PDIA3_MOUSE
ID PDIA3_MOUSE Reviewed; 505 AA.
AC P27773; Q3TEI9; Q3TIL2; Q3UZK8; Q8C2F4; Q99LF6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Protein disulfide-isomerase A3;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P30101};
DE AltName: Full=58 kDa glucose-regulated protein;
DE AltName: Full=58 kDa microsomal protein;
DE Short=p58;
DE AltName: Full=Disulfide isomerase ER-60;
DE AltName: Full=Endoplasmic reticulum resident protein 57;
DE Short=ER protein 57;
DE Short=ERp57;
DE AltName: Full=Endoplasmic reticulum resident protein 60;
DE Short=ER protein 60;
DE Short=ERp60;
DE Flags: Precursor;
GN Name=Pdia3; Synonyms=Erp, Erp60, Grp58;
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].
RX PubMed=2033248;
RA Hempel W.M., Defranco A.L.;
RT "Expression of phospholipase C isozymes by murine B lymphocytes.";
RL J. Immunol. 146:3713-3720(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA Wang W., Jaiswal A.K.;
RT "Mouse GRP58 gene structure.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=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 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].
RC STRAIN=Czech II, and 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 [6]
RP PROTEIN SEQUENCE OF 25-41 AND 306-329.
RC TISSUE=Fibroblast;
RX PubMed=7523108; DOI=10.1002/elps.11501501101;
RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT "Separation and sequencing of familiar and novel murine proteins using
RT preparative two-dimensional gel electrophoresis.";
RL Electrophoresis 15:735-745(1994).
RN [7]
RP PROTEIN SEQUENCE OF 25-41, AND PHOSPHORYLATION.
RC TISSUE=Fibroblast;
RA Merrick B.A., Wichter L.L., Patterson R.M., He C., Selkirk J.K.;
RT "Identification of the two isoforms of phospholipase C-alpha from dividing
RT murine fibroblasts by protein microsequencing.";
RL Biochem. Arch. 9:335-340(1993).
RN [8]
RP PROTEIN SEQUENCE OF 63-73; 94-103; 119-128; 130-139; 147-172; 183-193;
RP 195-214; 234-251; 258-270; 306-329; 335-343; 347-362; 366-378; 448-459 AND
RP 472-495, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
RN [10]
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).
RN [11]
RP INTERACTION WITH MZB1.
RX PubMed=21093319; DOI=10.1016/j.immuni.2010.11.013;
RA Flach H., Rosenbaum M., Duchniewicz M., Kim S., Zhang S.L., Cahalan M.D.,
RA Mittler G., Grosschedl R.;
RT "Mzb1 protein regulates calcium homeostasis, antibody secretion, and
RT integrin activation in innate-like B cells.";
RL Immunity 33:723-735(2010).
RN [12]
RP INTERACTION WITH ATP2A2.
RX PubMed=23395171; DOI=10.1016/j.cmet.2013.01.002;
RA Kim H., Kim T., Jeong B.C., Cho I.T., Han D., Takegahara N.,
RA Negishi-Koga T., Takayanagi H., Lee J.H., Sul J.Y., Prasad V., Lee S.H.,
RA Choi Y.;
RT "Tmem64 modulates calcium signaling during RANKL-mediated osteoclast
RT differentiation.";
RL Cell Metab. 17:249-260(2013).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152; LYS-252; LYS-362 AND
RP LYS-494, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-129 AND LYS-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Disulfide isomerase which catalyzes the formation,
CC isomerization, and reduction or oxidation of disulfide bonds (By
CC similarity). Associates with calcitriol, the active form of vitamin D3
CC which mediates the action of this vitamin on cells (By similarity).
CC Association with calcitriol does not affect its enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P30101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P30101};
CC -!- SUBUNIT: Subunit of the TAP complex, also known as the peptide loading
CC complex (PLC). Can form disulfide-linked heterodimers with TAPBP.
CC Interacts with ERP27 and CANX (By similarity). Interacts with MZB1 in a
CC calcium-dependent manner. Interacts with SERPINA2 and with the S and Z
CC variants of SERPINA1 (By similarity). Interacts with ATP2A2
CC (PubMed:23395171). {ECO:0000250|UniProtKB:P30101,
CC ECO:0000269|PubMed:23395171}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen
CC {ECO:0000250}. Melanosome {ECO:0000250|UniProtKB:P30101}.
CC -!- TISSUE SPECIFICITY: In caput and cauda epididymal spermatozoa, detected
CC in the acrosome and principal piece (at protein level).
CC {ECO:0000269|PubMed:20400973}.
CC -!- PTM: Phosphorylated. {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a phosphatidylinositol 4,5-
CC bisphosphate phosphodiesterase type I (phospholipase C-alpha).
CC {ECO:0000305|PubMed:2033248}.
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DR EMBL; M73329; AAA39944.1; -; mRNA.
DR EMBL; DQ000491; AAY16987.1; -; Genomic_DNA.
DR EMBL; AK088721; BAC40527.1; -; mRNA.
DR EMBL; AK133799; BAE21849.1; -; mRNA.
DR EMBL; AK167807; BAE39834.1; -; mRNA.
DR EMBL; AK169611; BAE41259.1; -; mRNA.
DR EMBL; AL845466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003285; AAH03285.1; -; mRNA.
DR EMBL; BC033439; AAH33439.1; -; mRNA.
DR CCDS; CCDS16643.1; -.
DR RefSeq; NP_031978.2; NM_007952.2.
DR AlphaFoldDB; P27773; -.
DR SMR; P27773; -.
DR BioGRID; 200077; 38.
DR ComplexPortal; CPX-531; Tapasin-ERp57 complex.
DR IntAct; P27773; 4.
DR MINT; P27773; -.
DR STRING; 10090.ENSMUSP00000028683; -.
DR iPTMnet; P27773; -.
DR PhosphoSitePlus; P27773; -.
DR SwissPalm; P27773; -.
DR REPRODUCTION-2DPAGE; IPI00230108; -.
DR REPRODUCTION-2DPAGE; P27773; -.
DR REPRODUCTION-2DPAGE; Q3TEI9; -.
DR REPRODUCTION-2DPAGE; Q8C2F4; -.
DR SWISS-2DPAGE; P27773; -.
DR EPD; P27773; -.
DR jPOST; P27773; -.
DR MaxQB; P27773; -.
DR PaxDb; P27773; -.
DR PeptideAtlas; P27773; -.
DR PRIDE; P27773; -.
DR ProteomicsDB; 288080; -.
DR TopDownProteomics; P27773; -.
DR Antibodypedia; 1223; 955 antibodies from 46 providers.
DR DNASU; 14827; -.
DR Ensembl; ENSMUST00000028683; ENSMUSP00000028683; ENSMUSG00000027248.
DR GeneID; 14827; -.
DR KEGG; mmu:14827; -.
DR UCSC; uc008lzb.1; mouse.
DR CTD; 2923; -.
DR MGI; MGI:95834; Pdia3.
DR VEuPathDB; HostDB:ENSMUSG00000027248; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000155425; -.
DR HOGENOM; CLU_025879_6_0_1; -.
DR InParanoid; P27773; -.
DR OMA; YIAKHAT; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; P27773; -.
DR TreeFam; TF106382; -.
DR BRENDA; 5.3.4.1; 3474.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-901042; Calnexin/calreticulin cycle.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 14827; 14 hits in 76 CRISPR screens.
DR ChiTaRS; Pdia3; mouse.
DR PRO; PR:P27773; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P27773; protein.
DR Bgee; ENSMUSG00000027248; Expressed in seminal vesicle and 251 other tissues.
DR ExpressionAtlas; P27773; baseline and differential.
DR Genevisible; P27773; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042825; C:TAP complex; ISO:MGI.
DR GO; GO:0061779; C:Tapasin-ERp57 complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0071305; P:cellular response to vitamin D; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:1903334; P:positive regulation of protein folding; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd03069; PDI_b_ERp57; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR041868; PDIA3_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Isomerase; Methylation; Phosphoprotein;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:7523108, ECO:0000269|Ref.7"
FT CHAIN 25..505
FT /note="Protein disulfide-isomerase A3"
FT /id="PRO_0000034226"
FT DOMAIN 25..133
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 343..485
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 502..505
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 407
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 408
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 471
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30101"
FT MOD_RES 129
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 218
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30101"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 57
FT /note="Interchain (with C-118 in TAPBP); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 85..92
FT /evidence="ECO:0000250"
FT DISULFID 406..409
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 20
FT /note="R -> C (in Ref. 3; BAC40527/BAE41259)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Missing (in Ref. 1; AAA39944)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="D -> A (in Ref. 1; AAA39944)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> A (in Ref. 1; AAA39944)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="Y -> F (in Ref. 3; BAE39834)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="G -> S (in Ref. 1; AAA39944)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="D -> G (in Ref. 3; BAE39834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56678 MW; 3A7CD1C35981C4B3 CRC64;
MRFSCLALLP GVALLLASAR LAAASDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT
ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD
NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI
FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA
VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN
LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG
EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL
QREATNPPII QEEKPKKKKK AQEDL
