ID MASP1_RAT Reviewed; 704 AA.
AC Q8CHN8; O09020; Q5U365; Q8CG41; Q9JJS9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 24-JAN-2024, entry version 138.
DE RecName: Full=Mannan-binding lectin serine protease 1;
DE EC=3.4.21.-;
DE AltName: Full=Complement factor MASP-3;
DE AltName: Full=Complement-activating component of Ra-reactive factor;
DE AltName: Full=Mannose-binding lectin-associated serine protease 1;
DE Short=MASP-1;
DE AltName: Full=Mannose-binding protein-associated serine protease;
DE AltName: Full=Ra-reactive factor serine protease p100;
DE Short=RaRF;
DE AltName: Full=Serine protease 5;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 1 heavy chain;
DE Contains:
DE RecName: Full=Mannan-binding lectin serine protease 1 light chain;
DE Flags: Precursor;
GN Name=Masp1; Synonyms=Crarf, Masp3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 307-461 (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12847554; DOI=10.1038/sj.gene.6363970;
RA Stover C.M., Lynch N.J., Dahl M.R., Hanson S., Takahashi M.,
RA Frankenberger M., Ziegler-Heitbrock L., Eperon I., Thiel S.,
RA Schwaeble W.J.;
RT "Murine serine proteases MASP-1 and MASP-3, components of the lectin
RT pathway activation complex of complement, are encoded by a single
RT structural gene.";
RL Genes Immun. 4:374-384(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-704 (ISOFORM 1), GLYCOSYLATION,
RP HOMODIMERIZATION, AND INTERACTION WITH MBL1.
RC TISSUE=Liver;
RX PubMed=10913141; DOI=10.1074/jbc.m004030200;
RA Wallis R., Dodd R.B.;
RT "Interaction of mannose-binding protein with associated serine proteases:
RT effects of naturally occurring mutations.";
RL J. Biol. Chem. 275:30962-30969(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-223 (ISOFORM 1).
RX PubMed=9314946;
RA Knittel T., Fellmer P., Neubauer K., Kawakami M., Grundmann A.,
RA Ramadori G.;
RT "The complement-activating protease P100 is expressed by hepatocytes and is
RT induced by IL-6 in vitro and during the acute phase reaction in vivo.";
RL Lab. Invest. 77:221-230(1997).
RN [5]
RP MUTAGENESIS OF SER-651, AUTOCATALYTIC CLEAVAGE, HOMODIMERIZATION, AND
RP INTERACTION WITH MBL1.
RX PubMed=11337510; DOI=10.1074/jbc.m103539200;
RA Chen C.-B., Wallis R.;
RT "Stoichiometry of complexes between mannose-binding protein and its
RT associated serine proteases. Defining functional units for complement
RT activation.";
RL J. Biol. Chem. 276:25894-25902(2001).
RN [6]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15060079; DOI=10.1074/jbc.m401318200;
RA Chen C.-B., Wallis R.;
RT "Two mechanisms for mannose-binding protein modulation of the activity of
RT its associated serine proteases.";
RL J. Biol. Chem. 279:26058-26065(2004).
CC -!- FUNCTION: Functions in the lectin pathway of complement, which performs
CC a key role in innate immunity by recognizing pathogens through patterns
CC of sugar moieties and neutralizing them. The lectin pathway is
CC triggered upon binding of mannan-binding lectin (MBL) and ficolins to
CC sugar moieties which leads to activation of the associated proteases
CC MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2
CC or C2 or directly activate C3 the key component of complement reaction.
CC Isoform 2 may have an inhibitory effect on the activation of the lectin
CC pathway of complement or may cleave IGFBP5. Also plays a role in
CC development. {ECO:0000250|UniProtKB:P48740}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for C2 (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15060079};
CC -!- SUBUNIT: Homodimer. Interacts with the oligomeric lectins MBL2, FCN2
CC and FCN3; triggers the lectin pathway of complement through activation
CC of C3. Interacts with SERPING1. Interacts with COLEC11; probably
CC triggers the lectin pathway of complement.
CC {ECO:0000250|UniProtKB:P48740}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12847554}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=MASP-1;
CC IsoId=Q8CHN8-1; Sequence=Displayed;
CC Name=2; Synonyms=MASP-3;
CC IsoId=Q8CHN8-2; Sequence=VSP_036818, VSP_036819;
CC Name=3;
CC IsoId=Q8CHN8-3; Sequence=VSP_036816, VSP_036817;
CC -!- TISSUE SPECIFICITY: Protein of the plasma which is primarily expressed
CC by liver. {ECO:0000269|PubMed:12847554}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- PTM: N-glycosylated. Some N-linked glycan are of the complex-type.
CC {ECO:0000269|PubMed:10913141}.
CC -!- PTM: Autoproteolytic processing of the proenzyme produces the active
CC enzyme composed on the heavy and the light chain held together by a
CC disulfide bond. Isoform 1 but not isoform 2 is activated through
CC autoproteolytic processing (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AJ457084; CAD29746.1; -; mRNA.
DR EMBL; AJ487624; CAD32173.1; -; mRNA.
DR EMBL; BC085685; AAH85685.1; -; mRNA.
DR EMBL; AJ277423; CAB89695.1; -; mRNA.
DR EMBL; AF004661; AAB65832.1; -; mRNA.
DR RefSeq; NP_071593.1; NM_022257.1. [Q8CHN8-1]
DR RefSeq; XP_006248588.1; XM_006248526.3. [Q8CHN8-2]
DR RefSeq; XP_008767026.1; XM_008768804.2. [Q8CHN8-3]
DR PDB; 3POB; X-ray; 1.80 A; A=188-301.
DR PDB; 3POE; X-ray; 1.50 A; A=188-301.
DR PDB; 3POF; X-ray; 1.50 A; A/B=188-301.
DR PDB; 3POG; X-ray; 2.75 A; A/B/C=188-301.
DR PDB; 3POI; X-ray; 1.70 A; A/B=188-301.
DR PDB; 3POJ; X-ray; 1.45 A; A/B=188-301.
DR PDB; 5CKQ; X-ray; 3.70 A; A=25-301.
DR PDBsum; 3POB; -.
DR PDBsum; 3POE; -.
DR PDBsum; 3POF; -.
DR PDBsum; 3POG; -.
DR PDBsum; 3POI; -.
DR PDBsum; 3POJ; -.
DR PDBsum; 5CKQ; -.
DR AlphaFoldDB; Q8CHN8; -.
DR SMR; Q8CHN8; -.
DR CORUM; Q8CHN8; -.
DR STRING; 10116.ENSRNOP00000002507; -.
DR MEROPS; S01.198; -.
DR GlyCosmos; Q8CHN8; 6 sites, No reported glycans.
DR GlyGen; Q8CHN8; 4 sites.
DR PhosphoSitePlus; Q8CHN8; -.
DR Ensembl; ENSRNOT00000047678.5; ENSRNOP00000044812.3; ENSRNOG00000001827.9. [Q8CHN8-3]
DR Ensembl; ENSRNOT00000094154.1; ENSRNOP00000079792.1; ENSRNOG00000001827.9. [Q8CHN8-1]
DR Ensembl; ENSRNOT00055007350; ENSRNOP00055005508; ENSRNOG00055004619. [Q8CHN8-1]
DR Ensembl; ENSRNOT00060022314; ENSRNOP00060017698; ENSRNOG00060013056. [Q8CHN8-1]
DR Ensembl; ENSRNOT00065005045; ENSRNOP00065003585; ENSRNOG00065003514. [Q8CHN8-1]
DR GeneID; 64023; -.
DR KEGG; rno:64023; -.
DR UCSC; RGD:620213; rat. [Q8CHN8-1]
DR AGR; RGD:620213; -.
DR CTD; 5648; -.
DR RGD; 620213; Masp1.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_006842_14_0_1; -.
DR InParanoid; Q8CHN8; -.
DR OrthoDB; 5394076at2759; -.
DR PhylomeDB; Q8CHN8; -.
DR TreeFam; TF330373; -.
DR BRENDA; 3.4.21.B7; 5301.
DR Reactome; R-RNO-166662; Lectin pathway of complement activation.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
DR SABIO-RK; Q8CHN8; -.
DR EvolutionaryTrace; Q8CHN8; -.
DR PRO; PR:Q8CHN8; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001827; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR ExpressionAtlas; Q8CHN8; baseline and differential.
DR Genevisible; Q8CHN8; RN.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006956; P:complement activation; NAS:RGD.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF13; MANNAN-BINDING LECTIN SERINE PROTEASE 1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autocatalytic cleavage; Calcium;
KW Complement activation lectin pathway; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Hydroxylation; Immunity; Innate immunity;
KW Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..704
FT /note="Mannan-binding lectin serine protease 1"
FT /id="PRO_0000369242"
FT CHAIN 25..453
FT /note="Mannan-binding lectin serine protease 1 heavy chain"
FT /id="PRO_0000369243"
FT CHAIN 454..704
FT /note="Mannan-binding lectin serine protease 1 light chain"
FT /id="PRO_0000369244"
FT DOMAIN 25..143
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 144..187
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000250"
FT DOMAIN 190..302
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 304..369
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 370..439
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 454..701
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 25..305
FT /note="Interaction with MBL1"
FT REGION 25..283
FT /note="Interaction with FCN2"
FT /evidence="ECO:0000250"
FT REGION 25..189
FT /note="Homodimerization"
FT REGION 25..189
FT /note="Interaction with MBL2"
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 557
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 651
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT SITE 453..454
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..96
FT /evidence="ECO:0000250"
FT DISULFID 148..162
FT /evidence="ECO:0000250"
FT DISULFID 158..171
FT /evidence="ECO:0000250"
FT DISULFID 173..186
FT /evidence="ECO:0000250"
FT DISULFID 190..217
FT /evidence="ECO:0000250"
FT DISULFID 247..265
FT /evidence="ECO:0000250"
FT DISULFID 306..354
FT /evidence="ECO:0000250"
FT DISULFID 334..367
FT /evidence="ECO:0000250"
FT DISULFID 372..419
FT /evidence="ECO:0000250"
FT DISULFID 402..437
FT /evidence="ECO:0000250"
FT DISULFID 441..577
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00302"
FT DISULFID 480..496
FT /evidence="ECO:0000250"
FT DISULFID 619..636
FT /evidence="ECO:0000250"
FT DISULFID 647..677
FT /evidence="ECO:0000250"
FT VAR_SEQ 369..385
FT /note="IVDCGVPAVLKHGLVTF -> KSEIDLEEELESEQVAE (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036816"
FT VAR_SEQ 386..704
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036817"
FT VAR_SEQ 443
FT /note="L -> QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRIPNDKWFGSG
FT ALLSESWILTAAHVLRSQRRDNTVIPVSKDHVTVYLGLHDVRDKSGAVNSSAARVVLHP
FT DFNIQNYNHDIALVQLQEPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTV
FT DEIIISGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCL
FT GDSGGAFVIFDEMSQRWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLLEEMNSPRG
FT VRELQVER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12847554"
FT /id="VSP_036818"
FT VAR_SEQ 444..704
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12847554"
FT /id="VSP_036819"
FT MUTAGEN 651
FT /note="S->A: Prevents protease self-activation through
FT proteolytic cleavage into heavy and light chain."
FT /evidence="ECO:0000269|PubMed:11337510"
FT CONFLICT 60
FT /note="Missing (in Ref. 1; CAD29746)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Q -> H (in Ref. 1; CAD29746)"
FT /evidence="ECO:0000305"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3POJ"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:3POJ"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3POJ"
FT CARBOHYD Q8CHN8-2:538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD Q8CHN8-2:604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 80097 MW; 3CB61ED661967127 CRC64;
MRFLSFRRLL LYHVLCLTLT EVSAHTVELN EMFGQIQSPG YPDSYPSDSE VTWNITVPEG
FRVQLYFMHF NLESSYLCEY DYVKVETEDQ VLATFCGRET TDTEQTPGQE VVLSPGSFMS
VTFRSDFSNE ERFTGFDAHY MAVDVDECKE REDEELSCDH YCHNYIGGYY CSCRFGYILH
TDNRTCRVEC SGNLFTQRTG TITSPDYPNP YPKSSECSYT IDLEEGFMVT LQFEDIFDIE
DHPEVPCPYD YIKIKAGSKV WGPFCGEKSP EPISTQSHSI QILFRSDNSG ENRGWRLSYR
AAGNECPKLQ PPVYGKIEPS QAVYSFKDQV LISCDTGYKV LKDNEVMDTF QIECLKDGAW
SNKIPTCKIV DCGVPAVLKH GLVTFSTRNN LTTYKSEIRY SCQQPYYKML HNTTGVYTCS
AHGTWTNEVL KRSLPTCLPV CGLPKFSRKH ISRIFNGRPA QKGTTPWIAM LSQLNGQPFC
GGSLLGSNWV LTAAHCLHHP LDPEEPILHN SHLLSPSDFK IIMGKHWRRR SDEDEQHLHV
KHIMLHPLYN PSTFENDLGL VELSESPRLN DFVMPVCLPE HPSTEGTMVI VSGWGKQFLQ
RLPENLMEIE IPIVNYHTCQ EAYTPLGKKV TQDMICAGEK EGGKDACAGD SGGPMVTKDA
ERDQWYLVGV VSWGEDCGKK DRYGVYSYIY PNKDWIQRVT GVRN
//
