FKBP8_MOUSE
ID FKBP8_MOUSE Reviewed; 402 AA.
AC O35465; Q3UK86; Q6GTX9; Q811M7; Q811R4; Q8C2F0; Q99L93;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8;
DE Short=PPIase FKBP8;
DE EC=5.2.1.8;
DE AltName: Full=38 kDa FK506-binding protein;
DE Short=38 kDa FKBP;
DE Short=FKBP-38;
DE Short=mFKBP38;
DE AltName: Full=FK506-binding protein 8;
DE Short=FKBP-8;
DE AltName: Full=FKBPR38;
DE AltName: Full=Rotamase;
GN Name=Fkbp8; Synonyms=Fkbp38, Sam11;
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] (ISOFORM 1), AND INTERACTION WITH BCL2 AND
RP BCL2L1/BCLXL.
RX PubMed=12510191; DOI=10.1038/ncb894;
RA Shirane M., Nakayama K.I.;
RT "Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and
RT inhibits apoptosis.";
RL Nat. Cell Biol. 5:28-37(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15105374; DOI=10.1242/dev.01122;
RA Bulgakov O.V., Eggenschwiler J.T., Hong D.-H., Anderson K.V., Li T.;
RT "FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural
RT tissues.";
RL Development 131:2149-2159(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow macrophage, Placenta, Spleen, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 39-402 (ISOFORM 1), SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=10197430;
RX DOI=10.1002/(sici)1522-2683(19990201)20:2<249::aid-elps249>3.0.co;2-f;
RA Pedersen K.M., Finsen B., Celis J.E., Jensen N.A.;
RT "muFKBP38: a novel murine immunophilin homolog differentially expressed in
RT Schwannoma cells and central nervous system neurons in vivo.";
RL Electrophoresis 20:249-255(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-402, SEQUENCE REVISION TO 100 AND
RP 400, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=14667822; DOI=10.1016/j.ygeno.2003.07.001;
RA Nielsen J.V., Mitchelmore C., Pedersen K.M., Kjaerulff K.M., Finsen B.,
RA Jensen N.A.;
RT "Fkbp8: novel isoforms, genomic organization, and characterization of a
RT forebrain promoter in transgenic mice.";
RL Genomics 83:181-192(2004).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=18459960; DOI=10.1111/j.1365-2443.2008.01194.x;
RA Shirane M., Ogawa M., Motoyama J., Nakayama K.I.;
RT "Regulation of apoptosis and neurite extension by FKBP38 is required for
RT neural tube formation in the mouse.";
RL Genes Cells 13:635-651(2008).
RN [8]
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: Constitutively inactive PPiase, which becomes active when
CC bound to calmodulin and calcium. Seems to act as a chaperone for BCL2,
CC targets it to the mitochondria and modulates its phosphorylation state.
CC The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the
CC binding of BCL2 to its targets. The active form of FKBP8 may therefore
CC play a role in the regulation of apoptosis (By similarity). Required
CC for normal embryonic development. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homomultimers or heteromultimers (Potential). Forms
CC heterodimer with calmodulin. When activated by calmodulin and calcium,
CC interacts with the BH4 domain of BCL2 and weakly with BCLX isoform Bcl-
CC X(L). Does not bind and inhibit calcineurin (By similarity). Interacts
CC with ZFYVE27; may negatively regulate ZFYVE27 phosphorylation (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:15105374}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15105374}; Cytoplasmic side
CC {ECO:0000269|PubMed:15105374}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35465-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35465-2; Sequence=VSP_034487;
CC -!- TISSUE SPECIFICITY: Detected throughout the embryonic body, in caudal
CC neural tube, limbs and head. Detected in adult retina, brain, heart,
CC kidney, liver, pancreas, lung, testis and urinary bladder (at protein
CC level). Detected in adult brain, kidney, liver, testis and trigeminal
CC nerve, and in embryo. Detected at lower levels in lung, spleen, heart
CC and ovary. Widely expressed in forebrain. Detected in the Purkinje cell
CC layer in the cerebellum and in hippocampus neurons.
CC {ECO:0000269|PubMed:10197430, ECO:0000269|PubMed:14667822,
CC ECO:0000269|PubMed:15105374}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q14318}.
CC -!- DISRUPTION PHENOTYPE: Mice die shortly after birth. They display neural
CC tube and skeletal defects. The neuroepithelium is disorganized and the
CC formation of dorsal root ganglia is defective, likely as a result of an
CC increased frequency of apoptosis and aberrant migration of neuronal
CC cells. The extension of nerve fibers in the spinal cord is also
CC abnormal. {ECO:0000269|PubMed:18459960}.
CC -!- MISCELLANEOUS: Binds the immunosuppressant FK506 only in its
CC calmodulin/calcium activated form. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH03739.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH27808.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAO27795.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC40541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE26916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE31027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE38118.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE39713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AY225340; AAO39021.1; -; mRNA.
DR EMBL; AY278608; AAQ84562.1; -; mRNA.
DR EMBL; AK088739; BAC40541.1; ALT_INIT; mRNA.
DR EMBL; AK146122; BAE26916.1; ALT_INIT; mRNA.
DR EMBL; AK152198; BAE31027.1; ALT_INIT; mRNA.
DR EMBL; AK165281; BAE38118.1; ALT_INIT; mRNA.
DR EMBL; AK167663; BAE39713.1; ALT_INIT; mRNA.
DR EMBL; BC003739; AAH03739.1; ALT_INIT; mRNA.
DR EMBL; BC027808; AAH27808.1; ALT_INIT; mRNA.
DR EMBL; AF030635; AAB86422.1; ALT_INIT; mRNA.
DR EMBL; AY187231; AAO27795.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS52575.1; -. [O35465-2]
DR CCDS; CCDS52576.1; -. [O35465-1]
DR RefSeq; NP_001104536.1; NM_001111066.1. [O35465-2]
DR RefSeq; NP_001186560.1; NM_001199631.1. [O35465-2]
DR RefSeq; NP_034353.2; NM_010223.2. [O35465-1]
DR RefSeq; XP_006509619.1; XM_006509556.2. [O35465-2]
DR RefSeq; XP_017168056.1; XM_017312567.1. [O35465-1]
DR RefSeq; XP_017168057.1; XM_017312568.1. [O35465-1]
DR AlphaFoldDB; O35465; -.
DR SMR; O35465; -.
DR BioGRID; 199689; 5.
DR IntAct; O35465; 2.
DR MINT; O35465; -.
DR STRING; 10090.ENSMUSP00000114069; -.
DR iPTMnet; O35465; -.
DR PhosphoSitePlus; O35465; -.
DR SwissPalm; O35465; -.
DR EPD; O35465; -.
DR jPOST; O35465; -.
DR MaxQB; O35465; -.
DR PaxDb; O35465; -.
DR PeptideAtlas; O35465; -.
DR PRIDE; O35465; -.
DR ProteomicsDB; 272922; -. [O35465-1]
DR ProteomicsDB; 272923; -. [O35465-2]
DR Antibodypedia; 28073; 414 antibodies from 34 providers.
DR DNASU; 14232; -.
DR Ensembl; ENSMUST00000075491; ENSMUSP00000074935; ENSMUSG00000019428. [O35465-2]
DR Ensembl; ENSMUST00000119353; ENSMUSP00000112527; ENSMUSG00000019428. [O35465-1]
DR Ensembl; ENSMUST00000119698; ENSMUSP00000114069; ENSMUSG00000019428. [O35465-2]
DR GeneID; 14232; -.
DR KEGG; mmu:14232; -.
DR UCSC; uc009mao.2; mouse. [O35465-2]
DR UCSC; uc009map.2; mouse. [O35465-1]
DR CTD; 23770; -.
DR MGI; MGI:1341070; Fkbp8.
DR VEuPathDB; HostDB:ENSMUSG00000019428; -.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000156705; -.
DR HOGENOM; CLU_013615_1_3_1; -.
DR InParanoid; O35465; -.
DR OMA; RRDQHNE; -.
DR OrthoDB; 787673at2759; -.
DR TreeFam; TF105295; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 14232; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fkbp8; mouse.
DR PRO; PR:O35465; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35465; protein.
DR Bgee; ENSMUSG00000019428; Expressed in embryonic brain and 257 other tissues.
DR ExpressionAtlas; O35465; baseline and differential.
DR Genevisible; O35465; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0048665; P:neuron fate specification; IMP:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0006457; P:protein folding; IMP:MGI.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Calcium; Isomerase; Isopeptide bond;
KW Membrane; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW Rotamase; TPR repeat; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..402
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP8"
FT /id="PRO_0000075332"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 110..194
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 211..244
FT /note="TPR 1"
FT REPEAT 262..295
FT /note="TPR 2"
FT REPEAT 296..329
FT /note="TPR 3"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 341
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q14318"
FT VAR_SEQ 173
FT /note="G -> GS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034487"
FT CONFLICT 100
FT /note="G -> C (in Ref. 1; AAO39021, 2; AAQ84562, 4;
FT AAH03739 and 5; AAB86422)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> T (in Ref. 3; BAE26916)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> A (in Ref. 3; BAC40541)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="A -> G (in Ref. 1; AAO39021, 2; AAQ84562, 4;
FT AAH03739 and 5; AAB86422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 43529 MW; 609A954FAD3A76F8 CRC64;
MASWAEPSEP AALRLPGAPL LEGFEVLDGV DDAEEEDDLS GLPPLEDMGQ PTVEEAEQPG
ALAREFLAAT EPEPAPAPAP EEWLDILGNG LLRMKTLVPG PKGSSRPLKG QVVTVHLQMS
LENGTRVQEE PELAFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG PQGRSPYIPP
HAALCLEVTL KTAEDGPDLE MLSGQERVAL ANRKRECGNA HYQRADFVLA ANSYDLAIKA
ITSNTKVDMT CEEEEELLQL KVKCLNNLAA SQLKLDHYRA ALRSCSQVLE HQPDNIKALF
RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKRAAQRSTE TALYRKMLGN
PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN
