SRGN_HUMAN
ID SRGN_HUMAN Reviewed; 158 AA.
AC P10124; B2R4L7; Q5VW06;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Serglycin;
DE AltName: Full=Hematopoietic proteoglycan core protein;
DE AltName: Full=Platelet proteoglycan core protein;
DE Short=P.PG;
DE AltName: Full=Secretory granule proteoglycan core protein;
DE Flags: Precursor;
GN Name=SRGN; Synonyms=PRG, PRG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-31.
RX PubMed=2835370; DOI=10.1016/s0021-9258(18)68639-9;
RA Stevens R.L., Avraham S., Gartner M.C., Bruns G.A.P., Austen K.F.,
RA Weis J.H.;
RT "Isolation and characterization of a cDNA that encodes the peptide core of
RT the secretory granule proteoglycan of human promyelocytic leukemia HL-60
RT cells.";
RL J. Biol. Chem. 263:7287-7291(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-31.
RX PubMed=2798108; DOI=10.1093/nar/17.18.7523;
RA Stellrecht C.M., Saunders G.F.;
RT "Nucleotide sequence of a cDNA encoding a hemopoietic proteoglycan core
RT protein.";
RL Nucleic Acids Res. 17:7523-7523(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-31.
RX PubMed=2180935; DOI=10.1016/s0021-9258(19)39446-3;
RA Nicodemus C.F., Avraham S., Austen K.F., Purdy S., Jablonski J.,
RA Stevens R.L.;
RT "Characterization of the human gene that encodes the peptide core of
RT secretory granule proteoglycans in promyelocytic leukemia HL-60 cells and
RT analysis of the translated product.";
RL J. Biol. Chem. 265:5889-5896(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1377686; DOI=10.1016/s0021-9258(18)42248-x;
RA Humphries D.E., Nicodemus C.F., Schiller V., Stevens R.L.;
RT "The human serglycin gene. Nucleotide sequence and methylation pattern in
RT human promyelocytic leukemia HL-60 cells and T-lymphoblast Molt-4 cells.";
RL J. Biol. Chem. 267:13558-13563(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-31.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-31.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-31.
RC TISSUE=Lung;
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 [9]
RP PROTEIN SEQUENCE OF 28-158, NUCLEOTIDE SEQUENCE [MRNA] OF 34-158, AND
RP GLYCOSYLATION AT SER-94 AND SER-96.
RX PubMed=3402609; DOI=10.1016/0014-5793(88)80298-9;
RA Alliel P.M., Perin J.-P., Maillet P., Bonnet F., Rosa J.-P., Jolles P.;
RT "Complete amino acid sequence of a human platelet proteoglycan.";
RL FEBS Lett. 236:123-126(1988).
RN [10]
RP PROTEIN SEQUENCE OF 28-93.
RX PubMed=3214420; DOI=10.1042/bj2551007;
RA Perin J.-P., Bonnet F., Maillet P., Jolles P.;
RT "Characterization and N-terminal sequence of human platelet proteoglycan.";
RL Biochem. J. 255:1007-1013(1988).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=11154222; DOI=10.1182/blood.v97.2.449;
RA Schick B.P., Gradowski J.F., San Antonio J.D.;
RT "Synthesis, secretion, and subcellular localization of serglycin
RT proteoglycan in human endothelial cells.";
RL Blood 97:449-458(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH GZMB.
RX PubMed=11911826; DOI=10.1016/s1074-7613(02)00286-8;
RA Metkar S.S., Wang B., Aguilar-Santelises M., Raja S.M., Uhlin-Hansen L.,
RA Podack E., Trapani J.A., Froelich C.J.;
RT "Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme B-
RT serglycin complexes into target cells without plasma membrane pore
RT formation.";
RL Immunity 16:417-428(2002).
RN [13]
RP INTERACTION WITH GZMB.
RX PubMed=12388539; DOI=10.1074/jbc.m209607200;
RA Raja S.M., Wang B., Dantuluri M., Desai U.R., Demeler B., Spiegel K.,
RA Metkar S.S., Froelich C.J.;
RT "Cytotoxic cell granule-mediated apoptosis. Characterization of the
RT macromolecular complex of granzyme B with serglycin.";
RL J. Biol. Chem. 277:49523-49530(2002).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15136585; DOI=10.1189/jlb.1003502;
RA Niemann C.U., Cowland J.B., Klausen P., Askaa J., Calafat J.,
RA Borregaard N.;
RT "Localization of serglycin in human neutrophil granulocytes and their
RT precursors.";
RL J. Leukoc. Biol. 76:406-415(2004).
RN [15]
RP FUNCTION.
RX PubMed=16420477; DOI=10.1111/j.1742-4658.2005.05085.x;
RA Zernichow L., Dalen K.T., Prydz K., Winberg J.-O., Kolset S.O.;
RT "Secretion of proteases in serglycin transfected Madin-Darby canine kidney
RT cells.";
RL FEBS J. 273:536-547(2006).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16870619; DOI=10.1074/jbc.m601061200;
RA Theocharis A.D., Seidel C., Borset M., Dobra K., Baykov V., Labropoulou V.,
RA Kanakis I., Dalas E., Karamanos N.K., Sundan A., Hjerpe A.;
RT "Serglycin constitutively secreted by myeloma plasma cells is a potent
RT inhibitor of bone mineralization in vitro.";
RL J. Biol. Chem. 281:35116-35128(2006).
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. {ECO:0000269|PubMed:11911826,
CC ECO:0000269|PubMed:16420477, ECO:0000269|PubMed:16870619}.
CC -!- SUBUNIT: Binds to activated CD44 and to GZMB.
CC -!- INTERACTION:
CC P10124; P10144: GZMB; NbExp=2; IntAct=EBI-744915, EBI-2505785;
CC P10124; P11226: MBL2; NbExp=4; IntAct=EBI-744915, EBI-5325353;
CC P10124; P61601: NCALD; NbExp=3; IntAct=EBI-744915, EBI-749635;
CC P10124; O00623: PEX12; NbExp=3; IntAct=EBI-744915, EBI-594836;
CC P10124; O43765: SGTA; NbExp=10; IntAct=EBI-744915, EBI-347996;
CC P10124; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-744915, EBI-744081;
CC P10124; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-744915, EBI-741480;
CC P10124; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-744915, EBI-10173939;
CC P10124; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-744915, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:11154222}. Cytolytic granule
CC {ECO:0000269|PubMed:11154222}. Secreted, extracellular space
CC {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:16870619}. Golgi
CC apparatus {ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}.
CC Note=Found in mast cell granules and in cytoplasmic granules of
CC cytolytic T lymphocytes from where it is secreted upon cell activation
CC (By similarity). Secreted constitutively by endothelial cells and
CC macrophages (PubMed:11154222). Located to Golgi apparatus during
CC neutrophil differentiation (PubMed:15136585).
CC {ECO:0000250|UniProtKB:P13609, ECO:0000269|PubMed:11154222,
CC ECO:0000269|PubMed:15136585}.
CC -!- INDUCTION: By Epstein-Barr virus (EBV).
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serglycin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03223; AAA60179.1; -; mRNA.
DR EMBL; X17042; CAA34900.1; -; mRNA.
DR EMBL; M33651; AAA60322.1; -; Genomic_DNA.
DR EMBL; M33649; AAA60322.1; JOINED; Genomic_DNA.
DR EMBL; M33650; AAA60322.1; JOINED; Genomic_DNA.
DR EMBL; M90058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK311873; BAG34814.1; -; mRNA.
DR EMBL; AL442635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54309.1; -; Genomic_DNA.
DR EMBL; BC015516; AAH15516.1; -; mRNA.
DR EMBL; X12765; CAA31255.1; -; mRNA.
DR CCDS; CCDS7285.1; -.
DR PIR; A35183; A28058.
DR RefSeq; NP_001307982.1; NM_001321053.1.
DR RefSeq; NP_001307983.1; NM_001321054.1.
DR RefSeq; NP_002718.2; NM_002727.3.
DR RefSeq; XP_016871881.1; XM_017016392.1.
DR AlphaFoldDB; P10124; -.
DR SMR; P10124; -.
DR BioGRID; 111543; 14.
DR IntAct; P10124; 23.
DR MINT; P10124; -.
DR STRING; 9606.ENSP00000242465; -.
DR GlyGen; P10124; 8 sites.
DR iPTMnet; P10124; -.
DR BioMuta; SRGN; -.
DR DMDM; 269849659; -.
DR EPD; P10124; -.
DR MassIVE; P10124; -.
DR MaxQB; P10124; -.
DR PaxDb; P10124; -.
DR PeptideAtlas; P10124; -.
DR PRIDE; P10124; -.
DR ProteomicsDB; 52568; -.
DR Antibodypedia; 609; 238 antibodies from 25 providers.
DR DNASU; 5552; -.
DR Ensembl; ENST00000242465.4; ENSP00000242465.3; ENSG00000122862.5.
DR GeneID; 5552; -.
DR KEGG; hsa:5552; -.
DR MANE-Select; ENST00000242465.4; ENSP00000242465.3; NM_002727.4; NP_002718.2.
DR UCSC; uc001joz.4; human.
DR CTD; 5552; -.
DR DisGeNET; 5552; -.
DR GeneCards; SRGN; -.
DR HGNC; HGNC:9361; SRGN.
DR HPA; ENSG00000122862; Tissue enriched (bone).
DR MIM; 177040; gene.
DR neXtProt; NX_P10124; -.
DR OpenTargets; ENSG00000122862; -.
DR PharmGKB; PA33733; -.
DR VEuPathDB; HostDB:ENSG00000122862; -.
DR eggNOG; ENOG502S72N; Eukaryota.
DR GeneTree; ENSGT00390000000885; -.
DR HOGENOM; CLU_142594_0_0_1; -.
DR InParanoid; P10124; -.
DR OMA; ANCIDEK; -.
DR OrthoDB; 1340705at2759; -.
DR PhylomeDB; P10124; -.
DR TreeFam; TF336310; -.
DR PathwayCommons; P10124; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P10124; -.
DR BioGRID-ORCS; 5552; 4 hits in 1076 CRISPR screens.
DR ChiTaRS; SRGN; human.
DR GeneWiki; SRGN; -.
DR GenomeRNAi; 5552; -.
DR Pharos; P10124; Tbio.
DR PRO; PR:P10124; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P10124; protein.
DR Bgee; ENSG00000122862; Expressed in trabecular bone tissue and 203 other tissues.
DR Genevisible; P10124; HS.
DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0042629; C:mast cell granule; ISS:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
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; IDA:GO_Central.
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:0030502; P:negative regulation of bone mineralization; IDA: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: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; 1.
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..27
FT /evidence="ECO:0000269|PubMed:3214420,
FT ECO:0000269|PubMed:3402609"
FT CHAIN 28..158
FT /note="Serglycin"
FT /id="PRO_0000026679"
FT REPEAT 94..95
FT /note="1"
FT REPEAT 96..97
FT /note="2"
FT REPEAT 98..99
FT /note="3"
FT REPEAT 100..101
FT /note="4"
FT REPEAT 102..103
FT /note="5"
FT REPEAT 104..105
FT /note="6"
FT REPEAT 106..107
FT /note="7"
FT REPEAT 108..109
FT /note="8"
FT REPEAT 110..111
FT /note="9"
FT REGION 94..111
FT /note="9 X 2 AA tandem repeats of [SF]-G"
FT REGION 134..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:3402609"
FT CARBOHYD 96
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000269|PubMed:3402609"
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 CARBOHYD 108
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 40..49
FT /evidence="ECO:0000255"
FT VARIANT 31
FT /note="R -> Q (in dbSNP:rs2229498)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2180935,
FT ECO:0000269|PubMed:2798108, ECO:0000269|PubMed:2835370,
FT ECO:0000269|Ref.7"
FT /id="VAR_032761"
FT CONFLICT 139
FT /note="N -> S (in Ref. 9; CAA31255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17652 MW; BD7767F39FFBC477 CRC64;
MMQKLLKCSR LVLALALILV LESSVQGYPT RRARYQWVRC NPDSNSANCL EEKGPMFELL
PGESNKIPRL RTDLFPKTRI QDLNRIFPLS EDYSGSGFGS GSGSGSGSGS GFLTEMEQDY
QLVDESDAFH DNLRSLDRNL PSDSQDLGQH GLEEDFML
