APOBR_HUMAN
ID APOBR_HUMAN Reviewed; 1097 AA.
AC Q0VD83; H3BU97; Q0VD81; Q8NC15; Q9NPJ9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Apolipoprotein B receptor {ECO:0000305};
DE AltName: Full=Apolipoprotein B-100 receptor;
DE AltName: Full=Apolipoprotein B-48 receptor;
DE Short=Apolipoprotein B48 receptor;
DE Short=apoB-48R;
GN Name=APOBR {ECO:0000312|HGNC:HGNC:24087}; Synonyms=APOB48R;
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] (ISOFORM 4), PROTEIN SEQUENCE OF
RP 823-830; 866-877 AND 919-928, FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP ALA-428 AND 352-GLU--GLY-360 DEL.
RC TISSUE=Monocytic leukemia, and Placenta;
RX PubMed=10852956; DOI=10.1073/pnas.120184097;
RA Brown M.L., Ramprasad M.P., Umeda P.K., Tanaka A., Kobayashi Y.,
RA Watanabe T., Shimoyamada H., Kuo W.-L., Li R., Song R., Bradley W.A.,
RA Gianturco S.H.;
RT "A macrophage receptor for apolipoprotein B48: cloning, expression, and
RT atherosclerosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7488-7493(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 2), AND VARIANTS
RP ALA-428 AND 352-GLU--GLY-360 DEL.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 765-1097 (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PROTEIN SEQUENCE OF 919-928, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP POST-TRANSLATIONAL MODIFICATION.
RX PubMed=10191299;
RA Bradley W.A., Brown M.L., Ramprasad M.P., Li R., Song R., Gianturco S.H.;
RT "Antipeptide antibodies reveal interrelationships of MBP 200 and MBP 235:
RT unique apoB-specific receptors for triglyceride-rich lipoproteins on human
RT monocyte-macrophages.";
RL J. Lipid Res. 40:744-752(1999).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=7619811; DOI=10.1021/bi00028a023;
RA Ramprasad M.P., Li R., Bradley W.A., Gianturco S.H.;
RT "Human THP-1 monocyte-macrophage membrane binding proteins: distinct
RT receptor(s) for triglyceride-rich lipoproteins.";
RL Biochemistry 34:9126-9135(1995).
RN [7]
RP FUNCTION.
RX PubMed=9633939; DOI=10.1161/01.atv.18.6.968;
RA Gianturco S.H., Ramprasad M.P., Song R., Li R., Brown M.L., Bradley W.A.;
RT "Apolipoprotein B-48 or its apolipoprotein B-100 equivalent mediates the
RT binding of triglyceride-rich lipoproteins to their unique human monocyte-
RT macrophage receptor.";
RL Arterioscler. Thromb. Vasc. Biol. 18:968-976(1998).
RN [8]
RP INDUCTION.
RX PubMed=12700342; DOI=10.1194/jlr.m300077-jlr200;
RA Haraguchi G., Kobayashi Y., Brown M.L., Tanaka A., Isobe M.,
RA Gianturco S.H., Bradley W.A.;
RT "PPAR(alpha) and PPAR(gamma) activators suppress the monocyte-macrophage
RT apoB-48 receptor.";
RL J. Lipid Res. 44:1224-1231(2003).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=15591219; DOI=10.1161/01.atv.0000152632.48937.2d;
RA Kawakami A., Tani M., Chiba T., Yui K., Shinozaki S., Nakajima K.,
RA Tanaka A., Shimokado K., Yoshida M.;
RT "Pitavastatin inhibits remnant lipoprotein-induced macrophage foam cell
RT formation through ApoB48 receptor-dependent mechanism.";
RL Arterioscler. Thromb. Vasc. Biol. 25:424-429(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-572, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP VARIANT ALA-428.
RX PubMed=15830122; DOI=10.1007/s10038-005-0240-1;
RA Fujita Y., Ezura Y., Bujo H., Nakajima T., Takahashi K., Kamimura K.,
RA Iino Y., Katayama Y., Saito Y., Emi M.;
RT "Association of nucleotide variations in the apolipoprotein B48 receptor
RT gene (APOB48R) with hypercholesterolemia.";
RL J. Hum. Genet. 50:203-209(2005).
CC -!- FUNCTION: Macrophage receptor that binds to the apolipoprotein B48
CC (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a
CC like domain of APOB in hypertriglyceridemic very low density
CC lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the
CC context of the macrophage. May provide essential lipids to
CC reticuloendothelial cells. Could also be involved in foam cell
CC formation with elevated TRL and remnant lipoprotein (RLP). Mediates the
CC rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and
CC trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages.
CC {ECO:0000269|PubMed:10852956, ECO:0000269|PubMed:15591219,
CC ECO:0000269|PubMed:9633939}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10191299,
CC ECO:0000269|PubMed:7619811}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10191299, ECO:0000269|PubMed:7619811}. Note=Binds
CC monocyte-macrophage membrane. Thought to be anchored in the membrane
CC through an interaction with an integral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=4;
CC IsoId=Q0VD83-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VD83-2; Sequence=VSP_060193;
CC Name=3;
CC IsoId=Q0VD83-3; Sequence=VSP_060194;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes > bone
CC marrow = spleen > lymph node, and only faintly visible in appendix and
CC thymus. Expressed in the brain, heart, kidney, liver, lung, pancreas,
CC and placenta. Expressed primarily by reticuloendothelial cells:
CC monocytes, macrophages, and endothelial cells. Expressed in
CC atherosclerotic lesion foam cells. {ECO:0000269|PubMed:10191299,
CC ECO:0000269|PubMed:10852956}.
CC -!- INDUCTION: Suppressed significantly by PPARA and PPARG in THP-1 and
CC blood-borne monocyte-macrophages. Decreased after pitavastatin
CC treatment in peripheral blood macrophages and remnant lipoprotein
CC (RLP)-induced foam cell formation. {ECO:0000269|PubMed:12700342,
CC ECO:0000269|PubMed:15591219}.
CC -!- PTM: There are 2 forms in macrophages, the membrane-binding proteins
CC 200 kDa (MBP 200) and 235 kDa (MBP 235), that can be reduced into a
CC single active ligand-binding species with intermediate mobility (MBP
CC 200R). {ECO:0000269|PubMed:7619811}.
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DR EMBL; AF141332; AAF76255.1; -; mRNA.
DR EMBL; AF141333; AAF76256.1; -; Genomic_DNA.
DR EMBL; AC138894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119786; AAI19787.1; -; mRNA.
DR EMBL; BC119788; AAI19789.1; -; mRNA.
DR EMBL; AK075085; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58442.1; -. [Q0VD83-4]
DR RefSeq; NP_061160.3; NM_018690.3. [Q0VD83-4]
DR AlphaFoldDB; Q0VD83; -.
DR BioGRID; 120996; 2.
DR IntAct; Q0VD83; 3.
DR STRING; 9606.ENSP00000457539; -.
DR DrugBank; DB14003; alpha-Tocopherol acetate.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11635; Tocofersolan.
DR DrugBank; DB11251; Tocopherol.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; Q0VD83; -.
DR PhosphoSitePlus; Q0VD83; -.
DR BioMuta; APOBR; -.
DR DMDM; 519668661; -.
DR EPD; Q0VD83; -.
DR jPOST; Q0VD83; -.
DR MassIVE; Q0VD83; -.
DR MaxQB; Q0VD83; -.
DR PaxDb; Q0VD83; -.
DR PeptideAtlas; Q0VD83; -.
DR PRIDE; Q0VD83; -.
DR ProteomicsDB; 42868; -.
DR ProteomicsDB; 58813; -. [Q0VD83-2]
DR ProteomicsDB; 58814; -. [Q0VD83-3]
DR Antibodypedia; 26469; 237 antibodies from 22 providers.
DR DNASU; 55911; -.
DR Ensembl; ENST00000564831.6; ENSP00000457539.1; ENSG00000184730.12. [Q0VD83-4]
DR GeneID; 55911; -.
DR KEGG; hsa:55911; -.
DR MANE-Select; ENST00000564831.6; ENSP00000457539.1; NM_018690.4; NP_061160.3.
DR UCSC; uc002dqb.2; human. [Q0VD83-4]
DR CTD; 55911; -.
DR DisGeNET; 55911; -.
DR GeneCards; APOBR; -.
DR HGNC; HGNC:24087; APOBR.
DR HPA; ENSG00000184730; Group enriched (bone marrow, intestine, lung, lymphoid tissue).
DR MIM; 605220; gene.
DR neXtProt; NX_Q0VD83; -.
DR OpenTargets; ENSG00000184730; -.
DR VEuPathDB; HostDB:ENSG00000184730; -.
DR eggNOG; ENOG502SSHE; Eukaryota.
DR GeneTree; ENSGT00530000065031; -.
DR HOGENOM; CLU_006101_0_0_1; -.
DR InParanoid; Q0VD83; -.
DR OMA; RVWVLEE; -.
DR OrthoDB; 248102at2759; -.
DR PhylomeDB; Q0VD83; -.
DR TreeFam; TF337147; -.
DR PathwayCommons; Q0VD83; -.
DR Reactome; R-HSA-8964046; VLDL clearance.
DR SignaLink; Q0VD83; -.
DR BioGRID-ORCS; 55911; 21 hits in 1080 CRISPR screens.
DR ChiTaRS; APOBR; human.
DR GenomeRNAi; 55911; -.
DR Pharos; Q0VD83; Tbio.
DR PRO; PR:Q0VD83; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q0VD83; protein.
DR Bgee; ENSG00000184730; Expressed in monocyte and 96 other tissues.
DR ExpressionAtlas; Q0VD83; baseline and differential.
DR Genevisible; Q0VD83; HS.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR InterPro; IPR026158; ApolipoprotB_rcpt.
DR PANTHER; PTHR15964; PTHR15964; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Atherosclerosis; Cell membrane;
KW Cholesterol metabolism; Chylomicron; Direct protein sequencing; LDL;
KW Lipid metabolism; Lipid transport; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Transport; VLDL.
FT CHAIN 1..1097
FT /note="Apolipoprotein B receptor"
FT /id="PRO_0000327263"
FT REGION 64..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBT6"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBT6"
FT VAR_SEQ 1..471
FT /note="Missing (in isoform 2)"
FT /id="VSP_060193"
FT VAR_SEQ 1056..1097
FT /note="SPLRHDGTPVPARRRPLGHGFGLAHPGMMQELQARLGRPKPQ -> RWEDRL
FT RPGVRDQPGQHSKIPIF (in isoform 3)"
FT /id="VSP_060194"
FT VARIANT 352..360
FT /note="Missing (in dbSNP:rs148114931)"
FT /evidence="ECO:0000269|PubMed:10852956,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_081733"
FT VARIANT 428
FT /note="P -> A (in dbSNP:rs180743)"
FT /evidence="ECO:0000269|PubMed:10852956,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15830122"
FT /id="VAR_042432"
FT CONFLICT 340
FT /note="A -> S (in Ref. 1; AAF76255/AAF76256)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="E -> Q (in Ref. 1; AAF76255/AAF76256)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="V -> A (in Ref. 1; AAF76255/AAF76256, 3; AAI19787/
FT AAI19789 and 4; AK075085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1097 AA; 115634 MW; 55BADDAD96EB16E1 CRC64;
MDFLRLYLPG LHQALRGALD SLGTFVSYLL GDAVPTVERE AQAAEELGVV AVGKTGKIVE
EEAQEDLEGL RGSQNEGAGR LRGPGDDRRH EVGSSAVEQT WGWGDGSSHG SQAERQDSGA
GETAKAARCQ EPSAHLEARK KSKAGSGACQ DRSGQAQERQ ESHEQEVNRE ERLRSWEQEE
EEEEVRAREP GMARGAESEW TWHGETEGKA GAVGPKAAGD NREMEQGVRE ADAGETEEPG
AEGAGKGEEV VVVEKACEST RAWGTWGPGA EPEDWGILGR EEARTTPGRE EARAILDGEE
ARTISGGEEA ETASGGEEAE TASGGEEAGT ASGGEEAGIA SGGEAGTASG GEEAGTASGG
EEAGTASGGD EAWTTSGKEE ADLLGVRQTE YGAVPGERLL EATGKVWVLE EEGDEEREAE
VSPFPKQPQV LGTERTEEAA ESQTAGREAV GGQEAGESFE GQVDLRGKEA EMRQDLGIRA
DRARMEELVQ AEEAQEERGS SRDPVAELPS DGEAEGTADL EATPEARPEE ELTGEESEAA
QTSCGLLGVE WGGLTHSVTK GQGPELMGGA QTPTKQPEER EAGEVELMGV LALSKEEQER
SLEAGPRHAG SVKPEASEAF PGAWENRTRK DMERGNTQED AADGEQREEE ETAGGQTLAA
EAEGDRESEL SEVPEAGGEG LTTQDAGCGT EEGEASVSEN QELDGSTGAD AGPCPSLGEA
YARETEDEEA EADRTSRRGW RLQAVAVGLP DREDAQTGSV AAGIMGGDVV PHISAAGAGE
ALEGVLGQGW DSKEKEEAAA GEHAGGQEFG LEGSAEEEVT GRGSQVEAFE SREGGPWGGR
VEAEESAGAE DSCGLDPAGS QTARAEGMGA MVEAGGLLEK WTLLEEEAVG WQEREQREDS
EGRCGDYHPE GEAPRLLDAE GLMVTGGRRA EAKETEPESL EHVRGQEEQP THQAPAEAAP
ESVGEAETAE AMGSARGGAA NSWSEAPLPG SLLDVSVPRS RVHLSRSSSQ RRSRPSFRRT
PAWEQQEEPP APNPPEEELS APEQRPLQLE EPLEPSPLRH DGTPVPARRR PLGHGFGLAH
PGMMQELQAR LGRPKPQ
