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   24-JAN-2024, entry version 162.
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   GlyCosmos; Q62028; 6 sites, No reported glycans.
DR   GlyGen; Q62028; 6 sites.
DR   PhosphoSitePlus; Q62028; -.
DR   MaxQB; Q62028; -.
DR   PaxDb; 10090-ENSMUSP00000108144; -.
DR   PeptideAtlas; Q62028; -.
DR   ProteomicsDB; 289611; -. [Q62028-1]
DR   ProteomicsDB; 289612; -. [Q62028-2]
DR   Pumba; Q62028; -.
DR   Antibodypedia; 2544; 256 antibodies from 26 providers.
DR   DNASU; 18779; -.
DR   Ensembl; ENSMUST00000112525.5; ENSMUSP00000108144.4; ENSMUSG00000054580.15. [Q62028-1]
DR   GeneID; 18779; -.
DR   KEGG; mmu:18779; -.
DR   UCSC; uc008jug.2; mouse. [Q62028-1]
DR   UCSC; uc008juh.2; mouse. [Q62028-2]
DR   AGR; MGI:102468; -.
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; GGDICEH; -.
DR   OrthoDB; 4271106at2759; -.
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 78 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 179 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; cd00037; CLECT; 8.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR   PANTHER; PTHR22803:SF74; SECRETORY PHOSPHOLIPASE A2 RECEPTOR; 1.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00059; Lectin_C; 8.
DR   PRINTS; PR00013; FNTYPEII.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 8.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
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.
DR   Genevisible; Q62028; MM.
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
//