPDSNSANCL EEKGPMFELL 

        70         80         90        100        110        120 
PGESNKIPRL RTDLFPKTRI QDLNRIFPLS EDYSGSGFGS GSGSGSGSGS GFLTEMEQDY 

       130        140        150 
QLVDESDAFH DNLRSLDRNL PSDSQDLGQH GLEEDFML 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA that encodes the peptide core of the secretory granule proteoglycan of human promyelocytic leukemia HL-60 cells."
Stevens R.L., Avraham S., Gartner M.C., Bruns G.A.P., Austen K.F., Weis J.H.
J. Biol. Chem. 263:7287-7291(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-31.
[2]"Nucleotide sequence of a cDNA encoding a hemopoietic proteoglycan core protein."
Stellrecht C.M., Saunders G.F.
Nucleic Acids Res. 17:7523-7523(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-31.
[3]"Characterization of the human gene that encodes the peptide core of secretory granule proteoglycans in promyelocytic leukemia HL-60 cells and analysis of the translated product."
Nicodemus C.F., Avraham S., Austen K.F., Purdy S., Jablonski J., Stevens R.L.
J. Biol. Chem. 265:5889-5896(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-31.
[4]"The human serglycin gene. Nucleotide sequence and methylation pattern in human promyelocytic leukemia HL-60 cells and T-lymphoblast Molt-4 cells."
Humphries D.E., Nicodemus C.F., Schiller V., Stevens R.L.
J. Biol. Chem. 267:13558-13563(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-31.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-31.
[8]"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], VARIANT GLN-31.
Tissue: Lung.
[9]"Complete amino acid sequence of a human platelet proteoglycan."
Alliel P.M., Perin J.-P., Maillet P., Bonnet F., Rosa J.-P., Jolles P.
FEBS Lett. 236:123-126(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-158, NUCLEOTIDE SEQUENCE [MRNA] OF 34-158, GLYCOSYLATION AT SER-94 AND SER-96.
[10]"Characterization and N-terminal sequence of human platelet proteoglycan."
Perin J.-P., Bonnet F., Maillet P., Jolles P.
Biochem. J. 255:1007-1013(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-93.
[11]"Synthesis, secretion, and subcellular localization of serglycin proteoglycan in human endothelial cells."
Schick B.P., Gradowski J.F., San Antonio J.D.
Blood 97:449-458(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation."
Metkar S.S., Wang B., Aguilar-Santelises M., Raja S.M., Uhlin-Hansen L., Podack E., Trapani J.A., Froelich C.J.
Immunity 16:417-428(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GZMB.
[13]"Cytotoxic cell granule-mediated apoptosis. Characterization of the macromolecular complex of granzyme B with serglycin."
Raja S.M., Wang B., Dantuluri M., Desai U.R., Demeler B., Spiegel K., Metkar S.S., Froelich C.J.
J. Biol. Chem. 277:49523-49530(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GZMB.
[14]"Localization of serglycin in human neutrophil granulocytes and their precursors."
Niemann C.U., Cowland J.B., Klausen P., Askaa J., Calafat J., Borregaard N.
J. Leukoc. Biol. 76:406-415(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Secretion of proteases in serglycin transfected Madin-Darby canine kidney cells."
Zernichow L., Dalen K.T., Prydz K., Winberg J.-O., Kolset S.O.
FEBS J. 273:536-547(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Serglycin constitutively secreted by myeloma plasma cells is a potent inhibitor of bone mineralization in vitro."
Theocharis A.D., Seidel C., Borset M., Dobra K., Baykov V., Labropoulou V., Kanakis I., Dalas E., Karamanos N.K., Sundan A., Hjerpe A.
J. Biol. Chem. 281:35116-35128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03223 mRNA. Translation: AAA60179.1.
X17042 mRNA. Translation: CAA34900.1.
M33651, M33649, M33650 Genomic DNA. Translation: AAA60322.1.
M90058 Genomic DNA. No translation available.
AK311873 mRNA. Translation: BAG34814.1.
AL442635 Genomic DNA. Translation: CAH71778.1.
CH471083 Genomic DNA. Translation: EAW54309.1.
BC015516 mRNA. Translation: AAH15516.1.
X12765 mRNA. Translation: CAA31255.1.
CCDSCCDS7285.1.
PIRA28058. A35183.
RefSeqNP_002718.2. NM_002727.2.
UniGeneHs.1908.

3D structure databases

ProteinModelPortalP10124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111543. 7 interactions.
IntActP10124. 16 interactions.
MINTMINT-1466608.
STRING9606.ENSP00000242465.

Polymorphism databases

DMDM269849659.

Proteomic databases

MaxQBP10124.
PaxDbP10124.
PRIDEP10124.

Protocols and materials databases

DNASU5552.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242465; ENSP00000242465; ENSG00000122862.
GeneID5552.
KEGGhsa:5552.
UCSCuc001joz.3. human.

Organism-specific databases

CTD5552.
GeneCardsGC10P070847.
HGNCHGNC:9361. SRGN.
HPAHPA000759.
MIM177040. gene.
neXtProtNX_P10124.
PharmGKBPA33733.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44969.
HOGENOMHOG000154415.
HOVERGENHBG008180.
InParanoidP10124.
KOK06849.
OrthoDBEOG7J9VS0.
PhylomeDBP10124.
TreeFamTF336310.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeP10124.
CleanExHS_SRGN.
GenevestigatorP10124.

Family and domain databases

InterProIPR007455. Serglycin.
[Graphical view]
PfamPF04360. Serglycin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRGN. human.
GeneWikiSRGN.
GenomeRNAi5552.
NextBio21518.
PROP10124.
SOURCESearch...

Entry information

Entry nameSRGN_HUMAN
AccessionPrimary (citable) accession number: P10124
Secondary accession number(s): B2R4L7, Q5VW06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM