SEZ6_MOUSE
ID SEZ6_MOUSE Reviewed; 991 AA.
AC Q7TSK2; Q3TT53; Q62223; Q62224; Q62269; Q7TPC9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Seizure protein 6;
DE Short=SEZ-6;
DE AltName: Full=Brain-specific receptor-like protein C;
DE Short=BSRP-C;
DE Flags: Precursor;
GN Name=Sez6; Synonyms=Kiaa4158;
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] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7488116; DOI=10.1006/bbrc.1995.2635;
RA Shimizu-Nishikawa K., Kajiwara K., Sugaya E.;
RT "Cloning and characterization of seizure-related gene, SEZ-6.";
RL Biochem. Biophys. Res. Commun. 216:382-389(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=7723619; DOI=10.1016/0169-328x(94)00203-q;
RA Shimizu-Nishikawa K., Kajiwara K., Kimura M., Katsuki M., Sugaya E.;
RT "Cloning and expression of SEZ-6, a brain-specific and seizure-related
RT cDNA.";
RL Brain Res. Mol. Brain Res. 28:201-210(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16814779; DOI=10.1016/j.febslet.2006.06.043;
RA Miyazaki T., Hashimoto K., Uda A., Sakagami H., Nakamura Y., Saito S.Y.,
RA Nishi M., Kume H., Tohgo A., Kaneko I., Kondo H., Fukunaga K., Kano M.,
RA Watanabe M., Takeshima H.;
RT "Disturbance of cerebellar synaptic maturation in mutant mice lacking
RT BSRPs, a novel brain-specific receptor-like protein family.";
RL FEBS Lett. 580:4057-4064(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-991 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=12351182; DOI=10.1016/s0925-4773(02)00238-1;
RA Kim M.H., Gunnersen J.M., Tan S.S.;
RT "Localized expression of the seizure-related gene SEZ-6 in developing and
RT adult forebrains.";
RL Mech. Dev. 118:171-174(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=18031681; DOI=10.1016/j.neuron.2007.09.018;
RA Gunnersen J.M., Kim M.H., Fuller S.J., De Silva M., Britto J.M.,
RA Hammond V.E., Davies P.J., Petrou S., Faber E.S., Sah P., Tan S.-S.;
RT "Sez-6 proteins affect dendritic arborization patterns and excitability of
RT cortical pyramidal neurons.";
RL Neuron 56:621-639(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: May play a role in cell-cell recognition and in neuronal
CC membrane signaling. Seems to be important for the achievement of the
CC necessary balance between dendrite elongation and branching during the
CC elaboration of a complex dendritic arbor. Involved in the development
CC of appropriate excitatory synaptic connectivity.
CC {ECO:0000269|PubMed:18031681}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein. Cell projection, dendrite. Note=Localized on
CC dendrites and in the postsynaptic fraction. Does not appear to be
CC enriched at synapses, at least not in the presynaptic axon terminal.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein. Synapse. Cell projection, dendrite. Note=Localized on
CC dendrites and in the synaptic and postsynaptic fraction.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Type 2;
CC IsoId=Q7TSK2-1; Sequence=Displayed;
CC Name=2; Synonyms=Type 1;
CC IsoId=Q7TSK2-2; Sequence=VSP_034256, VSP_034257;
CC Name=3; Synonyms=Type 3;
CC IsoId=Q7TSK2-3; Sequence=VSP_034254, VSP_034255;
CC -!- TISSUE SPECIFICITY: Brain-specific. Expressed in extrasynaptic and
CC synaptic subcellular fractions (at protein level). Expression
CC correlates with the most active periods of cortical neurogenesis and
CC neuronal maturation. Expression is restricted to the gray matter with
CC higher levels in the forebrain including the olfactory bulb, anterior
CC olfactory nuclei, olfactory tubercle, striatum, hippocampal CA1
CC pyramidal cell layer and cerebral cortex. Expression is up-regulated
CC with the convulsant drug, pentylenetetrazole.
CC {ECO:0000269|PubMed:16814779, ECO:0000269|PubMed:7488116,
CC ECO:0000269|PubMed:7723619}.
CC -!- DEVELOPMENTAL STAGE: At 11.5 dpc, expression is localized to the
CC preplate and is absent from the ventricular zone which is the most
CC prominent layer during early cortical development. At 13 dpc highly
CC expressed in postmitotic, maturing neurons of the developing cortical
CC plate and subplate. At 15 dpc expression is closely tied with the
CC emergence of the neocortical layers and hippocampus. In the cortex,
CC expression diminishes after birth, but continues in the deep layer
CC pyramidal neurons and neuronal subpopulations of layer II/III. In the
CC hippocampus, expression persists in CA1 pyramidal neurons and in the
CC dentate gyrus. Postnatally, expression remains high in specific
CC cortical neuron populations, particularly those of the deep cortical
CC layers. {ECO:0000269|PubMed:12351182, ECO:0000269|PubMed:18031681}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:7488116}.
CC -!- DISRUPTION PHENOTYPE: Mice show reduced exploratory behavior and motor
CC coordination, altered maze performance, and poorer memory retention.
CC Molecular, morphological, and electrophysiological evidence of defects
CC in dendritic arbor patterning was also seen. Secreted and membrane-
CC bound isoforms in null mutants exerted opposite actions. The secreted
CC isoform showed an increased neurite number, while, the membrane-bound
CC isoform displayed a decrease in dendritic arborization. Embryos were
CC viable, fertile and normal in other respects. Mice lacking Sez6,
CC Sez6l1, Sez6l2 exhibited motor discordination, and Purkinje cells were
CC often innervated by multiple climbing fibers with different neuronal
CC origins in the cerebellum. {ECO:0000269|PubMed:16814779,
CC ECO:0000269|PubMed:18031681}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D64009; BAA10889.1; -; mRNA.
DR EMBL; D64010; BAA10890.1; -; mRNA.
DR EMBL; D29763; BAA06167.1; -; mRNA.
DR EMBL; AB206791; BAE44444.1; -; mRNA.
DR EMBL; AL591065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053011; AAH53011.1; -; mRNA.
DR EMBL; BC055345; AAH55345.1; -; mRNA.
DR EMBL; AK161576; BAE36472.1; ALT_INIT; mRNA.
DR CCDS; CCDS25087.1; -. [Q7TSK2-1]
DR CCDS; CCDS70255.1; -. [Q7TSK2-2]
DR PIR; I52657; I52657.
DR RefSeq; NP_001278154.1; NM_001291225.1. [Q7TSK2-2]
DR RefSeq; NP_067261.2; NM_021286.4. [Q7TSK2-1]
DR RefSeq; XP_006532703.1; XM_006532640.2.
DR AlphaFoldDB; Q7TSK2; -.
DR SMR; Q7TSK2; -.
DR STRING; 10090.ENSMUSP00000091532; -.
DR GlyConnect; 2693; 1 N-Linked glycan (1 site).
DR GlyGen; Q7TSK2; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q7TSK2; -.
DR PhosphoSitePlus; Q7TSK2; -.
DR MaxQB; Q7TSK2; -.
DR PaxDb; Q7TSK2; -.
DR PRIDE; Q7TSK2; -.
DR ProteomicsDB; 256626; -. [Q7TSK2-1]
DR ProteomicsDB; 256627; -. [Q7TSK2-2]
DR ProteomicsDB; 256628; -. [Q7TSK2-3]
DR Antibodypedia; 2178; 41 antibodies from 14 providers.
DR DNASU; 20370; -.
DR Ensembl; ENSMUST00000000646; ENSMUSP00000000646; ENSMUSG00000000632. [Q7TSK2-2]
DR Ensembl; ENSMUST00000093995; ENSMUSP00000091532; ENSMUSG00000000632. [Q7TSK2-1]
DR GeneID; 20370; -.
DR KEGG; mmu:20370; -.
DR UCSC; uc007khn.2; mouse. [Q7TSK2-3]
DR UCSC; uc007kho.2; mouse. [Q7TSK2-2]
DR UCSC; uc007khp.2; mouse. [Q7TSK2-1]
DR CTD; 124925; -.
DR MGI; MGI:104745; Sez6.
DR VEuPathDB; HostDB:ENSMUSG00000000632; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156995; -.
DR HOGENOM; CLU_011474_2_0_1; -.
DR InParanoid; Q7TSK2; -.
DR OMA; GPAPCNR; -.
DR OrthoDB; 126806at2759; -.
DR PhylomeDB; Q7TSK2; -.
DR TreeFam; TF330037; -.
DR BioGRID-ORCS; 20370; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Sez6; mouse.
DR PRO; PR:Q7TSK2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TSK2; protein.
DR Bgee; ENSMUSG00000000632; Expressed in cortical plate and 114 other tissues.
DR ExpressionAtlas; Q7TSK2; baseline and differential.
DR Genevisible; Q7TSK2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IGI:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:MGI.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IGI:MGI.
DR GO; GO:0060074; P:synapse maturation; IGI:MGI.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 3.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00042; CUB; 3.
DR SUPFAM; SSF49854; SSF49854; 3.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50923; SUSHI; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Sushi; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..991
FT /note="Seizure protein 6"
FT /id="PRO_0000341348"
FT TOPO_DOM 20..922
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 241..353
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 352..411
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 413..524
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 527..588
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 590..701
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 705..764
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 766..829
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 833..894
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 79..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 241..268
FT /evidence="ECO:0000250"
FT DISULFID 354..394
FT /evidence="ECO:0000250"
FT DISULFID 380..409
FT /evidence="ECO:0000250"
FT DISULFID 413..440
FT /evidence="ECO:0000250"
FT DISULFID 529..571
FT /evidence="ECO:0000250"
FT DISULFID 556..586
FT /evidence="ECO:0000250"
FT DISULFID 590..616
FT /evidence="ECO:0000250"
FT DISULFID 707..749
FT /evidence="ECO:0000250"
FT DISULFID 735..762
FT /evidence="ECO:0000250"
FT DISULFID 768..810
FT /evidence="ECO:0000250"
FT DISULFID 796..827
FT /evidence="ECO:0000250"
FT DISULFID 835..877
FT /evidence="ECO:0000250"
FT DISULFID 863..892
FT /evidence="ECO:0000250"
FT VAR_SEQ 588..605
FT /note="AVCSGEITDSAGVVLSPN -> GQQAPVGGSARATSRVGP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7488116"
FT /id="VSP_034254"
FT VAR_SEQ 606..991
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7488116"
FT /id="VSP_034255"
FT VAR_SEQ 895..907
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7723619"
FT /id="VSP_034256"
FT VAR_SEQ 982..991
FT /note="SLSFAGDERI -> ETREYEVSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7723619"
FT /id="VSP_034257"
FT CONFLICT 216
FT /note="A -> G (in Ref. 1; BAA10889/BAA10890, 2; BAA06167
FT and 3; BAE44444)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> P (in Ref. 1; BAA10889/BAA10890, 2; BAA06167
FT and 3; BAE44444)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="G -> R (in Ref. 1; BAA10889/BAA10890, 2; BAA06167
FT and 3; BAE44444)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="D -> N (in Ref. 1; BAA10889, 2; BAA06167 and 3;
FT BAE44444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 107433 MW; 4B3DAA14AD2A29F3 CRC64;
MRPAALLLLP SLLALLAHGL SSEAPITGEG HATGIRETDG ELTAAPTPEQ SDRGVHFVTT
APTLKLLNHH PLLEEFLQEG LEREEAPQPA LPFQPDSPTH FTPSPLPRLT NQDNRPVFTS
PTPAVAAAPT QPHSREKPWN LESKPPELSI TSSLPPGPSM AVPTLLPEDR PSTTPPSQAW
TPTQEGPGDM DRPWVPEVMS KTTGLGVEGT IATSTASGDD EETTTTIITT TVTTVQPPGP
CSWNFSGPEG SLDSPTAPSS PSDVGLDCFY YISVYPGYGV EIKVENISLQ EGETITVEGL
GGPDPLPLAN QSFLLRGQVI RSPTHQAALR FQSLPLPAGP GTFHFRYQAY LLSCHFPRRP
AYGDVTVTSL HPGGSAHFHC ATGYQLKGAR FLTCLNATQP FWDSQEPVCI AACGGVIRNA
TTGRIVSPGF PGNYSNNLTC HWLLEAPESQ RLHLHFEKVS LAEDDDRLII RNGNNVEAPP
VYDSYEVEYL PIEGLLSSGR HFFVEFSTDS SGAAAGMALR YEAFQQGHCY EPFVKYGNFS
SSAPSYPVGT TVEFSCDPGY TLEQGSIIIE CVDLHDPQWN ETEPACRAVC SGEITDSAGV
VLSPNWPEPY GRGQDCIWGV HVEEDKRIML DIRVLRIGSG DVLTFYDGDD LTARVLGQYS
GPRGHFKLFT SMADVTIQFQ SDPGTSALGY QQGFVIHFFE VPRNDTCPEL PEIPNGWKNP
SQPELVHGTV VTYQCYPGYQ VVGSSILMCQ WDLSWSEDLP SCQRVTSCHD PGDVEHSRRL
ISSPKFPVGA TVQYVCDQGF VLTGSAILTC HDRQAGSPKW SDRAPKCLLE QFKPCHGLSA
PENGARSPEK RLHPAGATIH FSCAPGYVLK GQASIKCVPG HPSHWSDPPP ICRAASLDGF
YNGRSLDVAK APAASSALDA AHLAAAIFLP LVAMVLLVGG VYLYFSRFQG KSPLQLPRTH
PRPYNRITVE SAFDNPTYET GSLSFAGDER I
