P10124 (SRGN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	158 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › extracellular 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 process	Apoptosis Biomineralization
Cellular component	Golgi apparatus Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from direct assay Ref.12. Source: UniProtKB biomineral tissue development Inferred from electronic annotation. Source: UniProtKB-KW 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 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_component	Golgi apparatus Inferred from direct assay Ref.14. Source: UniProtKB 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: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GZMB	P10144	2	EBI-744915,EBI-2505785

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Ref.9 Ref.10
	Chain	28 – 158	131	Serglycin		PRO_0000026679
Regions
	Repeat	94 – 95	2	1
	Repeat	96 – 97	2	2
	Repeat	98 – 99	2	3
	Repeat	100 – 101	2	4
	Repeat	102 – 103	2	5
	Repeat	104 – 105	2	6
	Repeat	106 – 107	2	7
	Repeat	108 – 109	2	8
	Repeat	110 – 111	2	9
	Region	94 – 111	18	9 X 2 AA tandem repeats of [SF]-G
Amino acid modifications
	Glycosylation	94	1	O-linked (Xyl...) (glycosaminoglycan) Ref.9
	Glycosylation	96	1	O-linked (Xyl...) (glycosaminoglycan) Ref.9
	Glycosylation	100	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	102	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	104	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	106	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	108	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Glycosylation	110	1	O-linked (Xyl...) (glycosaminoglycan) Potential
	Disulfide bond	40 ↔ 49		Potential
Natural variations
	Natural variant	31	1	R → Q. Ref.1 Ref.2 Ref.3 Ref.5 Ref.7 Ref.8 Corresponds to variant rs2805910 [ dbSNP | Ensembl ].		VAR_032761
Experimental info
	Sequence conflict	139	1	N → S in CAA31255. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P10124 [UniParc]. Last modified November 24, 2009. Version 3. Checksum: BD7767F39FFBC477	FASTA	158	17,652
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00019372.
PIR	A28058. A35183.
RefSeq	NP_002718.2. NM_002727.2.
UniGene	Hs.1908.
3D structure databases
ProteinModelPortal	P10124.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10124. 8 interactions.
MINT	MINT-1466608.
STRING	9606.ENSP00000242465.
Polymorphism databases
DMDM	269849659.
Proteomic databases
PaxDb	P10124.
PRIDE	P10124.
Protocols and materials databases
DNASU	5552.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242465; ENSP00000242465; ENSG00000122862.
GeneID	5552.
KEGG	hsa:5552.
UCSC	uc001joz.3. human.
Organism-specific databases
CTD	5552.
GeneCards	GC10P070847.
HGNC	HGNC:9361. SRGN.
HPA	HPA000759.
MIM	177040. gene.
neXtProt	NX_P10124.
PharmGKB	PA33733.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG44969.
HOGENOM	HOG000154415.
HOVERGEN	HBG008180.
InParanoid	P10124.
KO	K06849.
OMA	DSNSANC.
OrthoDB	EOG4FFD3J.
PhylomeDB	P10124.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
Bgee	P10124.
CleanEx	HS_SRGN.
Genevestigator	P10124.
GermOnline	ENSG00000122862. Homo sapiens.
Family and domain databases
InterPro	IPR007455. Serglycin. [Graphical view]
Pfam	PF04360. Serglycin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SRGN. human.
GenomeRNAi	5552.
NextBio	21518.
SOURCE	Search...

Entry information

Entry name

SRGN_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.