ID MEP1A_MOUSE Reviewed; 747 AA.
AC P28825; B0V2P9; Q91WH9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 4.
DT 24-JAN-2024, entry version 201.
DE RecName: Full=Meprin A subunit alpha;
DE EC=3.4.24.18;
DE AltName: Full=Endopeptidase-2;
DE AltName: Full=MEP-1;
DE Flags: Precursor;
GN Name=Mep1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 65-103; 107-122;
RP 273-292; 314-348; 370-375; 377-386; 389-398 AND 527-557.
RC STRAIN=C3H/He, and C57BL/6J; TISSUE=Kidney;
RX PubMed=1374387; DOI=10.1016/s0021-9258(19)50406-9;
RA Jiang W., Gorbea C.M., Flannery A.V., Beynon R.J., Grant G.A., Bond J.S.;
RT "The alpha subunit of meprin A. Molecular cloning and sequencing,
RT differential expression in inbred mouse strains, and evidence for divergent
RT evolution of the alpha and beta subunits.";
RL J. Biol. Chem. 267:9185-9193(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP PROTEIN SEQUENCE OF 21-25 AND 65-69.
RX PubMed=8615815; DOI=10.1042/bj3150461;
RA Beynon R.J., Oliver S., Robertson D.H.L.;
RT "Characterization of the soluble, secreted form of urinary meprin.";
RL Biochem. J. 315:461-465(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-258.
RC STRAIN=129;
RX PubMed=9161413; DOI=10.1016/s0378-1119(96)00834-7;
RA Jiang W., Flannery A.V.;
RT "Correlation of the exon/intron organization to the secondary structures of
RT the protease domain of mouse meprin alpha subunit.";
RL Gene 189:65-71(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-262.
RX PubMed=1939172; DOI=10.1016/s0021-9258(18)54648-2;
RA Dumermuth E., Sterchi E.E., Jiang W., Wolz R.L., Bond J.S., Flannery A.V.,
RA Beynon R.J.;
RT "The astacin family of metalloendopeptidases.";
RL J. Biol. Chem. 266:21381-21385(1991).
RN [7]
RP PROTEIN SEQUENCE OF 65-72; 315-348 AND 529-546, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RC STRAIN=ICR; TISSUE=Kidney;
RX PubMed=1894622; DOI=10.1016/s0021-9258(19)47380-8;
RA Kounnas M.Z., Wolz R.L., Gorbea C.M., Bond J.S.;
RT "Meprin-A and -B. Cell surface endopeptidases of the mouse kidney.";
RL J. Biol. Chem. 266:17350-17357(1991).
RN [8]
RP SUBUNIT.
RX PubMed=1929422; DOI=10.1016/0003-9861(91)90580-c;
RA Gorbea C.M., Flannery A.V., Bond J.S.;
RT "Homo- and heterotetrameric forms of the membrane-bound
RT metalloendopeptidases meprin A and B.";
RL Arch. Biochem. Biophys. 290:549-553(1991).
RN [9]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1883833; DOI=10.1021/bi00098a029;
RA Wolz R.L., Harris R.B., Bond J.S.;
RT "Mapping the active site of meprin-A with peptide substrates and
RT inhibitors.";
RL Biochemistry 30:8488-8493(1991).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=11278902; DOI=10.1074/jbc.m011414200;
RA Bertenshaw G.P., Turk B.E., Hubbard S.J., Matters G.L., Bylander J.E.,
RA Crisman J.M., Cantley L.C., Bond J.S.;
RT "Marked differences between metalloproteases meprin A and B in substrate
RT and peptide bond specificity.";
RL J. Biol. Chem. 276:13248-13255(2001).
RN [11]
RP INTERACTION WITH MBL2.
RX PubMed=16116208; DOI=10.4049/jimmunol.175.5.3177;
RA Hirano M., Ma B.Y., Kawasaki N., Okimura K., Baba M., Nakagawa T., Miwa K.,
RA Kawasaki N., Oka S., Kawasaki T.;
RT "Mannan-binding protein blocks the activation of metalloproteases meprin
RT alpha and beta.";
RL J. Immunol. 175:3177-3185(2005).
RN [12]
RP SUBUNIT, GLYCOSYLATION AT ASN-28; ASN-139; ASN-221; ASN-257; ASN-317;
RP ASN-413; ASN-439; ASN-533 AND ASN-540, AND MUTAGENESIS OF ASN-139; SER-141;
RP ASN-221; ASN-257 AND THR-259.
RX PubMed=17040911; DOI=10.1074/jbc.m602769200;
RA Ishmael S.S., Ishmael F.T., Jones A.D., Bond J.S.;
RT "Protease domain glycans affect oligomerization, disulfide bond formation,
RT and stability of the meprin A metalloprotease homo-oligomer.";
RL J. Biol. Chem. 281:37404-37415(2006).
RN [13]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17976009; DOI=10.1515/bc.2007.156;
RA Bylander J.E., Bertenshaw G.P., Matters G.L., Hubbard S.J., Bond J.S.;
RT "Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate
RT and inhibitor specificities.";
RL Biol. Chem. 388:1163-1172(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP 3D-STRUCTURE MODELING.
RX PubMed=8508794; DOI=10.1111/j.1432-1033.1993.tb17915.x;
RA Stoecker W., Gomis-Rueth F.-X., Bode W., Zwilling R.;
RT "Implications of the three-dimensional structure of astacin for the
RT structure and function of the astacin family of zinc-endopeptidases.";
RL Eur. J. Biochem. 214:215-231(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of protein and peptide substrates preferentially on
CC carboxyl side of hydrophobic residues.; EC=3.4.24.18;
CC Evidence={ECO:0000269|PubMed:11278902, ECO:0000269|PubMed:1883833};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- ACTIVITY REGULATION: Inhibited by metal ion chelators EDTA and 1,10-
CC phenanthroline, bradykinin analogs, cysteine, CONA65, and several
CC hydroxamate compounds, particularly tyrosine hydroxamate. Not inhibited
CC by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine
CC proteinase inhibitors iodoacetic acid and E-64.
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29.6 uM for GRP {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=67.2 uM for PTH 12-34 {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=111 uM for secretin {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=30.6 uM for substance P {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=156 uM for LHRH {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=22.3 uM for alpha-MSH {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=101 uM for bradykinin {ECO:0000269|PubMed:17976009,
CC ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622};
CC KM=290 uM for Arg-Pro-Pro-Gly-Npa-Ser-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=331 uM for Arg-Pro-Pro-Gly-Npa-Ala-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=174 uM for Arg-Pro-Pro-Gly-Npa-Arg-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=226 uM for Arg-Pro-Pro-Gly-Npa-Phe-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=182 uM for Arg-Pro-Pro-Gly-Npa-Lys-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=339 uM for Arg-Pro-Pro-Gly-Npa-Glu-Pro-Phe-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=366 uM for 2ABz-Arg-Pro-Gly-Phe-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=296 uM for 2ABz-Arg-Pro-Ile-Phe-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=183 uM for 2ABz-Arg-Hyp-Gly-Phe-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=220 uM for 2ABz-Arg-Gly-Pro-Phe-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=1380 uM for 2ABz-Arg-Pro-Gly-Ala-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=1220 uM for 2ABz-Arg-Pro-Gly-Glu-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=402 uM for 2ABz-Arg-Pro-Gly-Lys-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC KM=2460 uM for 2ABz-Arg-Pro-Gly-Leu-Ser-Pro-Npa-Arg
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC Temperature dependence:
CC The half-life at 58 degrees Celsius is 50 minutes.
CC {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833,
CC ECO:0000269|PubMed:1894622};
CC -!- SUBUNIT: Homotetramer consisting of disulfide-linked alpha subunits,
CC homooligomer consisting of disulfide-linked alpha subunit homodimers,
CC or heterotetramer of two alpha and two beta subunits formed by non-
CC covalent association of two disulfide-linked heterodimers. Genetic
CC factors determine which oligomer(s) will be formed (strain-specific).
CC Interacts with MBL2 through its carbohydrate moiety. This interaction
CC may inhibit its catalytic activity. {ECO:0000269|PubMed:16116208,
CC ECO:0000269|PubMed:17040911, ECO:0000269|PubMed:1929422}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Kidney, intestinal brush borders and salivary
CC ducts.
CC -!- PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small
CC amount of fucose. {ECO:0000269|PubMed:17040911,
CC ECO:0000269|PubMed:1894622}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75354.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15258.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M74897; AAA75354.1; ALT_INIT; mRNA.
DR EMBL; CT010585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015258; AAH15258.1; ALT_INIT; mRNA.
DR EMBL; U62765; AAC53194.1; -; Genomic_DNA.
DR PIR; A40195; A40195.
DR RefSeq; NP_032611.2; NM_008585.2.
DR RefSeq; XP_006523814.1; XM_006523751.3.
DR AlphaFoldDB; P28825; -.
DR SMR; P28825; -.
DR BioGRID; 201396; 2.
DR IntAct; P28825; 1.
DR MINT; P28825; -.
DR STRING; 10090.ENSMUSP00000024707; -.
DR MEROPS; M12.002; -.
DR GlyCosmos; P28825; 9 sites, 11 glycans.
DR GlyGen; P28825; 9 sites.
DR iPTMnet; P28825; -.
DR PhosphoSitePlus; P28825; -.
DR jPOST; P28825; -.
DR MaxQB; P28825; -.
DR PaxDb; 10090-ENSMUSP00000024707; -.
DR PeptideAtlas; P28825; -.
DR ProteomicsDB; 295924; -.
DR DNASU; 17287; -.
DR Ensembl; ENSMUST00000117137.8; ENSMUSP00000113838.2; ENSMUSG00000023914.17.
DR GeneID; 17287; -.
DR KEGG; mmu:17287; -.
DR UCSC; uc008cpc.1; mouse.
DR AGR; MGI:96963; -.
DR CTD; 4224; -.
DR MGI; MGI:96963; Mep1a.
DR VEuPathDB; HostDB:ENSMUSG00000023914; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00950000183111; -.
DR HOGENOM; CLU_021966_1_0_1; -.
DR InParanoid; P28825; -.
DR OMA; FEMFRLR; -.
DR OrthoDB; 2876645at2759; -.
DR PhylomeDB; P28825; -.
DR TreeFam; TF315280; -.
DR BRENDA; 3.4.24.18; 3474.
DR SABIO-RK; P28825; -.
DR BioGRID-ORCS; 17287; 1 hit in 65 CRISPR screens.
DR ChiTaRS; Mep1a; mouse.
DR PRO; PR:P28825; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P28825; Protein.
DR Bgee; ENSMUSG00000023914; Expressed in right kidney and 47 other cell types or tissues.
DR ExpressionAtlas; P28825; baseline and differential.
DR Genevisible; P28825; MM.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0017090; C:meprin A complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0070573; F:metallodipeptidase activity; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0038004; P:epidermal growth factor receptor ligand maturation; ISO:MGI.
DR GO; GO:0140448; P:signaling receptor ligand precursor processing; ISO:MGI.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008294; Meprin.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR049342; TRAF_MEP1_MATH_dom.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF824; MEPRIN A SUBUNIT ALPHA; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF21355; TRAF-mep_MATH; 1.
DR PIRSF; PIRSF001196; Meprin; 1.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8615815"
FT PROPEP 21..64
FT /evidence="ECO:0000269|PubMed:1374387,
FT ECO:0000269|PubMed:1894622, ECO:0000269|PubMed:8615815"
FT /id="PRO_0000028879"
FT CHAIN 65..747
FT /note="Meprin A subunit alpha"
FT /id="PRO_0000028880"
FT TOPO_DOM 65..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..259
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 263..432
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 433..594
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 671..711
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 638..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT SITE 601
FT /note="Not glycosylated"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17040911"
FT DISULFID 106..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 127..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 268..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 307
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 675..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 680..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 697..710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 139
FT /note="N->Q: Increased susceptibility to heat-inactivation.
FT Forms homodimers and oligomers; when associated with Q-221.
FT Inactive, impaired ability to form homodimers or oligomers;
FT when associated with Q-257 or Q-221 and Q-257."
FT /evidence="ECO:0000269|PubMed:17040911"
FT MUTAGEN 141
FT /note="S->A: Impaired ability to form homodimers or
FT oligomers; when associated with A-259."
FT /evidence="ECO:0000269|PubMed:17040911"
FT MUTAGEN 221
FT /note="N->Q: Increased susceptibility to heat-inactivation.
FT Forms homodimers and oligomers; when associated with Q-139
FT or Q-257. Inactive, impaired ability to form homodimers or
FT oligomers; when associated with Q-139 and Q-257."
FT /evidence="ECO:0000269|PubMed:17040911"
FT MUTAGEN 257
FT /note="N->Q: Increased susceptibility to heat-inactivation.
FT Forms homodimers and oligomers; when associated with Q-221.
FT Inactive, impaired ability to form homodimers or oligomers;
FT when associated with Q-139 or Q-139 and Q-221."
FT /evidence="ECO:0000269|PubMed:17040911"
FT MUTAGEN 259
FT /note="T->A: Impaired ability to form homodimers or
FT oligomers; when associated with A-141."
FT /evidence="ECO:0000269|PubMed:17040911"
FT CONFLICT 482
FT /note="F -> L (in Ref. 1; AAA75354)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="N -> I (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="N -> S (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="W -> T (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84231 MW; 2A1A268043559953 CRC64;
MLWIQPACLL SLIFSAHIAA VSIKHLLNGS DHDTDVGEQK DIFEINLAAG LNLFQGDILL
PRTRNAMRDP SSRWKLPIPY ILADNLELNA KGAILHAFEM FRLKSCVDFK PYEGESSYII
FQKLSGCWSM IGDQQVGQNI SIGEGCDFKA TIEHEILHAL GFFHEQSRTD RDDYVNIWWD
QIITDYEHNF NTYDDNTITD LNTPYDYESL MHYGPFSFNK NESIPTITTK IPEFNTIIGQ
LPDFSAIDLI RLNRMYNCTA THTLLDHCDF EKTNVCGMIQ GTRDDADWAH GDSSQPEQVD
HTLVGQCKGA GYFMFFNTSL GARGEAALLE SRILYPKRKQ QCLQFFYKMT GSPADRFEVW
VRRDDNAGKV RQLAKIQTFQ GDSDHNWKIA HVTLNEEKKF RYVFLGTKGD PGNSSGGIYL
DDITLTETPC PAGVWTIRNI SQILENTVKG DKLVSPRFYN SEGYGVGVTL YPNGRITSNS
GFLGLTFHLY SGDNDAILEW PVENRQAIMT ILDQEADTRN RMSLTLMFTT SKNQTSSAIN
GSVIWDRPSK VGVYDKDCDC FRSLDWGWGQ AISHQLLKRR NFLKGDSLII FVDFKDLTHL
NRTEVPASAR STMPRGLLLQ GQESPALGES SRKAMLEESL PSSLGQRHPS RQKRSVENTG
PMEDHNWPQY FRDPCDPNPC QNEGTCVNVK GMASCRCVSG HAFFYAGERC QAMHVHGSLL
GLLIGCIAGL IFLTFVTFST TNGKLRQ
//
