APOB_MOUSE
ID APOB_MOUSE Reviewed; 4505 AA.
AC E9Q414; Q3UH74; Q497D8; Q61314; Q61318; Q8CGG8;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Apolipoprotein B-100;
DE Short=Apo B-100;
DE Contains:
DE RecName: Full=Apolipoprotein B-48;
DE Short=Apo B-48;
DE Flags: Precursor;
GN Name=Apob;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1477 AND 3004-4505.
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2734-3518.
RX PubMed=2332175; DOI=10.1016/0378-1119(90)90319-m;
RA Smith T.J., Hautamaa D., Maeda N.;
RT "Sequence of the putative low-density lipoprotein receptor-binding regions
RT of apolipoprotein B in mouse and hamster.";
RL Gene 87:309-310(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2962-4505.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2773 AND ASN-2976.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Apolipoprotein B is a major protein constituent of
CC chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-
CC 100 functions as a recognition signal for the cellular binding and
CC internalization of LDL particles by the apoB/E receptor.
CC -!- SUBUNIT: Interacts with PCSK9. Interacts with MTTP. Interacts with
CC AUP1. {ECO:0000250|UniProtKB:P04114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
CC Secreted {ECO:0000250|UniProtKB:P04114}. Lipid droplet
CC {ECO:0000250|UniProtKB:P04114}.
CC -!- PTM: Palmitoylated; structural requirement for proper assembly of the
CC hydrophobic core of the lipoprotein particle. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=2179 {ECO:0000250}; Note=The stop codon
CC (UAA) at position 2179 is created by RNA editing. Apo B-48, derived
CC from the fully edited RNA, is produced only in the intestine and is
CC found in chylomicrons. Apo B-48 is a shortened form of apo B-100 which
CC lacks the LDL-receptor region. The unedited version (apo B-100) is
CC produced by the liver and is found in the VLDL and LDL (By similarity).
CC {ECO:0000250};
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI41358.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI41361.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE27983.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC163900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038263; AAH38263.1; -; mRNA.
DR EMBL; BC100607; AAI00608.1; -; mRNA.
DR EMBL; BC141357; AAI41358.1; ALT_INIT; mRNA.
DR EMBL; BC141360; AAI41361.1; ALT_INIT; mRNA.
DR EMBL; M35186; AAA37246.1; -; Genomic_DNA.
DR EMBL; X15191; CAA33265.1; -; Genomic_DNA.
DR EMBL; AK147540; BAE27983.1; ALT_INIT; mRNA.
DR CCDS; CCDS49022.1; -.
DR RefSeq; NP_033823.2; NM_009693.2.
DR BioGRID; 231944; 13.
DR STRING; 10090.ENSMUSP00000036044; -.
DR GlyGen; E9Q414; 14 sites.
DR iPTMnet; E9Q414; -.
DR PhosphoSitePlus; E9Q414; -.
DR CPTAC; non-CPTAC-5577; -.
DR EPD; E9Q414; -.
DR jPOST; E9Q414; -.
DR MaxQB; E9Q414; -.
DR PaxDb; E9Q414; -.
DR PeptideAtlas; E9Q414; -.
DR PRIDE; E9Q414; -.
DR ProteomicsDB; 296268; -.
DR Antibodypedia; 4232; 1071 antibodies from 41 providers.
DR Ensembl; ENSMUST00000037811; ENSMUSP00000036044; ENSMUSG00000020609.
DR GeneID; 238055; -.
DR KEGG; mmu:238055; -.
DR UCSC; uc007mzf.2; mouse.
DR CTD; 338; -.
DR MGI; MGI:88052; Apob.
DR VEuPathDB; HostDB:ENSMUSG00000020609; -.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00590000083139; -.
DR InParanoid; E9Q414; -.
DR OMA; DYEMMIK; -.
DR OrthoDB; 5350at2759; -.
DR TreeFam; TF331316; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR Reactome; R-MMU-3000497; Scavenging by Class H Receptors.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8866423; VLDL assembly.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8963901; Chylomicron remodeling.
DR Reactome; R-MMU-8964026; Chylomicron clearance.
DR Reactome; R-MMU-8964038; LDL clearance.
DR Reactome; R-MMU-8964041; LDL remodeling.
DR Reactome; R-MMU-8964046; VLDL clearance.
DR Reactome; R-MMU-9707616; Heme signaling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 238055; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Apob; mouse.
DR PRO; PR:E9Q414; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; E9Q414; protein.
DR Bgee; ENSMUSG00000020609; Expressed in small intestine Peyer's patch and 69 other tissues.
DR ExpressionAtlas; E9Q414; baseline and differential.
DR Genevisible; E9Q414; MM.
DR GO; GO:0042627; C:chylomicron; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034359; C:mature chylomicron; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0031983; C:vesicle lumen; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0035473; F:lipase binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IGI:MGI.
DR GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IGI:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0030301; P:cholesterol transport; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IDA:MGI.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IGI:MGI.
DR GO; GO:0042159; P:lipoprotein catabolic process; IGI:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0042953; P:lipoprotein transport; IMP:MGI.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:MGI.
DR GO; GO:0009743; P:response to carbohydrate; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:MGI.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:MGI.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR022176; ApoB100_C.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR Pfam; PF12491; ApoB100_C; 1.
DR Pfam; PF06448; DUF1081; 1.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol metabolism; Chylomicron; Coiled coil; Cytoplasm;
KW Disulfide bond; Glycoprotein; Heparin-binding; LDL; Lipid droplet;
KW Lipid metabolism; Lipid transport; Lipoprotein; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; RNA editing; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transport; VLDL.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..4505
FT /note="Apolipoprotein B-100"
FT /id="PRO_0000420969"
FT CHAIN 28..2178
FT /note="Apolipoprotein B-48"
FT /id="PRO_0000420970"
FT DOMAIN 46..672
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT REGION 32..126
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 232..306
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 902..959
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 2042..2177
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3155..3230
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3168..3178
FT /note="Basic (possible receptor binding region)"
FT /evidence="ECO:0000250"
FT REGION 3368..3388
FT /note="LDL receptor binding"
FT /evidence="ECO:0000250"
FT REGION 3378..3511
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3381..3389
FT /note="Basic (possible receptor binding region)"
FT /evidence="ECO:0000250"
FT MOD_RES 2005
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT MOD_RES 3273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT MOD_RES 4013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 2976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 3095
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 78..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 186..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 245..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 385..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 478..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 966..976
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT CONFLICT 41..42
FT /note="KD -> N (in Ref. 2; AAI00608)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..332
FT /note="EL -> KK (in Ref. 2; AAI00608)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="L -> K (in Ref. 2; AAI00608)"
FT /evidence="ECO:0000305"
FT CONFLICT 1477
FT /note="Q -> K (in Ref. 2; AAH38263)"
FT /evidence="ECO:0000305"
FT CONFLICT 3265
FT /note="S -> R (in Ref. 3; AAA37246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4505 AA; 509432 MW; 09EADB2D499E7A82 CRC64;
MGPRKPALRT PLLLLFLLLF LDTSVWAQDE VLENLSFSCP KDATRFKHLR KYVYNYEAES
SSGVQGTADS RSATKINCKV ELEVPQICGF IMRTNQCTLK EVYGFNPEGK ALMKKTKNSE
EFAAAMSRYE LKLAIPEGKQ IVLYPDKDEP KYILNIKRGI ISALLVPPET EEDQQELFLD
TVYGNCSTQV TVNSRKGTVP TEMSTERNLQ QCDGFQPIST SVSPLALIKG LVHPLSTLIS
SSQTCQYTLD PKRKHVSEAV CDEQHLFLPF SYKNKYGIMT RVTQKLSLED TPKINSRFFS
EGTNRMGLAF ESTKSTSSPK QADAVLKTLQ ELKKLSISEQ NAQRANLFNK LVTELRGLTG
EAITSLLPQL IEVSSPITLQ ALVQCGQPQC YTHILQWLKT EKAHPLLVDI VTYLMALIPN
PSTQRLQEIF NTAKEQQSRA TLYALSHAVN SYFDVDHSRS PVLQDIAGYL LKQIDNECTG
NEDHTFLILR VIGNMGRTME QVMPALKSSV LSCVRSTKPS LLIQKAALQA LRKMELEDEV
RTILFDTFVN GVAPVEKRLA AYLLLMKNPS SSDINKIAQL LQWEQSEQVK NFVASHIANI
LNSEELYVQD LKVLIKNALE NSQFPTIMDF RKFSRNYQIS KSASLPMFDP VSVKIEGNLI
FDPSSYLPRE SLLKTTLTVF GLASLDLFEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY
WVNGRVPDGV SKVLVDHFGY TTDGKHEQDM VNGIMPIVDK LIKDLKSKEI PEARAYLRIL
GKELSFVRLQ DLQVLGKLLL SGAQTLQGIP QMVVQAIREG SKNDLFLHYI FMDNAFELPT
GAGLQLQVSS SGVFTPGIKA GVRLELANIQ AELVAKPSVS LEFVTNMGII IPDFAKSSVQ
MNTNFFHESG LEARVALKAG QLKVIIPSPK RPVKLFSGSN TLHLVSTTKT EVIPPLVENR
QSWSTCKPLF TGMNYCTTGA YSNASSTESA SYYPLTGDTR YELELRPTGE VEQYSATATY
ELLKEDKSLV DTLKFLVQAE GVQQSEATVL FKYNRRSRTL SSEVLIPGFD VNFGTILRVN
DESAKDKNTY KLILDIQNKK ITEVSLVGHL SYDKKGDGKI KGVVSIPRLQ AEARSEVHTH
WSSTKLLFQM DSSATAYGST ISKRVTWRYD NEIIEFDWNT GTNVDTKKVA SNFPVDLSHY
PRMLHEYANG LLDHRVPQTD VTFRDMGSKL IVATNTWLQM ATRGLPYPQT LQDHLNSLSE
LNLLKMGLSD FHIPDNLFLK TDGRVKYTMN RNKINIDIPL PLGGKSSKDL KMPESVRTPA
LNFKSVGFHL PSREVQVPTF TIPKTHQLQV PLLGVLDLST NVYSNLYNWS ASYTGGNTSR
DHFSLQAQYR MKTDSVVDLF SYSVQGSGET TYDSKNTFTL SCDGSLHHKF LDSKFKVSHV
EKFGNSPVSK GLLTFETSSA LGPQMSATVH LDSKKKQHLY VKDIKVDGQF RASSFYAQGK
YGLSCERDVT TGQLSGESNM RFNSTYFQGT NQIVGMYQDG ALSITSTSDL QDGIFKNTAS
LKYENYELTL KSDSSGQYEN FAASNKLDVT FSTQSALLRS EHQANYKSLR LVTLLSGSLT
SQGVELNADI LGTDKINTGA HKATLKIARD GLSTSATTNL KYSPLLLENE LNAELGLSGA
SMKLSTNGRF KEHHAKFSLD GRAALTEVSL GSIYQAMILG ADSKNIFNFK LSREGLRLSN
DLMGSYAEMK LDHTHSLNIA GLSLDFFSKM DNIYSGDKFY KQNFNLQLQP YSFITTLSND
LRYGALDLTN NGRFRLEPLK LNVGGNFKGT YQNNELKHIY TISYTDLVVA SYRADTVAKV
QGVEFSHRLN ADIEGLTSSV DVTTSYNSDP LHFNNVFHFS LAPFTLGIDT HTSGDGKLSF
WGEHTGQLYS KFLLKAEPLA LIVSHDYKGS TSHSLPYESS ISTALEHTVS ALLTPAEQTS
TWKFKTKLND KVYSQDFEAY NTKDKIGVEL SGRADLSGLY SPIKLPFFYS EPVNVLNGLE
VNDAVDKPQE FTIIAVVKYD KNQDVHTINL PFFKSLPDYL ERNRRGMISL LEAMRGELQR
LSVDQFVRKY RAALSRLPQQ IHHYLNASDW ERQVAGAKEK ITSFMENYRI TDNDVLIAID
SAKINFNEKL SQLETYAIQF DQYIKDNYDP HDLKRTIAEI IDRIIEKLKI LDEQYHIRVN
LAKSIHNLYL FVENVDLNQV SSSNTSWIQN VDSNYQVRIQ IQEKLQQLRT QIQNIDIQQL
AAEVKRQMDA IDVTMHLDQL RTAILFQRIS DIIDRVKYFV MNLIEDFKVT EKINTFRVIV
RELIEKYEVD QHIQVLMDKS VELAHRYSLS EPLQKLSNVL QRIEIKDYYE KLVGFIDDTV
EWLKALSFKN TIEELNRLTD MLVKKLKAFD YHQFVDKTNS KIREMTQRIN AEIQALKLPQ
KMEALKLLVE DFKTTVSNSL ERLKDTKVTV VIDWLQDILT QMKDHFQDTL EDVRDRIYQM
DIQRELEHFL SLVNQVYSTL VTYMSDWWTL TAKNITDFAE QYSIQNWAES IKVLVEQGFI
VPEMQTFLWT MPAFEVSLRA LQEGNFQTPV FIVPLTDLRI PSIRINFKML KNIKIPLRFS
TPEFTLLNTF HVHSFTIDLL EIKAKIIRTI DQILSSELQW PLPEMYLRDL DVVNIPLARL
TLPDFHVPEI TIPEFTIPNV NLKDLHVPDL HIPEFQLPHL SHTIEIPAFG KLHSILKIQS
PLFILDANAN IQNVTTSGNK AEIVASVTAK GESQFEALNF DFQAQAQFLE LNPHPPVLKE
SMNFSSKHVR MEHEGEIVFD GKAIEGKSDT VASLHTEKNE VEFNNGMTVK VNNQLTLDSH
TKYFHKLSVP RLDFSSKASL NNEIKTLLEA GHVALTSSGT GSWNWACPNF SDEGIHSSQI
SFTVDGPIAF VGLSNNINGK HLRVIQKLTY ESGFLNYSKF EVESKVESQH VGSSILTANG
RALLKDAKAE MTGEHNANLN GKVIGTLKNS LFFSAQPFEI TASTNNEGNL KVGFPLKLTG
KIDFLNNYAL FLSPRAQQAS WQASTRFNQY KYNQNFSAIN NEHNIEASIG MNGDANLDFL
NIPLTIPEIN LPYTEFKTPL LKDFSIWEET GLKEFLKTTK QSFDLSVKAQ YKKNSDKHSI
VVPLGMFYEF ILNNVNSWDR KFEKVRNNAL HFLTTSYNEA KIKVDKYKTE NSLNQPSGTF
QNHGYTIPVV NIEVSPFAVE TLASSHVIPT AISTPSVTIP GPNIMVPSYK LVLPPLELPV
FHGPGNLFKF FLPDFKGFNT IDNIYIPAMG NFTYDFSFKS SVITLNTNAG LYNQSDIVAH
FLSSSSFVTD ALQYKLEGTS RLMRKRGLKL ATAVSLTNKF VKGSHDSTIS LTKKNMEASV
RTTANLHAPI FSMNFKQELN GNTKSKPTVS SSIELNYDFN SSKLHSTATG GIDHKFSLES
LTSYFSIESF TKGNIKSSFL SQEYSGSVAN EANVYLNSKG TRSSVRLQGA SKVDGIWNVE
VGENFAGEAT LQRIYTTWEH NMKNHLQVYS YFFTKGKQTC RATLELSPWT MSTLLQVHVS
QLSSLLDLHH FDQEVILKAN TKNQKISWKG GVQVESRVLQ HNAQFSNDQE EIRLDLAGSL
DGQLWDLEAI FLPVYGKSLQ ELLQMDGKRQ YLQASTSLLY TKNPNGYLLS LPVQELADRF
IIPGIKLNDF SGVKIYKKLS TSPFALNLTM LPKVKFPGID LLTQYSTPEG SSVPIFEATI
PEIHLTVSQF TLPKSLPVGN TVFDLNKLAN MIADVDLPSV TLPEQTIVIP PLEFSVPAGI
FIPFFGELTA RAGMASPLYN VTWSAGWKTK ADHVETFLDS MCTSTLQFLE YALKVVETHK
IEEDLLTYNI KGTLQHCDFN VEYNEDGLFK GLWDWQGEAH LDITSPALTD FHLYYKEDKT
SLSASAASST IGTVGLDSST DDQSVELNVY FHPQSPPEKK LSIFKTEWRY KESDGERYIK
INWEEEAASR LLGSLKSNVP KASKAIYDYA NKYHLEYVSS ELRKSLQVNA EHARRMVDEM
NMSFQRVARD TYQNLYEEML AQKSLSIPEN LKKRVLDSIV HVTQKYHMAV MWLMDSFIHF
LKFNRVQFPG YAGTYTVDEL YTIVMKETKK SLSQLFNGLG NLLSYVQNQV EKSRLINDIT
FKCPFFSKPC KLKDLILIFR EELNILSNIG QQDIKFTTIL SSLQGFLERV LDIIEEQIKC
LKDNESTCVA DHINMVFKIQ VPYAFKSLRE DIYFVLGEFN DFLQSILQEG SYKLQQVHQY
MKALREEYFD PSMVGWTVKY YEIEENMVEL IKTLLVSFRD VYSEYSVTAA DFASKMSTQV
EQFVSRDIRE YLSMLTDING KWMEKIAELS IVAKETMKSW VTAVAKIMSD YPQQFHSNLQ
DFSDQLSSYY EKFVGESTRL IDLSIQNYHV FLRYITELLR KLQVATANNV SPYIKLAQGE
LMITF
