PLA2R_HUMAN
ID PLA2R_HUMAN Reviewed; 1463 AA.
AC Q13018; B2RTU9; D3DPB1; Q13019; Q15095; Q53R45; Q53RR7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
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=C-type lectin domain family 13 member C;
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=CLEC13C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, VARIANTS VAL-292 AND ASP-300, AND INTERACTION WITH PLA2G1B.
RC TISSUE=Kidney;
RX PubMed=7721806; DOI=10.1074/jbc.270.15.8963;
RA Ancian P., Lambeau G., Mattei M.-G., Lazdunski M.;
RT "The human 180-kDa receptor for secretory phospholipases A2. Molecular
RT cloning, identification of a secreted soluble form, expression, and
RT chromosomal localization.";
RL J. Biol. Chem. 270:8963-8970(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 532-942, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=9481783; DOI=10.1016/s0143-4004(98)90096-0;
RA Moses E.K., Freed K.A., Brennecke S.P., Rice G.E.;
RT "Distribution of the phospholipase A2 receptor messenger RNA in human
RT gestational tissues.";
RL Placenta 19:35-40(1998).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15611272; DOI=10.4049/jimmunol.174.1.464;
RA Granata F., Petraroli A., Boilard E., Bezzine S., Bollinger J.,
RA Del Vecchio L., Gelb M.H., Lambeau G., Marone G., Triggiani M.;
RT "Activation of cytokine production by secreted phospholipase A2 in human
RT lung macrophages expressing the M-type receptor.";
RL J. Immunol. 174:464-474(2005).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25335547; DOI=10.1038/srep06660;
RA Pan Y., Wan J., Liu Y., Yang Q., Liang W., Singhal P.C., Saleem M.A.,
RA Ding G.;
RT "sPLA2 IB induces human podocyte apoptosis via the M-type phospholipase A2
RT receptor.";
RL Sci. Rep. 4:6660-6660(2014).
CC -!- FUNCTION: Receptor for secretory phospholipase A2 (sPLA2). Acts as a
CC receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A.
CC Also able to bind to snake PA2-like toxins. Although its precise
CC function remains unclear, binding of sPLA2 to its receptor participates
CC in both positive and negative regulation of sPLA2 functions as well as
CC clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects
CC depending on the cell type, such as activation of the mitogen-activated
CC protein kinase (MAPK) cascade to induce cell proliferation, the
CC production of lipid mediators, selective release of arachidonic acid in
CC bone marrow-derived mast cells. In neutrophils, binding of sPLA2-
CC IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell
CC adhesion. May be involved in responses in pro-inflammatory cytokine
CC productions during endotoxic shock. Also has endocytic properties and
CC rapidly internalizes sPLA2 ligands, which is particularly important for
CC the clearance of extracellular sPLA2s to protect their potent enzymatic
CC activities. The soluble secretory phospholipase A2 receptor form is
CC circulating and acts as a negative regulator of sPLA2 functions by
CC blocking the biological functions of sPLA2-IB/PLA2G1B (PubMed:15611272,
CC PubMed:7721806). In podocytes, binding of sPLA2-IB/PLA2G1B can regulate
CC podocyte survival and glomerular homeostasis (PubMed:25335547).
CC {ECO:0000269|PubMed:15611272, ECO:0000269|PubMed:25335547,
CC ECO:0000269|PubMed:7721806}.
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:7721806). Interacts with
CC sPLA2-X/PLA2G10; this interaction mediates sPLA2-X/PLA2G10 clearance
CC and inactivation (By similarity). {ECO:0000250|UniProtKB:Q62028,
CC ECO:0000269|PubMed:7721806}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Soluble secretory phospholipase A2 receptor]:
CC Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13018-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13018-2; Sequence=VSP_029493, VSP_029494;
CC -!- TISSUE SPECIFICITY: Expressed in podocytes (at protein level)
CC (PubMed:25335547). Present in lung macrophage (at protein level).
CC Highly expressed in kidney. Also expressed in pancreas, amnion,
CC choriodecidua and placenta. Isoform 2 is expressed at much lower level.
CC {ECO:0000269|PubMed:15611272, ECO:0000269|PubMed:25335547,
CC ECO:0000269|PubMed:7721806, ECO:0000269|PubMed:7925459,
CC ECO:0000269|PubMed:9481783}.
CC -!- DOMAIN: C-type lectin domains 3-5 mediate the interaction with
CC phospholipase PLA2G1B.
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, or by alternative splicing, as in the
CC case of isoform 2 that shares all characteristics of secretory
CC phospholipase A2 receptor form (By similarity). {ECO:0000250}.
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_hum_Ctlect_253";
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; U17033; AAA70110.1; -; mRNA.
DR EMBL; U17034; AAC50163.1; -; mRNA.
DR EMBL; AC080166; AAY24052.1; -; Genomic_DNA.
DR EMBL; AC093873; AAY24190.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11392.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11393.1; -; Genomic_DNA.
DR EMBL; BC140823; AAI40824.1; -; mRNA.
DR EMBL; D30780; BAA06444.1; -; mRNA.
DR CCDS; CCDS33309.1; -. [Q13018-1]
DR CCDS; CCDS42767.1; -. [Q13018-2]
DR PIR; A56395; A56395.
DR PIR; B56395; B56395.
DR RefSeq; NP_001007268.1; NM_001007267.2. [Q13018-2]
DR RefSeq; NP_001182570.1; NM_001195641.1.
DR RefSeq; NP_031392.3; NM_007366.4. [Q13018-1]
DR RefSeq; XP_005246449.1; XM_005246392.3. [Q13018-1]
DR RefSeq; XP_011509122.1; XM_011510820.2. [Q13018-1]
DR RefSeq; XP_016859087.1; XM_017003598.1. [Q13018-1]
DR PDB; 6JLI; X-ray; 1.78 A; A=1108-1234.
DR PDBsum; 6JLI; -.
DR AlphaFoldDB; Q13018; -.
DR SMR; Q13018; -.
DR BioGRID; 116585; 2.
DR IntAct; Q13018; 2.
DR STRING; 9606.ENSP00000283243; -.
DR ChEMBL; CHEMBL3713395; -.
DR GlyConnect; 674; 1 N-Linked glycan (1 site).
DR GlyGen; Q13018; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q13018; -.
DR PhosphoSitePlus; Q13018; -.
DR BioMuta; PLA2R1; -.
DR DMDM; 160419241; -.
DR EPD; Q13018; -.
DR jPOST; Q13018; -.
DR MassIVE; Q13018; -.
DR PaxDb; Q13018; -.
DR PeptideAtlas; Q13018; -.
DR PRIDE; Q13018; -.
DR ProteomicsDB; 59106; -. [Q13018-1]
DR ProteomicsDB; 59107; -. [Q13018-2]
DR Antibodypedia; 2544; 242 antibodies from 26 providers.
DR DNASU; 22925; -.
DR Ensembl; ENST00000283243.13; ENSP00000283243.7; ENSG00000153246.13. [Q13018-1]
DR Ensembl; ENST00000392771.1; ENSP00000376524.1; ENSG00000153246.13. [Q13018-2]
DR GeneID; 22925; -.
DR KEGG; hsa:22925; -.
DR MANE-Select; ENST00000283243.13; ENSP00000283243.7; NM_007366.5; NP_031392.3.
DR UCSC; uc002ube.3; human. [Q13018-1]
DR CTD; 22925; -.
DR DisGeNET; 22925; -.
DR GeneCards; PLA2R1; -.
DR HGNC; HGNC:9042; PLA2R1.
DR HPA; ENSG00000153246; Tissue enhanced (salivary gland, thyroid gland).
DR MIM; 604939; gene.
DR neXtProt; NX_Q13018; -.
DR OpenTargets; ENSG00000153246; -.
DR PharmGKB; PA33369; -.
DR VEuPathDB; HostDB:ENSG00000153246; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; Q13018; -.
DR OMA; HKWISYM; -.
DR OrthoDB; 29241at2759; -.
DR PhylomeDB; Q13018; -.
DR TreeFam; TF316663; -.
DR PathwayCommons; Q13018; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q13018; -.
DR BioGRID-ORCS; 22925; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; PLA2R1; human.
DR GenomeRNAi; 22925; -.
DR Pharos; Q13018; Tbio.
DR PRO; PR:Q13018; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13018; protein.
DR Bgee; ENSG00000153246; Expressed in parotid gland and 155 other tissues.
DR Genevisible; Q13018; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA: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; IDA:UniProtKB.
DR GO; GO:1900139; P:negative regulation of arachidonic acid secretion; ISS:UniProtKB.
DR GO; GO:1900138; P:negative regulation of phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0090403; P:oxidative stress-induced premature senescence; IMP:UniProtKB.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:1904635; P:positive regulation of podocyte apoptotic process; IMP:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0090399; P:replicative senescence; IMP: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; 3.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endocytosis; Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..1463
FT /note="Secretory phospholipase A2 receptor"
FT /id="PRO_5000144349"
FT CHAIN 21..?
FT /note="Soluble secretory phospholipase A2 receptor"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311250"
FT TOPO_DOM 21..1397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1398..1418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1419..1463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..161
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 173..221
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 238..355
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 385..502
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 522..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 965..1096
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1121..1232
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1257..1378
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 1436..1442
FT /note="Endocytosis signal"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 51..64
FT /evidence="ECO:0000250"
FT DISULFID 89..106
FT /evidence="ECO:0000250"
FT DISULFID 178..204
FT /evidence="ECO:0000250"
FT DISULFID 192..219
FT /evidence="ECO:0000250"
FT DISULFID 260..354
FT /evidence="ECO:0000250"
FT DISULFID 330..346
FT /evidence="ECO:0000250"
FT DISULFID 406..501
FT /evidence="ECO:0000250"
FT DISULFID 478..493
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 1067..1087
FT /evidence="ECO:0000250"
FT DISULFID 1209..1223
FT /evidence="ECO:0000250"
FT DISULFID 1280..1377
FT /evidence="ECO:0000250"
FT DISULFID 1354..1369
FT /evidence="ECO:0000250"
FT VAR_SEQ 1323..1324
FT /note="NE -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7721806"
FT /id="VSP_029493"
FT VAR_SEQ 1325..1463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7721806"
FT /id="VSP_029494"
FT VARIANT 142
FT /note="R -> Q (in dbSNP:rs12327936)"
FT /id="VAR_037203"
FT VARIANT 177
FT /note="P -> S (in dbSNP:rs13394676)"
FT /id="VAR_037204"
FT VARIANT 279
FT /note="I -> V (in dbSNP:rs965290)"
FT /id="VAR_037205"
FT VARIANT 292
FT /note="M -> V (in dbSNP:rs3749117)"
FT /evidence="ECO:0000269|PubMed:7721806"
FT /id="VAR_037206"
FT VARIANT 300
FT /note="H -> D (in dbSNP:rs35771982)"
FT /evidence="ECO:0000269|PubMed:7721806"
FT /id="VAR_037207"
FT VARIANT 370
FT /note="A -> E (in dbSNP:rs34916310)"
FT /id="VAR_061354"
FT VARIANT 404
FT /note="R -> H (in dbSNP:rs33985939)"
FT /id="VAR_037208"
FT VARIANT 1106
FT /note="G -> S (in dbSNP:rs3828323)"
FT /id="VAR_037209"
FT CONFLICT 15..17
FT /note="APR -> GAA (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..64
FT /note="ENC -> GRTGS (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 521..523
FT /note="RHG -> ETC (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="S -> P (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="A -> P (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 1224
FT /note="E -> D (in Ref. 1; AAA70110/AAC50163)"
FT /evidence="ECO:0000305"
FT CONFLICT 1263
FT /note="S -> K (in Ref. 1; AAA70110)"
FT /evidence="ECO:0000305"
FT STRAND 1118..1121
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1124..1133
FT /evidence="ECO:0007829|PDB:6JLI"
FT HELIX 1135..1144
FT /evidence="ECO:0007829|PDB:6JLI"
FT HELIX 1155..1168
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1172..1177
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1198..1200
FT /evidence="ECO:0007829|PDB:6JLI"
FT HELIX 1202..1204
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1208..1212
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1218..1221
FT /evidence="ECO:0007829|PDB:6JLI"
FT STRAND 1227..1233
FT /evidence="ECO:0007829|PDB:6JLI"
SQ SEQUENCE 1463 AA; 168600 MW; 4E65EA5AC5D597E2 CRC64;
MLLSPSLLLL LLLGAPRGCA EGVAAALTPE RLLEWQDKGI FVIQSESLKK CIQAGKSVLT
LENCKQANKH MLWKWVSNHG LFNIGGSGCL GLNFSAPEQP LSLYECDSTL VSLRWRCNRK
MITGPLQYSV QVAHDNTVVA SRKYIHKWIS YGSGGGDICE YLHKDLHTIK GNTHGMPCMF
PFQYNHQWHH ECTREGREDD LLWCATTSRY ERDEKWGFCP DPTSAEVGCD TIWEKDLNSH
ICYQFNLLSS LSWSEAHSSC QMQGGTLLSI TDETEENFIR EHMSSKTVEV WMGLNQLDEH
AGWQWSDGTP LNYLNWSPEV NFEPFVEDHC GTFSSFMPSA WRSRDCESTL PYICKKYLNH
IDHEIVEKDA WKYYATHCEP GWNPYNRNCY KLQKEEKTWH EALRSCQADN SALIDITSLA
EVEFLVTLLG DENASETWIG LSSNKIPVSF EWSNDSSVIF TNWHTLEPHI FPNRSQLCVS
AEQSEGHWKV KNCEERLFYI CKKAGHVLSD AESGCQEGWE RHGGFCYKID TVLRSFDQAS
SGYYCPPALV TITNRFEQAF ITSLISSVVK MKDSYFWIAL QDQNDTGEYT WKPVGQKPEP
VQYTHWNTHQ PRYSGGCVAM RGRHPLGRWE VKHCRHFKAM SLCKQPVENQ EKAEYEERWP
FHPCYLDWES EPGLASCFKV FHSEKVLMKR TWREAEAFCE EFGAHLASFA HIEEENFVNE
LLHSKFNWTE ERQFWIGFNK RNPLNAGSWE WSDRTPVVSS FLDNTYFGED ARNCAVYKAN
KTLLPLHCGS KREWICKIPR DVKPKIPFWY QYDVPWLFYQ DAEYLFHTFA SEWLNFEFVC
SWLHSDLLTI HSAHEQEFIH SKIKALSKYG ASWWIGLQEE RANDEFRWRD GTPVIYQNWD
TGRERTVNNQ SQRCGFISSI TGLWGSEECS VSMPSICKRK KVWLIEKKKD TPKQHGTCPK
GWLYFNYKCL LLNIPKDPSS WKNWTHAQHF CAEEGGTLVA IESEVEQAFI TMNLFGQTTS
VWIGLQNDDY ETWLNGKPVV YSNWSPFDII NIPSHNTTEV QKHIPLCALL SSNPNFHFTG
KWYFEDCGKE GYGFVCEKMQ DTSGHGVNTS DMYPMPNTLE YGNRTYKIIN ANMTWYAAIK
TCLMHKAQLV SITDQYHQSF LTVVLNRLGY AHWIGLFTTD NGLNFDWSDG TKSSFTFWKD
EESSLLGDCV FADSNGRWHS TACESFLQGA ICHVPPETRQ SEHPELCSET SIPWIKFKSN
CYSFSTVLDS MSFEAAHEFC KKEGSNLLTI KDEAENAFLL EELFAFGSSV QMVWLNAQFD
GNNETIKWFD GTPTDQSNWG IRKPDTDYFK PHHCVALRIP EGLWQLSPCQ EKKGFICKME
ADIHTAEALP EKGPSHSIIP LAVVLTLIVI VAICTLSFCI YKHNGGFFRR LAGFRNPYYP
ATNFSTVYLE ENILISDLEK SDQ
