PLA2R_MOUSE
ID PLA2R_MOUSE Reviewed; 1487 AA.
AC Q62028; A2AS64; B9EJ68; Q80ZL5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Secretory phospholipase A2 receptor;
DE Short=PLA2-R;
DE Short=PLA2R;
DE AltName: Full=180 kDa secretory phospholipase A2 receptor;
DE AltName: Full=M-type receptor;
DE Contains:
DE RecName: Full=Soluble secretory phospholipase A2 receptor;
DE Short=Soluble PLA2-R;
DE Short=Soluble PLA2R;
DE Flags: Precursor;
GN Name=Pla2r1; Synonyms=Pla2g1br;
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), FUNCTION, DOMAIN, AND TISSUE
RP SPECIFICITY.
RX PubMed=7925459; DOI=10.1111/j.1432-1033.1994.00375.x;
RA Higashino K., Ishizaki J., Kishino J., Ohara O., Arita H.;
RT "Structural comparison of phospholipase-A2-binding regions in
RT phospholipase-A2 receptors from various mammals.";
RL Eur. J. Biochem. 225:375-382(1994).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9407054; DOI=10.1074/jbc.272.52.32792;
RA Hanasaki K., Yokota Y., Ishizaki J., Itoh T., Arita H.;
RT "Resistance to endotoxic shock in phospholipase A2 receptor-deficient
RT mice.";
RL J. Biol. Chem. 272:32792-32797(1997).
RN [5]
RP FUNCTION, AND INTERACTION WITH PLA2G1B.
RX PubMed=10066760; DOI=10.1074/jbc.274.11.7043;
RA Cupillard L., Mulherkar R., Gomez N., Kadam S., Valentin E., Lazdunski M.,
RA Lambeau G.;
RT "Both group IB and group IIA secreted phospholipases A2 are natural ligands
RT of the mouse 180-kDa M-type receptor.";
RL J. Biol. Chem. 274:7043-7051(1999).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10864436; DOI=10.1006/abbi.2000.1849;
RA Yokota Y., Ikeda M., Higashino K., Nakano K., Fujii N., Arita H.,
RA Hanasaki K.;
RT "Enhanced tissue expression and elevated circulating level of phospholipase
RT A(2) receptor during murine endotoxic shock.";
RL Arch. Biochem. Biophys. 379:7-17(2000).
RN [7]
RP FUNCTION.
RX PubMed=11019817; DOI=10.1006/abbi.2000.1977;
RA Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K.,
RA Fujii N., Ishizaki J., Arita H., Hanasaki K.;
RT "Mouse group X secretory phospholipase A2 induces a potent release of
RT arachidonic acid from spleen cells and acts as a ligand for the
RT phospholipase A2 receptor.";
RL Arch. Biochem. Biophys. 381:31-42(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH PLA2G10.
RX PubMed=10922494; DOI=10.1016/s0014-5793(00)01848-2;
RA Yokota Y., Higashino K., Nakano K., Arita H., Hanasaki K.;
RT "Identification of group X secretory phospholipase A(2) as a natural ligand
RT for mouse phospholipase A(2) receptor.";
RL FEBS Lett. 478:187-191(2000).
RN [9]
RP FUNCTION.
RX PubMed=10946309; DOI=10.4049/jimmunol.165.5.2773;
RA Fonteh A.N., Atsumi G., LaPorte T., Chilton F.H.;
RT "Secretory phospholipase A2 receptor-mediated activation of cytosolic
RT phospholipase A2 in murine bone marrow-derived mast cells.";
RL J. Immunol. 165:2773-2782(2000).
RN [10]
RP FUNCTION.
RX PubMed=11481246; DOI=10.1096/fj.00-0831fje;
RA Mandal A.K., Zhang Z., Chou J.Y., Mukherjee A.B.;
RT "Pancreatic phospholipase A2 via its receptor regulates expression of key
RT enzymes of phospholipid and sphingolipid metabolism.";
RL FASEB J. 15:1834-1836(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH PLA2G10.
RX PubMed=11741598; DOI=10.1016/s0014-5793(01)03173-8;
RA Yokota Y., Notoya M., Higashino K., Ishimoto Y., Nakano K., Arita H.,
RA Hanasaki K.;
RT "Clearance of group X secretory phospholipase A(2) via mouse phospholipase
RT A(2) receptor.";
RL FEBS Lett. 509:250-254(2001).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12225974; DOI=10.1152/ajpcell.00608.2001;
RA Silliman C.C., Moore E.E., Zallen G., Gonzalez R., Johnson J.L., Elzi D.J.,
RA Meng X., Hanasaki K., Ishizaki J., Arita H., Ao L., England K.M.,
RA Banerjee A.;
RT "Presence of the M-type sPLA(2) receptor on neutrophils and its role in
RT elastase release and adhesion.";
RL Am. J. Physiol. 283:C1102-C1113(2002).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND POSSIBLE PROTEOLYTIC PROCESSING.
RX PubMed=11830583; DOI=10.1074/jbc.m108752200;
RA Higashino Ki K., Yokota Y., Ono T., Kamitani S., Arita H., Hanasaki K.;
RT "Identification of a soluble form phospholipase A2 receptor as a
RT circulating endogenous inhibitor for secretory phospholipase A2.";
RL J. Biol. Chem. 277:13583-13588(2002).
RN [14]
RP FUNCTION.
RX PubMed=16815622; DOI=10.1016/j.biochi.2006.06.008;
RA Prijatelj P., Vardjan N., Rowan E.G., Krizaj I., Pungercar J.;
RT "Binding to the high-affinity M-type receptor for secreted phospholipases
RT A(2) is not obligatory for the presynaptic neurotoxicity of ammodytoxin
RT A.";
RL Biochimie 88:1425-1433(2006).
RN [15]
RP FUNCTION.
RX PubMed=17279628; DOI=10.1021/bi062119b;
RA Rouault M., Le Calvez C., Boilard E., Surrel F., Singer A., Ghomashchi F.,
RA Bezzine S., Scarzello S., Bollinger J., Gelb M.H., Lambeau G.;
RT "Recombinant production and properties of binding of the full set of mouse
RT secreted phospholipases A2 to the mouse M-type receptor.";
RL Biochemistry 46:1647-1662(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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: Receptor for secretory phospholipase A2 (sPLA2). Acts as a
CC receptor for phospholipases sPLA2-IB/PLA2G1B, sPLA2-X/PLA2G10 and, with
CC lower affinity, sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like
CC toxins. Although its precise function remains unclear, binding of sPLA2
CC to its receptor participates in both positive and negative regulation
CC of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-
CC IB/PLA2G1B induces various effects depending on the cell type, such as
CC activation of the mitogen-activated protein kinase (MAPK) cascade to
CC induce cell proliferation, the production of lipid mediators, selective
CC release of arachidonic acid in bone marrow-derived mast cells. In
CC neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to
CC stimulate elastase release and cell adhesion. May be involved in
CC responses in pro-inflammatory cytokine productions during endotoxic
CC shock. Also has endocytic properties and rapidly internalizes sPLA2
CC ligands, which is particularly important for the clearance of
CC extracellular sPLA2s to protect their potent enzymatic activities. The
CC soluble secretory phospholipase A2 receptor form is circulating and
CC acts as a negative regulator of sPLA2 functions by blocking the
CC biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10. In
CC podocytes, binding of sPLA2-IB/PLA2G1B can regulate podocyte survival
CC and glomerular homeostasis. {ECO:0000250|UniProtKB:Q13018,
CC ECO:0000269|PubMed:10066760, ECO:0000269|PubMed:10922494,
CC ECO:0000269|PubMed:10946309, ECO:0000269|PubMed:11019817,
CC ECO:0000269|PubMed:11481246, ECO:0000269|PubMed:11741598,
CC ECO:0000269|PubMed:11830583, ECO:0000269|PubMed:12225974,
CC ECO:0000269|PubMed:16815622, ECO:0000269|PubMed:17279628,
CC ECO:0000269|PubMed:7925459, ECO:0000269|PubMed:9407054}.
CC -!- SUBUNIT: Interacts with sPLA2-IB/PLA2G1B; this interaction mediates
CC intracellular signaling as well as clearance of extracellular sPLA2-
CC IB/PLA2G1B via endocytotic pathway (PubMed:10066760). Interacts with
CC sPLA2-X/PLA2G10; this interaction mediates sPLA2-X/PLA2G10 clearance
CC and inactivation (PubMed:10922494, PubMed:11741598).
CC {ECO:0000269|PubMed:10066760, ECO:0000269|PubMed:10922494,
CC ECO:0000269|PubMed:11741598}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11830583};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11830583}.
CC -!- SUBCELLULAR LOCATION: [Soluble secretory phospholipase A2 receptor]:
CC Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62028-2; Sequence=VSP_029495, VSP_029496;
CC -!- TISSUE SPECIFICITY: Widely expressed. Present in type II alveolar
CC epithelial cells and a subset of splenic lymphocytes. Present at the
CC surface of polymorphonuclear neutrophils (at protein level).
CC {ECO:0000269|PubMed:10864436, ECO:0000269|PubMed:12225974,
CC ECO:0000269|PubMed:7925459}.
CC -!- INDUCTION: Following exposure to endotoxin (at protein level).
CC {ECO:0000269|PubMed:10864436}.
CC -!- DOMAIN: C-type lectin domains 3-5 mediate the interaction with
CC phospholipase PLA2G1B. {ECO:0000269|PubMed:7925459}.
CC -!- DOMAIN: The endocytosis signal probably mediates endocytosis via
CC clathrin-coated pits. {ECO:0000250}.
CC -!- PTM: The secretory phospholipase A2 receptor form may be produced by
CC the action of metalloproteinases. It contains all extracellular domains
CC and only lacks transmembrane and cytosolic regions. It is however
CC unclear whether this form is produced by proteolytic cleavage as
CC suggested by some experiments reported by PubMed:11830583, or by
CC alternative splicing.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and without evident
CC histopathological abnormalities. After challenge with bacterial
CC lipopolysaccharide (LPS), they exhibit longer survival than wild-type
CC mice. They are also resistant to lethal effects of exogenous sPLA2-
CC IB/PLA2G1B after sensitization with sublethal dose of LPS, suggesting a
CC potential role in the progression of endotoxic shock.
CC {ECO:0000269|PubMed:9407054}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM22305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM23630.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Phospholipase A2 receptor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_356";
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DR EMBL; D30779; BAA06443.1; -; mRNA.
DR EMBL; BX679662; CAM22305.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL928546; CAM22305.1; JOINED; Genomic_DNA.
DR EMBL; AL928546; CAM23630.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX679662; CAM23630.1; JOINED; Genomic_DNA.
DR EMBL; BC048780; AAH48780.1; -; mRNA.
DR EMBL; BC141355; AAI41356.1; -; mRNA.
DR EMBL; BC141356; AAI41357.1; -; mRNA.
DR CCDS; CCDS16059.1; -. [Q62028-1]
DR PIR; S48719; S48719.
DR RefSeq; NP_032893.1; NM_008867.2. [Q62028-1]
DR AlphaFoldDB; Q62028; -.
DR SMR; Q62028; -.
DR BioGRID; 202218; 2.
DR STRING; 10090.ENSMUSP00000108144; -.
DR GlyGen; Q62028; 6 sites.
DR PhosphoSitePlus; Q62028; -.
DR MaxQB; Q62028; -.
DR PaxDb; Q62028; -.
DR PeptideAtlas; Q62028; -.
DR PRIDE; Q62028; -.
DR ProteomicsDB; 289611; -. [Q62028-1]
DR ProteomicsDB; 289612; -. [Q62028-2]
DR Antibodypedia; 2544; 242 antibodies from 26 providers.
DR DNASU; 18779; -.
DR Ensembl; ENSMUST00000112525; ENSMUSP00000108144; ENSMUSG00000054580. [Q62028-1]
DR GeneID; 18779; -.
DR KEGG; mmu:18779; -.
DR UCSC; uc008jug.2; mouse. [Q62028-1]
DR UCSC; uc008juh.2; mouse. [Q62028-2]
DR CTD; 22925; -.
DR MGI; MGI:102468; Pla2r1.
DR VEuPathDB; HostDB:ENSMUSG00000054580; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; Q62028; -.
DR OMA; HKWISYM; -.
DR PhylomeDB; Q62028; -.
DR TreeFam; TF316663; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 18779; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pla2r1; mouse.
DR PRO; PR:Q62028; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62028; protein.
DR Bgee; ENSMUSG00000054580; Expressed in retinal neural layer and 178 other tissues.
DR Genevisible; Q62028; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0043274; F:phospholipase binding; IPI:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:1900139; P:negative regulation of arachidonic acid secretion; IDA:UniProtKB.
DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0090403; P:oxidative stress-induced premature senescence; ISS:UniProtKB.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; ISS:UniProtKB.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 8.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 8.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endocytosis;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..1487
FT /note="Secretory phospholipase A2 receptor"
FT /id="PRO_5000139804"
FT CHAIN 27..?
FT /note="Soluble secretory phospholipase A2 receptor"
FT /evidence="ECO:0000305"
FT /id="PRO_0000311251"
FT TOPO_DOM 27..1396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1397..1417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1418..1487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..165
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 176..224
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 241..357
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 387..504
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 524..643
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 673..797
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 819..938
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 964..1095
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1120..1231
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1256..1377
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1463..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1435..1441
FT /note="Endocytosis signal"
FT COMPBIAS 1463..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..68
FT /evidence="ECO:0000250"
FT DISULFID 93..110
FT /evidence="ECO:0000250"
FT DISULFID 181..207
FT /evidence="ECO:0000250"
FT DISULFID 195..222
FT /evidence="ECO:0000250"
FT DISULFID 263..356
FT /evidence="ECO:0000250"
FT DISULFID 333..348
FT /evidence="ECO:0000250"
FT DISULFID 408..503
FT /evidence="ECO:0000250"
FT DISULFID 480..495
FT /evidence="ECO:0000250"
FT DISULFID 617..634
FT /evidence="ECO:0000250"
FT DISULFID 699..796
FT /evidence="ECO:0000250"
FT DISULFID 774..788
FT /evidence="ECO:0000250"
FT DISULFID 840..937
FT /evidence="ECO:0000250"
FT DISULFID 914..929
FT /evidence="ECO:0000250"
FT DISULFID 1066..1086
FT /evidence="ECO:0000250"
FT DISULFID 1208..1222
FT /evidence="ECO:0000250"
FT DISULFID 1279..1376
FT /evidence="ECO:0000250"
FT DISULFID 1353..1368
FT /evidence="ECO:0000250"
FT VAR_SEQ 680..689
FT /note="VFHSEKVLMK -> DTGKAVLDWI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029495"
FT VAR_SEQ 690..1487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029496"
SQ SEQUENCE 1487 AA; 170512 MW; AD8D905859B0EDE8 CRC64;
MVQWLAMLQL LWLQQLLLLG IHQGIAQDLT HIQEPSLEWR DKGIFIIQSE SLKTCIQAGK
SVLTLENCKQ PNEHMLWKWV SDDHLFNVGG SGCLGLNISA LEQPLKLYEC DSTLISLRWH
CDRKMIEGPL QYKVQVKSDN TVVARKQIHR WIAYTSSGGD ICEHPSRDLY TLKGNAHGMP
CVFPFQFKGH WHHDCIREGQ KEHLLWCATT SRYEEDEKWG FCPDPTSMKV FCDATWQRNG
SSRICYQFNL LSSLSWNQAH SSCLMQGGAL LSIADEDEED FIRKHLSKVV KEVWIGLNQL
DEKAGWQWSD GTPLSYLNWS QEITPGPFVE HHCGTLEVVS AAWRSRDCES TLPYICKRDL
NHTAQGILEK DSWKYHATHC DPDWTPFNRK CYKLKKDRKS WLGALHSCQS NDSVLMDVAS
LAEVEFLVSL LRDENASETW IGLSSNKIPV SFEWSSGSSV IFTNWYPLEP RILPNRRQLC
VSAEESDGRW KVKDCKERLF YICKKAGQVP ADEQSGCPAG WERHGRFCYK IDTVLRSFEE
ASSGYYCSPA LLTITSRFEQ AFITSLISSV AEKDSYFWIA LQDQNNTGEY TWKTVGQREP
VQYTYWNTRQ PSNRGGCVVV RGGSSLGRWE VKDCSDFKAM SLCKTPVKIW EKTELEERWP
FHPCYMDWES ATGLASCFKV FHSEKVLMKR SWREAEAFCE EFGAHLASFA HIEEENFVNE
LLHSKFNWTQ ERQFWIGFNR RNPLNAGSWA WSDGSPVVSS FLDNAYFEED AKNCAVYKAN
KTLLPSNCAS KHEWICRIPR DVRPKFPDWY QYDAPWLFYQ NAEYLFHTHP AEWATFEFVC
GWLRSDFLTI YSAQEQEFIH SKIKGLTKYG VKWWIGLEEG GARDQIQWSN GSPVIFQNWD
KGREERVDSQ RKRCVFISSI TGLWGTENCS VPLPSICKRV KIWVIEKEKP PTQPGTCPKG
WLYFNYKCFL VTIPKDPREL KTWTGAQEFC VAKGGTLVSI KSELEQAFIT MNLFGQTTNV
WIGLQSTNHE KWVNGKPLVY SNWSPSDIIN IPSYNTTEFQ KHIPLCALMS SNPNFHFTGK
WYFDDCGKEG YGFVCEKMQD TLEHHVNVSD TSAIPSTLEY GNRTYKIIRG NMTWYAAGKS
CRMHRAELAS IPDAFHQAFL TVLLSRLGHT HWIGLSTTDN GQTFDWSDGT KSPFTYWKDE
ESAFLGDCAF ADTNGRWHST ACESFLQGAI CHVVTETKAF EHPGLCSETS VPWIKFKGNC
YSFSTVLDSR SFEDAHEFCK SEGSNLLAIR DAAENSFLLE ELLAFGSSVQ MVWLNAQFDN
NNKTLRWFDG TPTEQSNWGL RKPDMDHLKP HPCVVLRIPE GIWHFTPCED KKGFICKMEA
GIPAVTAQPE KGLSHSIVPV TVTLTLIIAL GIFMLCFWIY KQKSDIFQRL TGSRGSYYPT
LNFSTAHLEE NILISDLEKN TNDEEVRDAP ATESKRGHKG RPICISP
