MASP1_MOUSE
ID MASP1_MOUSE Reviewed; 704 AA.
AC P98064; A2RRH8; A2RRH9; Q8CD27; Q8CIR8; Q920S0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 178.
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 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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8133044;
RA Takayama Y., Takada F., Takahashi A., Kawakami M.;
RT "A 100-kDa protein in the C4-activating component of Ra-reactive factor is
RT a new serine protease having module organization similar to C1r and C1s.";
RL J. Immunol. 152:2308-2316(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
RP SPLICING (ISOFORM 1).
RC STRAIN=BALB/cJ; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 465-704 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8439319; DOI=10.1006/bbrc.1993.1103;
RA Takahashi A., Takayama Y., Hatsuse H., Kawakami M.;
RT "Presence of a serine protease in the complement-activating component of
RT the complement-dependent bactericidal factor, RaRF, in mouse serum.";
RL Biochem. Biophys. Res. Commun. 190:681-687(1993).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18424734; DOI=10.4049/jimmunol.180.9.6132;
RA Takahashi M., Iwaki D., Kanno K., Ishida Y., Xiong J., Matsushita M.,
RA Endo Y., Miura S., Ishii N., Sugamura K., Fujita T.;
RT "Mannose-binding lectin (MBL)-associated serine protease (MASP)-1
RT contributes to activation of the lectin complement pathway.";
RL J. Immunol. 180:6132-6138(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
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 ECO:0000269|PubMed:18424734}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}.
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:8133044}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MASP-1;
CC IsoId=P98064-1; Sequence=Displayed;
CC Name=2; Synonyms=MASP-3;
CC IsoId=P98064-2; Sequence=VSP_036814, VSP_036815;
CC -!- TISSUE SPECIFICITY: Protein of the plasma which is primarily expressed
CC by liver. {ECO:0000269|PubMed:18424734, ECO:0000269|PubMed:8133044}.
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 (By
CC similarity). {ECO:0000250}.
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 -!- DISRUPTION PHENOTYPE: Mice are smaller and more vulnerable indicating
CC developmental and growth defects. Mice serum has low C4 and C3 cleavage
CC activity together with low MASP2 activation.
CC {ECO:0000269|PubMed:18424734}.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains a N-linked (GlcNAc...) asparagine
CC at position 538 Contains a N-linked (GlcNAc...) asparagine at position
CC 604. {ECO:0000250|UniProtKB:P48740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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; D16492; BAA03944.1; -; mRNA.
DR EMBL; AB049755; BAB69688.1; -; mRNA.
DR EMBL; AY135527; AAN39850.1; -; Genomic_DNA.
DR EMBL; AY135525; AAN39850.1; JOINED; Genomic_DNA.
DR EMBL; AK031598; BAC27469.1; -; mRNA.
DR EMBL; CH466521; EDK97670.1; -; Genomic_DNA.
DR EMBL; CH466521; EDK97671.1; -; Genomic_DNA.
DR EMBL; BC131637; AAI31638.1; -; mRNA.
DR EMBL; BC131638; AAI31639.1; -; mRNA.
DR CCDS; CCDS37303.1; -. [P98064-1]
DR CCDS; CCDS88904.1; -. [P98064-2]
DR PIR; PC1235; PC1235.
DR RefSeq; NP_032581.2; NM_008555.2. [P98064-1]
DR RefSeq; XP_006521891.1; XM_006521828.3.
DR AlphaFoldDB; P98064; -.
DR SMR; P98064; -.
DR BioGRID; 201316; 2.
DR STRING; 10090.ENSMUSP00000087327; -.
DR MEROPS; S01.132; -.
DR MEROPS; S01.198; -.
DR GlyGen; P98064; 4 sites.
DR iPTMnet; P98064; -.
DR PhosphoSitePlus; P98064; -.
DR CPTAC; non-CPTAC-3723; -.
DR MaxQB; P98064; -.
DR PaxDb; P98064; -.
DR PeptideAtlas; P98064; -.
DR PRIDE; P98064; -.
DR ProteomicsDB; 292089; -. [P98064-1]
DR ProteomicsDB; 292090; -. [P98064-2]
DR Antibodypedia; 889; 374 antibodies from 28 providers.
DR DNASU; 17174; -.
DR Ensembl; ENSMUST00000089883; ENSMUSP00000087327; ENSMUSG00000022887. [P98064-1]
DR Ensembl; ENSMUST00000229619; ENSMUSP00000155665; ENSMUSG00000022887. [P98064-2]
DR GeneID; 17174; -.
DR KEGG; mmu:17174; -.
DR UCSC; uc007ytr.1; mouse. [P98064-1]
DR UCSC; uc007yts.1; mouse. [P98064-2]
DR CTD; 5648; -.
DR MGI; MGI:88492; Masp1.
DR VEuPathDB; HostDB:ENSMUSG00000022887; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR HOGENOM; CLU_006842_14_1_1; -.
DR InParanoid; P98064; -.
DR OMA; RYSGFMA; -.
DR OrthoDB; 156878at2759; -.
DR PhylomeDB; P98064; -.
DR TreeFam; TF330373; -.
DR BRENDA; 3.4.21.B7; 3474.
DR Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR BioGRID-ORCS; 17174; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Masp1; mouse.
DR PRO; PR:P98064; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P98064; protein.
DR Bgee; ENSMUSG00000022887; Expressed in decidua and 167 other tissues.
DR ExpressionAtlas; P98064; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:MGI.
DR GO; GO:0001867; P:complement activation, lectin pathway; IMP:UniProtKB.
DR GO; GO:0045916; P:negative regulation of complement activation; ISO:MGI.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.290; -; 2.
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; 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 Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 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; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 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 Alternative splicing; Autocatalytic cleavage; Calcium;
KW Complement activation lectin pathway; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Hydroxylation;
KW Immunity; Innate immunity; Metal-binding; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..24
FT CHAIN 25..704
FT /note="Mannan-binding lectin serine protease 1"
FT /id="PRO_0000027595"
FT CHAIN 25..453
FT /note="Mannan-binding lectin serine protease 1 heavy chain"
FT /id="PRO_0000027596"
FT CHAIN 454..704
FT /note="Mannan-binding lectin serine protease 1 light chain"
FT /id="PRO_0000027597"
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 /evidence="ECO:0000250"
FT REGION 25..283
FT /note="Interaction with FCN2"
FT /evidence="ECO:0000250"
FT REGION 25..189
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
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 443
FT /note="V -> QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRVPNDKWFGSG
FT ALLSESWILTAAHVLRSQRRDNTVIPVSKEHVTVYLGLHDVRDKSGAVNSSAARVILHP
FT DFNIQNYNHDIALVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTV
FT DEIILSGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCL
FT GDSGGAFVIFDEMSQHWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPRA
FT VRDLQVER (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12847554,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036814"
FT VAR_SEQ 444..704
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12847554,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036815"
FT CONFLICT 257
FT /note="G -> A (in Ref. 5; AAI31638)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="E -> G (in Ref. 1; BAA03944 and 2; BAB69688)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="E -> K (in Ref. 1; BAA03944)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="M -> T (in Ref. 2; AAN39850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 79968 MW; 4CF0B17916C10961 CRC64;
MRFLSFWRLL LYHALCLALP EVSAHTVELN EMFGQIQSPG YPDSYPSDSE VTWNITVPEG
FRIKLYFMHF NLESSYLCEY DYVKVETEDQ VLATFCGRET TDTEQTPGQE VVLSPGTFMS
VTFRSDFSNE ERFTGFDAHY MAVDVDECKE REDEELSCDH YCHNYIGGYY CSCRFGYILH
TDNRTCRVEC SGNLFTQRTG TITSPDYPNP YPKSSECSYT IDLEEGFMVS LQFEDIFDIE
DHPEVPCPYD YIKIKAGSKV WGPFCGEKSP EPISTQTHSV QILFRSDNSG ENRGWRLSYR
AAGNECPKLQ PPVYGKIEPS QAVYSFKDQV LVSCDTGYKV LKDNEVMDTF QIECLKDGAW
SNKIPTCKIV DCGAPAGLKH GLVTFSTRNN LTTYKSEIRY SCQQPYYKML HNTTGVYTCS
AHGTWTNEVL KRSLPTCLPV CGVPKFSRKQ ISRIFNGRPA QKGTMPWIAM LSHLNGQPFC
GGSLLGSNWV LTAAHCLHQS LDPEEPTLHS SYLLSPSDFK IIMGKHWRRR SDEDEQHLHV
KRTTLHPLYN PSTFENDLGL VELSESPRLN DFVMPVCLPE QPSTEGTMVI VSGWGKQFLQ
RFPENLMEIE IPIVNSDTCQ EAYTPLKKKV TKDMICAGEK EGGKDACAGD SGGPMVTKDA
ERDQWYLVGV VSWGEDCGKK DRYGVYSYIY PNKDWIQRIT GVRN
