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   24-JAN-2024, entry version 198.
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}.
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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   GlyCosmos; P10124; 8 sites, No reported glycans.
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; 9606-ENSP00000242465; -.
DR   PeptideAtlas; P10124; -.
DR   ProteomicsDB; 52568; -.
DR   Antibodypedia; 609; 270 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   AGR; HGNC:9361; -.
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; QWVRCSP; -.
DR   OrthoDB; 4534120at2759; -.
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 1154 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 204 other cell types or tissues.
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   PANTHER; PTHR17178; SECRETORY GRANULE PROTEOGLYCAN CORE PROTEIN; 1.
DR   PANTHER; PTHR17178:SF0; SERGLYCIN; 1.
DR   Pfam; PF04360; Serglycin; 1.
DR   Genevisible; P10124; HS.
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
//