SO2A1_HUMAN
ID SO2A1_HUMAN Reviewed; 643 AA.
AC Q92959; Q86V98; Q8IUN2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Solute carrier organic anion transporter family member 2A1 {ECO:0000305};
DE AltName: Full=Prostaglandin transporter;
DE Short=PGT;
DE AltName: Full=Solute carrier family 21 member 2;
GN Name=SLCO2A1 {ECO:0000312|HGNC:HGNC:10955}; Synonyms=OATP2A1, SLC21A2;
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 [GENOMIC DNA / MRNA], VARIANT THR-396, TRANSPORTER
RP ACTIVITY, AND FUNCTION.
RX PubMed=8787677; DOI=10.1172/jci118897;
RA Lu R., Kanai N., Bao Y., Schuster V.L.;
RT "Cloning, in vitro expression, and tissue distribution of a human
RT prostaglandin transporter cDNA(hPGT).";
RL J. Clin. Invest. 98:1142-1149(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-396.
RX PubMed=9618293; DOI=10.1006/bbrc.1998.8715;
RA Lu R., Schuster V.L.;
RT "Molecular cloning of the gene for the human prostaglandin transporter
RT hPGT: gene organization, promoter activity, and chromosomal localization.";
RL Biochem. Biophys. Res. Commun. 246:805-812(1998).
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].
RC TISSUE=Brain, and Prostate;
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 TISSUE SPECIFICITY, AND VARIANT PHOAR2 SER-557.
RX PubMed=22331663; DOI=10.1002/humu.22042;
RA Seifert W., Kuhnisch J., Tuysuz B., Specker C., Brouwers A., Horn D.;
RT "Mutations in the prostaglandin transporter encoding gene SLCO2A1 cause
RT primary hypertrophic osteoarthropathy and isolated digital clubbing.";
RL Hum. Mutat. 33:660-664(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP VARIANTS PHOAR2 ARG-222 AND GLU-255.
RX PubMed=22197487; DOI=10.1016/j.ajhg.2011.11.019;
RA Zhang Z., Xia W., He J., Zhang Z., Ke Y., Yue H., Wang C., Zhang H., Gu J.,
RA Hu W., Fu W., Hu Y., Li M., Liu Y.;
RT "Exome sequencing identifies SLCO2A1 mutations as a cause of primary
RT hypertrophic osteoarthropathy.";
RL Am. J. Hum. Genet. 90:125-132(2012).
RN [8]
RP VARIANTS PHOAR2 PHE-85; HIS-97; ALA-181; ASP-181; LEU-204; ARG-222; PHE-420
RP AND GLY-565, VARIANT CYS-445, AND CHARACTERIZATION OF VARIANT PHOAR2
RP PHE-420.
RX PubMed=22553128; DOI=10.1002/humu.22111;
RA Diggle C.P., Parry D.A., Logan C.V., Laissue P., Rivera C., Restrepo C.M.,
RA Fonseca D.J., Morgan J.E., Allanore Y., Fontenay M., Wipff J., Varret M.,
RA Gibault L., Dalantaeva N., Korbonits M., Zhou B., Yuan G., Harifi G.,
RA Cefle K., Palanduz S., Akoglu H., Zwijnenburg P.J., Lichtenbelt K.D.,
RA Aubry-Rozier B., Superti-Furga A., Dallapiccola B., Accadia M.,
RA Brancati F., Sheridan E.G., Taylor G.R., Carr I.M., Johnson C.A.,
RA Markham A.F., Bonthron D.T.;
RT "Prostaglandin transporter mutations cause pachydermoperiostosis with
RT myelofibrosis.";
RL Hum. Mutat. 33:1175-1181(2012).
RN [9]
RP VARIANTS PHOAR2 ARG-255 AND HIS-556.
RX PubMed=22696055; DOI=10.1038/jid.2012.146;
RA Busch J., Frank V., Bachmann N., Otsuka A., Oji V., Metze D., Shah K.,
RA Danda S., Watzer B., Traupe H., Bolz H.J., Kabashima K., Bergmann C.;
RT "Mutations in the prostaglandin transporter SLCO2A1 cause primary
RT hypertrophic osteoarthropathy with digital clubbing.";
RL J. Invest. Dermatol. 132:2473-2476(2012).
RN [10]
RP VARIANTS PHOAR2 165-GLU--ILE-643 DEL; ARG-222; ASP-369; GLU-379 AND
RP LYS-465, AND INVOLVEMENT IN PHOAD.
RX PubMed=23509104; DOI=10.1210/jc.2012-3568;
RA Zhang Z., He J.W., Fu W.Z., Zhang C.Q., Zhang Z.L.;
RT "Mutations in the SLCO2A1 gene and primary hypertrophic osteoarthropathy: a
RT clinical and biochemical characterization.";
RL J. Clin. Endocrinol. Metab. 98:E923-E933(2013).
RN [11]
RP VARIANTS PHOAR2 ARG-181; 207-TYR--ILE-643 DEL; ARG-255; SER-328 AND
RP LEU-374, VARIANTS PHOAD ARG-222; ASP-369; ARG-554 AND 603-ARG--ILE-643 DEL,
RP AND INVOLVEMENT IN PHOAD.
RX PubMed=33852188; DOI=10.1002/jbmr.4310;
RA Xu Y., Zhang Z., Yue H., Li S., Zhang Z.;
RT "Monoallelic mutations in SLCO2A1 cause autosomal dominant primary
RT hypertrophic osteoarthropathy.";
RL J. Bone Miner. Res. 36:1459-1468(2021).
CC -!- FUNCTION: Transports PGD2, as well as PGE1, PGE2 and PGF2A. Mediates
CC the clearance of prostaglandins from the circulation through uptake
CC across cell membrane which allows cytoplasmic oxidation and
CC prostaglandin signal termination (PubMed:8787677). May mediate the
CC release of newly synthesized prostaglandins from cells and the
CC transepithelial transport of prostaglandins (Probable).
CC {ECO:0000269|PubMed:8787677, ECO:0000305|PubMed:8787677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin D2(out) = prostaglandin D2(in);
CC Xref=Rhea:RHEA:50976, ChEBI:CHEBI:57406;
CC Evidence={ECO:0000269|PubMed:8787677};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin E1(out) = prostaglandin E1(in);
CC Xref=Rhea:RHEA:50980, ChEBI:CHEBI:57397;
CC Evidence={ECO:0000269|PubMed:8787677};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000269|PubMed:8787677};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in);
CC Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404;
CC Evidence={ECO:0000269|PubMed:8787677};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thromboxane B2(out) = thromboxane B2(in);
CC Xref=Rhea:RHEA:50992, ChEBI:CHEBI:90696;
CC Evidence={ECO:0000269|PubMed:8787677};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8787677};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Significant expression observed in
CC ling, kidney, spleen, and heart. {ECO:0000269|PubMed:22331663}.
CC -!- DISEASE: Hypertrophic osteoarthropathy, primary, autosomal recessive, 2
CC (PHOAR2) [MIM:614441]: A disease characterized by digital clubbing,
CC periostosis, acroosteolysis, painful joint enlargement, and variable
CC features of pachydermia that include thickened facial skin and a
CC thickened scalp. Other developmental anomalies include delayed closure
CC of the cranial sutures and congenital heart disease.
CC {ECO:0000269|PubMed:22197487, ECO:0000269|PubMed:22331663,
CC ECO:0000269|PubMed:22553128, ECO:0000269|PubMed:22696055,
CC ECO:0000269|PubMed:23509104, ECO:0000269|PubMed:33852188}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Hypertrophic osteoarthropathy, primary, autosomal dominant
CC (PHOAD) [MIM:167100]: A form of primary hypertrophic osteoarthropathy,
CC a disease characterized by digital clubbing, periostosis,
CC acroosteolysis, painful joint enlargement, and variable features of
CC pachydermia that include thickened facial skin and a thickened scalp.
CC PHOAD patients may also experience joint swelling and pain, and some
CC have reported gastrointestinal symptoms, including watery diarrhea.
CC Males are more commonly affected, and more severely affected, than
CC females. {ECO:0000269|PubMed:23509104, ECO:0000269|PubMed:33852188}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Solute carrier organic anion transporter family,
CC member 2A1 (SLCO2A1); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/SLCO2A1";
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DR EMBL; U70867; AAC09469.1; -; mRNA.
DR EMBL; AF056732; AAC62004.1; -; Genomic_DNA.
DR EMBL; AF056719; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056720; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056721; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056722; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056723; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056724; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056725; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056726; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056727; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056728; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056729; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056730; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; AF056731; AAC62004.1; JOINED; Genomic_DNA.
DR EMBL; CH471052; EAW79156.1; -; Genomic_DNA.
DR EMBL; BC041140; AAH41140.2; -; mRNA.
DR EMBL; BC051347; AAH51347.1; -; mRNA.
DR CCDS; CCDS3084.1; -.
DR RefSeq; NP_005621.2; NM_005630.2.
DR PDB; 3MRR; X-ray; 1.60 A; P=178-187.
DR PDBsum; 3MRR; -.
DR AlphaFoldDB; Q92959; -.
DR SMR; Q92959; -.
DR IntAct; Q92959; 1.
DR STRING; 9606.ENSP00000311291; -.
DR BindingDB; Q92959; -.
DR ChEMBL; CHEMBL2073703; -.
DR DrugBank; DB00770; Alprostadil.
DR DrugBank; DB04557; Arachidonic Acid.
DR DrugBank; DB04551; beta-D-fructofuranose 1,6-bisphosphate.
DR DrugBank; DB02263; D-glyceraldehyde 3-phosphate.
DR DrugBank; DB01160; Dinoprost tromethamine.
DR DrugBank; DB00917; Dinoprostone.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB03581; Glucose-6-Phosphate.
DR DrugBank; DB01088; Iloprost.
DR DrugBank; DB04398; Lactic acid.
DR DrugBank; DB00654; Latanoprost.
DR DrugBank; DB01174; Phenobarbital.
DR DrugBank; DB01819; Phosphoenolpyruvate.
DR DrugBank; DB02056; Prostaglandin D2.
DR DrugBank; DB00119; Pyruvic acid.
DR DrugBank; DB11753; Rifamycin.
DR SwissLipids; SLP:000001646; -.
DR TCDB; 2.A.60.1.19; the organo anion transporter (oat) family.
DR GlyGen; Q92959; 3 sites.
DR iPTMnet; Q92959; -.
DR PhosphoSitePlus; Q92959; -.
DR BioMuta; SLCO2A1; -.
DR DMDM; 218511799; -.
DR EPD; Q92959; -.
DR jPOST; Q92959; -.
DR MassIVE; Q92959; -.
DR PaxDb; Q92959; -.
DR PeptideAtlas; Q92959; -.
DR PRIDE; Q92959; -.
DR ProteomicsDB; 75631; -.
DR Antibodypedia; 33384; 75 antibodies from 16 providers.
DR DNASU; 6578; -.
DR Ensembl; ENST00000310926.11; ENSP00000311291.4; ENSG00000174640.15.
DR GeneID; 6578; -.
DR KEGG; hsa:6578; -.
DR MANE-Select; ENST00000310926.11; ENSP00000311291.4; NM_005630.3; NP_005621.2.
DR UCSC; uc003eqa.4; human.
DR CTD; 6578; -.
DR DisGeNET; 6578; -.
DR GeneCards; SLCO2A1; -.
DR HGNC; HGNC:10955; SLCO2A1.
DR HPA; ENSG00000174640; Tissue enhanced (lung).
DR MalaCards; SLCO2A1; -.
DR MIM; 167100; phenotype.
DR MIM; 601460; gene.
DR MIM; 614441; phenotype.
DR neXtProt; NX_Q92959; -.
DR OpenTargets; ENSG00000174640; -.
DR Orphanet; 468641; Chronic enteropathy associated with SLCO2A1 gene.
DR Orphanet; 2796; Pachydermoperiostosis.
DR PharmGKB; PA35840; -.
DR VEuPathDB; HostDB:ENSG00000174640; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR InParanoid; Q92959; -.
DR OMA; ISWKVKR; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q92959; -.
DR TreeFam; TF317540; -.
DR PathwayCommons; Q92959; -.
DR Reactome; R-HSA-5619095; Defective SLCO2A1 causes primary, autosomal recessive hypertrophic osteoarthropathy 2 (PHOAR2).
DR Reactome; R-HSA-879518; Transport of organic anions.
DR SignaLink; Q92959; -.
DR BioGRID-ORCS; 6578; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; SLCO2A1; human.
DR EvolutionaryTrace; Q92959; -.
DR GeneWiki; SLCO2A1; -.
DR GenomeRNAi; 6578; -.
DR Pharos; Q92959; Tchem.
DR PRO; PR:Q92959; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92959; protein.
DR Bgee; ENSG00000174640; Expressed in right lung and 167 other tissues.
DR ExpressionAtlas; Q92959; baseline and differential.
DR Genevisible; Q92959; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005319; F:lipid transporter activity; TAS:ProtInc.
DR GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; TAS:ProtInc.
DR GO; GO:0015732; P:prostaglandin transport; IBA:GO_Central.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW Lipid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..643
FT /note="Solute carrier organic anion transporter family
FT member 2A1"
FT /id="PRO_0000191058"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..279
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..343
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..387
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..415
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..541
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..576
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..610
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..629
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 438..496
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 444..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 450..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 459..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VARIANT 85
FT /note="I -> F (in PHOAR2; dbSNP:rs387907296)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068636"
FT VARIANT 97
FT /note="R -> H (in PHOAR2; dbSNP:rs1376989560)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068637"
FT VARIANT 165..643
FT /note="Missing (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:23509104"
FT /id="VAR_085955"
FT VARIANT 181
FT /note="G -> A (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068638"
FT VARIANT 181
FT /note="G -> D (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068639"
FT VARIANT 181
FT /note="G -> R (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085956"
FT VARIANT 204
FT /note="S -> L (in PHOAR2; dbSNP:rs555934769)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068640"
FT VARIANT 207..643
FT /note="Missing (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085957"
FT VARIANT 222
FT /note="G -> R (in PHOAR2 and PHOAD; dbSNP:rs774795340)"
FT /evidence="ECO:0000269|PubMed:22197487,
FT ECO:0000269|PubMed:22553128, ECO:0000269|PubMed:23509104,
FT ECO:0000269|PubMed:33852188"
FT /id="VAR_067598"
FT VARIANT 255
FT /note="G -> E (in PHOAR2; dbSNP:rs387906806)"
FT /evidence="ECO:0000269|PubMed:22197487"
FT /id="VAR_067599"
FT VARIANT 255
FT /note="G -> R (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22696055,
FT ECO:0000269|PubMed:33852188"
FT /id="VAR_068641"
FT VARIANT 328
FT /note="F -> S (in PHOAR2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085958"
FT VARIANT 369
FT /note="G -> D (in PHOAR2 and PHOAD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23509104,
FT ECO:0000269|PubMed:33852188"
FT /id="VAR_085959"
FT VARIANT 374
FT /note="P -> L (in PHOAR2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085960"
FT VARIANT 379
FT /note="G -> E (in PHOAR2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23509104"
FT /id="VAR_085961"
FT VARIANT 396
FT /note="A -> T (in dbSNP:rs34550074)"
FT /evidence="ECO:0000269|PubMed:8787677,
FT ECO:0000269|PubMed:9618293"
FT /id="VAR_053674"
FT VARIANT 420
FT /note="C -> F (in PHOAR2; reduced activity;
FT dbSNP:rs387907295)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068642"
FT VARIANT 445
FT /note="R -> C (in dbSNP:rs146970901)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068643"
FT VARIANT 465
FT /note="E -> K (in PHOAR2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23509104"
FT /id="VAR_085962"
FT VARIANT 554
FT /note="G -> R (in PHOAD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085963"
FT VARIANT 556
FT /note="Q -> H (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22696055"
FT /id="VAR_068644"
FT VARIANT 557
FT /note="F -> S (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22331663"
FT /id="VAR_068352"
FT VARIANT 565
FT /note="W -> G (in PHOAR2)"
FT /evidence="ECO:0000269|PubMed:22553128"
FT /id="VAR_068645"
FT VARIANT 603..643
FT /note="Missing (in PHOAD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33852188"
FT /id="VAR_085964"
FT CONFLICT 9
FT /note="A -> V (in Ref. 1; AAC09469 and 2; AAC62004)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="V -> I (in Ref. 1; AAC09469 and 2; AAC62004)"
FT /evidence="ECO:0000305"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3MRR"
SQ SEQUENCE 643 AA; 70044 MW; A1FF933246480984 CRC64;
MGLLPKLGAS QGSDTSTSRA GRCARSVFGN IKVFVLCQGL LQLCQLLYSA YFKSSLTTIE
KRFGLSSSSS GLISSLNEIS NAILIIFVSY FGSRVHRPRL IGIGGLFLAA GAFILTLPHF
LSEPYQYTLA STGNNSRLQA ELCQKHWQDL PPSKCHSTTQ NPQKETSSMW GLMVVAQLLA
GIGTVPIQPF GISYVDDFSE PSNSPLYISI LFAISVFGPA FGYLLGSVML QIFVDYGRVN
TAAVNLVPGD PRWIGAWWLG LLISSALLVL TSFPFFFFPR AMPIGAKRAP ATADEARKLE
EAKSRGSLVD FIKRFPCIFL RLLMNSLFVL VVLAQCTFSS VIAGLSTFLN KFLEKQYGTS
AAYANFLIGA VNLPAAALGM LFGGILMKRF VFSLQAIPRI ATTIITISMI LCVPLFFMGC
STPTVAEVYP PSTSSSIHPQ SPACRRDCSC PDSIFHPVCG DNGIEYLSPC HAGCSNINMS
SATSKQLIYL NCSCVTGGSA SAKTGSCPVP CAHFLLPAIF LISFVSLIAC ISHNPLYMMV
LRVVNQEEKS FAIGVQFLLM RLLAWLPSPA LYGLTIDHSC IRWNSLCLGR RGACAYYDND
ALRDRYLGLQ MGYKALGMLL LCFISWRVKK NKEYNVQKAA GLI
